HUMAN:BLM

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	BLM (synonyms: RECQ2, RECQL3)
Protein Name(s)	Bloom syndrome protein DNA helicase, RecQ-like type 2 RecQ2 RecQ protein-like 3
External Links
UniProt	P54132
EMBL	U39817 AY886902 BC093622 BC101567 BC115030 BC115032
CCDS	CCDS10363.1
PIR	A57570
RefSeq	NP_000048.1 NP_001274175.1 NP_001274176.1 NP_001274177.1
UniGene	Hs.725208
PDB	2KV2 2MH9 2RRD 3WE2 3WE3 4CDG 4CGZ 4O3M
PDBsum	2KV2 2MH9 2RRD 3WE2 3WE3 4CDG 4CGZ 4O3M
ProteinModelPortal	P54132
SMR	P54132
BioGrid	107110
DIP	DIP-33322N
IntAct	P54132
MINT	MINT-131918
STRING	9606.ENSP00000347232
BindingDB	P54132
ChEMBL	CHEMBL1293237
PhosphoSite	P54132
BioMuta	BLM
DMDM	1705486
MaxQB	P54132
PaxDb	P54132
PRIDE	P54132
Ensembl	ENST00000355112
GeneID	641
KEGG	hsa:641
UCSC	uc002bpr.3
CTD	641
GeneCards	GC15P091260
GeneReviews	BLM
HGNC	HGNC:1058
HPA	HPA005689
MIM	210900 604610
neXtProt	NX_P54132
Orphanet	125
PharmGKB	PA25369
eggNOG	COG0514
GeneTree	ENSGT00550000074520
HOGENOM	HOG000095239
HOVERGEN	HBG004850
InParanoid	P54132
KO	K10901
OMA	CENITEC
OrthoDB	EOG72NRPB
PhylomeDB	P54132
TreeFam	TF317801
Reactome	REACT_27271 REACT_355174
EvolutionaryTrace	P54132
GeneWiki	Bloom_syndrome_protein
GenomeRNAi	641
NextBio	2600
PMAP-CutDB	P54132
PRO	PR:P54132
Proteomes	UP000005640
Bgee	P54132
CleanEx	HS_BLM
ExpressionAtlas	P54132
Genevisible	P54132
GO	GO:0005737 GO:0000800 GO:0001673 GO:0000228 GO:0016363 GO:0005730 GO:0005654 GO:0005634 GO:0016605 GO:0045120 GO:0005657 GO:0036310 GO:0005524 GO:0043140 GO:0004003 GO:0008026 GO:0016887 GO:0000405 GO:0009378 GO:0051880 GO:0004386 GO:0002039 GO:0003697 GO:0046632 GO:0044267 GO:0072757 GO:0006974 GO:0072711 GO:0071479 GO:0000729 GO:0032508 GO:0006310 GO:0006281 GO:0000733 GO:0000724 GO:0007095 GO:0051782 GO:0045910 GO:0045950 GO:0070244 GO:0046641 GO:0045893 GO:0043687 GO:0051259 GO:0016925 GO:0051098 GO:0000079 GO:0031297 GO:0048478 GO:0010165 GO:0000723
Gene3D	1.10.10.10 1.10.150.80 3.40.50.300
InterPro	IPR012532 IPR011545 IPR002464 IPR004589 IPR014001 IPR001650 IPR010997 IPR002121 IPR027417 IPR018982 IPR011991
Pfam	PF08072 PF00270 PF00271 PF00570 PF09382
SMART	SM00487 SM00490 SM00341 SM00956
SUPFAM	SSF47819 SSF52540
TIGRFAMs	TIGR00614
PROSITE	PS00690 PS51192 PS51194 PS50967

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005737	cytoplasm		ECO:0000314			C		Source: HPA	Missing: reference
enables	GO:0008270	zinc ion binding	PMID:25901030^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008094	DNA-dependent ATPase activity	PMID:25901030^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004003	ATP-dependent DNA helicase activity	PMID:25901030^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032508	DNA duplex unwinding	PMID:25901030^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032508	DNA duplex unwinding	PMID:24816114^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004003	ATP-dependent DNA helicase activity	PMID:24816114^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008094	DNA-dependent ATPase activity	PMID:24816114^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:24816114^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:24816114^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:24816114^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0061821	telomeric D-loop binding	PMID:19734539^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	part_of:(GO:0061820)	Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:28228481^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051259	protein complex oligomerization	PMID:28228481^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:28228481^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0090329	regulation of DNA-dependent DNA replication	PMID:25901030^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:25901030^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000400	four-way junction DNA binding	PMID:25901030^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0009378	four-way junction helicase activity	PMID:25901030^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0061749	forked DNA-dependent helicase activity	PMID:25901030^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0061820	telomeric D-loop disassembly	PMID:19734539^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_at:(GO:0000781) occurs_at:(SO:0002171)	Seeded From UniProt	complete
enables	GO:1905773	8-hydroxy-2'-deoxyguanosine DNA binding	PMID:19734539^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_at:(GO:0000781) has_input:(CHEBI:40304) part_of:(GO:0061820) occurs_at:(SO:0002171)	Seeded From UniProt	complete
enables	GO:0003678	DNA helicase activity	PMID:19734539^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_at:(GO:0000781) has_input:(CHEBI:40304) part_of:(GO:0061820) occurs_at:(SO:0002171)	Seeded From UniProt	complete
enables	GO:0000403	Y-form DNA binding	PMID:11735402^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0061749	forked DNA-dependent helicase activity	PMID:11735402^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000400	four-way junction DNA binding	PMID:11735402^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000405	bubble DNA binding	PMID:11735402^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	part_of:(GO:0032508)	Seeded From UniProt	complete
involved_in	GO:0032508	DNA duplex unwinding	PMID:11735402^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0009378	four-way junction helicase activity	PMID:11735402^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0051880	G-quadruplex DNA binding	PMID:11735402^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0044806	G-quadruplex DNA unwinding	PMID:11735402^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005657	replication fork	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O88700	C	coincident_with:(SO:0000624)	Seeded From UniProt	complete
involved_in	GO:0044806	G-quadruplex DNA unwinding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O88700	P	occurs_at:(GO:0000781)	Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O88700	P	occurs_at:(GO:0000781)	Seeded From UniProt	complete
enables	GO:0000400	four-way junction DNA binding	PMID:20639533^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0072757	cellular response to camptothecin	PMID:23509288^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0072711	cellular response to hydroxyurea	PMID:23509288^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071479	cellular response to ionizing radiation	PMID:23509288^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051880	G-quadruplex DNA binding	PMID:11433031^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051782	negative regulation of cell division	PMID:11781842^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051259	protein complex oligomerization	PMID:10359700^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048478	replication fork protection	PMID:10779560^[11]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045910	negative regulation of DNA recombination	PMID:9671747^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:11781842^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0036310	annealing helicase activity	PMID:17878217^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0007095	mitotic G2 DNA damage checkpoint	PMID:11309417^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031297	replication fork processing	PMID:17115688^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:17878217^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:10728666^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0016605	PML body	PMID:10779560^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016363	nuclear matrix	PMID:11309417^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010165	response to X-ray	PMID:11309417^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0009378	four-way junction helicase activity	PMID:11433031^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0009378	four-way junction helicase activity	PMID:12818200^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008026	ATP-dependent helicase activity	PMID:12818200^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:12818200^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:23509288^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	PMID:10728666^[16]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	PMID:7585968^[18]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:7585968^[18]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	PMID:10779560^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9388480^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:11500040^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:17878217^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004386	helicase activity	PMID:17878217^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004386	helicase activity	PMID:12181313^[21]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004386	helicase activity	PMID:10871376^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004003	ATP-dependent DNA helicase activity	PMID:21325134^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004003	ATP-dependent DNA helicase activity	PMID:9388193^[24]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:12818200^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:11781842^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04637	F		Seeded From UniProt	complete
part_of	GO:0000800	lateral element	PMID:10728666^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0000781	chromosome, telomeric region	PMID:10779560^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000729	DNA double-strand break processing	PMID:21325134^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:11309417^[14]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000405	bubble DNA binding	PMID:11433031^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000228	nuclear chromosome	PMID:23509288^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000079	regulation of cyclin-dependent protein serine/threonine kinase activity	PMID:15604258^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003697	single-stranded DNA binding	PMID:20639533^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0061849	telomeric G-quadruplex DNA binding	PMID:19734539^[3]	ECO:0000305	curator inference used in manual assertion	GO:0061821,GO:1905773	F		Seeded From UniProt	complete
enables	GO:0043140	ATP-dependent 3'-5' DNA helicase activity	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0002906 FB:FBgn0040290 MGI:MGI:1328362 PANTHER:PTN000344873 PomBase:SPAC2G11.12 UniProtKB:O94761 WB:WBGene00006944	F		Seeded From UniProt	complete
involved_in	GO:0032508	DNA duplex unwinding	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0002906 FB:FBgn0040290 PANTHER:PTN000344873 PomBase:SPAC2G11.12 SGD:S000004802 TAIR:locus:2127998 TAIR:locus:2180255 TAIR:locus:2197555 UniProtKB:O94761 UniProtKB:P54132 UniProtKB:Q14191 UniProtKB:Q8I2W7 UniProtKB:Q9I920	P		Seeded From UniProt	complete
enables	GO:0009378	four-way junction helicase activity	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000344873 TAIR:locus:2127998 TAIR:locus:2197555 UniProtKB:P54132 UniProtKB:Q14191	F		Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10833 PANTHER:PTN000344873 TAIR:locus:2127998 TAIR:locus:2197394 TAIR:locus:2206031	P		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10833 FB:FBgn0002906 MGI:MGI:1328362 PANTHER:PTN000344873 TAIR:locus:2180255 TAIR:locus:2197394 UniProtKB:O94762	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10833 FB:FBgn0040290 MGI:MGI:1328362 PANTHER:PTN000344873	C		Seeded From UniProt	complete
part_of	GO:0005694	chromosome	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000344873 WB:WBGene00006944	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0002906 FB:FBgn0027375 FB:FBgn0040290 MGI:MGI:109635 PANTHER:PTN000749808 UniProtKB:O94762 UniProtKB:P46063 UniProtKB:P54132 WB:WBGene00004322 WB:WBGene00006944	C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10833 PANTHER:PTN000344873 UniProtKB:P54132 UniProtKB:Q14191 UniProtKB:Q9I920	F		Seeded From UniProt	complete
involved_in	GO:0000724	double-strand break repair via homologous recombination	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0002906 PANTHER:PTN000344874 PomBase:SPAC2G11.12 SGD:S000004802 TAIR:locus:2197394	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000733	DNA strand renaturation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0036310	P		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010997	F		Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002121 InterPro:IPR011545	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012532	F		Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010997	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011545 InterPro:IPR012532	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012532	C		Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012532 InterPro:IPR018982	P		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR018982	P		Seeded From UniProt	complete
involved_in	GO:0006310	DNA recombination	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004589	P		Seeded From UniProt	complete
enables	GO:0008026	ATP-dependent helicase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004589	F		Seeded From UniProt	complete
enables	GO:0016818	hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012532	F		Seeded From UniProt	complete
enables	GO:0043140	ATP-dependent 3'-5' DNA helicase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR018982	F		Seeded From UniProt	complete
involved_in	GO:0044237	cellular metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010997	P		Seeded From UniProt	complete
involved_in	GO:0090656	t-circle formation	PMID:27918544^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	part_of:(GO:0090737)	Seeded From UniProt	complete
involved_in	GO:1901796	regulation of signal transduction by p53 class mediator	Reactome:R-HSA-5633007	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	Reactome:R-HSA-5684887 Reactome:R-HSA-5684875	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-6799332 Reactome:R-HSA-5693620 Reactome:R-HSA-5693593 Reactome:R-HSA-5693589 Reactome:R-HSA-5693584 Reactome:R-HSA-5693580 Reactome:R-HSA-5693564 Reactome:R-HSA-5693561 Reactome:R-HSA-5693542 Reactome:R-HSA-5693539 Reactome:R-HSA-5686657 Reactome:R-HSA-5686642 Reactome:R-HSA-5686483 Reactome:R-HSA-5686469 Reactome:R-HSA-5686440 Reactome:R-HSA-5686410 Reactome:R-HSA-5686398 Reactome:R-HSA-5685994 Reactome:R-HSA-5685985 Reactome:R-HSA-5685838 Reactome:R-HSA-5685341 Reactome:R-HSA-5685156 Reactome:R-HSA-5685011 Reactome:R-HSA-5684887 Reactome:R-HSA-5684882 Reactome:R-HSA-5684875 Reactome:R-HSA-4568914	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004386	helicase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0347	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
involved_in	GO:0006260	DNA replication	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0235	P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 ^1.8 Newman, JA et al. (2015) Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes. Nucleic Acids Res. 43 5221-35 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Swan, MK et al. (2014) Structure of human Bloom's syndrome helicase in complex with ADP and duplex DNA. Acta Crystallogr. D Biol. Crystallogr. 70 1465-75 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Ghosh, A et al. (2009) Telomeric D-loops containing 8-oxo-2'-deoxyguanosine are preferred substrates for Werner and Bloom syndrome helicases and are bound by POT1. J. Biol. Chem. 284 31074-84 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Shi, J et al. (2017) A helical bundle in the N-terminal domain of the BLM helicase mediates dimer and potentially hexamer formation. J. Biol. Chem. 292 5909-5920 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Li, JL et al. (2001) Inhibition of the Bloom's and Werner's syndrome helicases by G-quadruplex interacting ligands. Biochemistry 40 15194-202 PubMed GONUTS page
↑ ^6.0 ^6.1 Kim, YM & Choi, BS (2010) Structure and function of the regulatory HRDC domain from human Bloom syndrome protein. Nucleic Acids Res. 38 7764-77 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Wan, L et al. (2013) Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair. Proc. Natl. Acad. Sci. U.S.A. 110 10646-51 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Mohaghegh, P et al. (2001) The Bloom's and Werner's syndrome proteins are DNA structure-specific helicases. Nucleic Acids Res. 29 2843-9 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Garkavtsev, IV et al. (2001) The Bloom syndrome protein interacts and cooperates with p53 in regulation of transcription and cell growth control. Oncogene 20 8276-80 PubMed GONUTS page
↑ Karow, JK et al. (1999) Oligomeric ring structure of the Bloom's syndrome helicase. Curr. Biol. 9 597-600 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Yankiwski, V et al. (2000) Nuclear structure in normal and Bloom syndrome cells. Proc. Natl. Acad. Sci. U.S.A. 97 5214-9 PubMed GONUTS page
↑ Yamagata, K et al. (1998) Bloom's and Werner's syndrome genes suppress hyperrecombination in yeast sgs1 mutant: implication for genomic instability in human diseases. Proc. Natl. Acad. Sci. U.S.A. 95 8733-8 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Guo, RB et al. (2007) Structural and functional analyses of disease-causing missense mutations in Bloom syndrome protein. Nucleic Acids Res. 35 6297-310 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 Bischof, O et al. (2001) Regulation and localization of the Bloom syndrome protein in response to DNA damage. J. Cell Biol. 153 367-80 PubMed GONUTS page
↑ Machwe, A et al. (2006) The Werner and Bloom syndrome proteins catalyze regression of a model replication fork. Biochemistry 45 13939-46 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Johnson, FB et al. (2000) Association of the Bloom syndrome protein with topoisomerase IIIalpha in somatic and meiotic cells. Cancer Res. 60 1162-7 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 Janscak, P et al. (2003) Characterization and mutational analysis of the RecQ core of the bloom syndrome protein. J. Mol. Biol. 330 29-42 PubMed GONUTS page
↑ ^18.0 ^18.1 Ellis, NA et al. (1995) The Bloom's syndrome gene product is homologous to RecQ helicases. Cell 83 655-66 PubMed GONUTS page
↑ Kaneko, H et al. (1997) BLM (the causative gene of Bloom syndrome) protein translocation into the nucleus by a nuclear localization signal. Biochem. Biophys. Res. Commun. 240 348-53 PubMed GONUTS page
↑ Suzuki, H et al. (2001) The N-terminal internal region of BLM is required for the formation of dots/rod-like structures which are associated with SUMO-1. Biochem. Biophys. Res. Commun. 286 322-7 PubMed GONUTS page
↑ Opresko, PL et al. (2002) Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases. J. Biol. Chem. 277 41110-9 PubMed GONUTS page
↑ Brosh, RM Jr et al. (2000) Potent inhibition of werner and bloom helicases by DNA minor groove binding drugs. Nucleic Acids Res. 28 2420-30 PubMed GONUTS page
↑ ^23.0 ^23.1 Nimonkar, AV et al. (2011) BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair. Genes Dev. 25 350-62 PubMed GONUTS page
↑ Karow, JK et al. (1997) The Bloom's syndrome gene product is a 3'-5' DNA helicase. J. Biol. Chem. 272 30611-4 PubMed GONUTS page
↑ Bayart, E et al. (2004) A major role for mitotic CDC2 kinase inactivation in the establishment of the mitotic DNA damage checkpoint. Cancer Res. 64 8954-9 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 ^26.6 ^26.7 ^26.8 ^26.9 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Rivera, T et al. (2017) A balance between elongation and trimming regulates telomere stability in stem cells. Nat. Struct. Mol. Biol. 24 30-39 PubMed GONUTS page

[PMID:25901030-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 ^1.8 Newman, JA et al. (2015) Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes. Nucleic Acids Res. 43 5221-35 PubMed GONUTS page

[PMID:24816114-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Swan, MK et al. (2014) Structure of human Bloom's syndrome helicase in complex with ADP and duplex DNA. Acta Crystallogr. D Biol. Crystallogr. 70 1465-75 PubMed GONUTS page

[PMID:19734539-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Ghosh, A et al. (2009) Telomeric D-loops containing 8-oxo-2'-deoxyguanosine are preferred substrates for Werner and Bloom syndrome helicases and are bound by POT1. J. Biol. Chem. 284 31074-84 PubMed GONUTS page

[PMID:28228481-4] 4.0 ^4.1 ^4.2 Shi, J et al. (2017) A helical bundle in the N-terminal domain of the BLM helicase mediates dimer and potentially hexamer formation. J. Biol. Chem. 292 5909-5920 PubMed GONUTS page

[PMID:11735402-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Li, JL et al. (2001) Inhibition of the Bloom's and Werner's syndrome helicases by G-quadruplex interacting ligands. Biochemistry 40 15194-202 PubMed GONUTS page

[PMID:20639533-6] 6.0 ^6.1 Kim, YM & Choi, BS (2010) Structure and function of the regulatory HRDC domain from human Bloom syndrome protein. Nucleic Acids Res. 38 7764-77 PubMed GONUTS page

[PMID:23509288-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Wan, L et al. (2013) Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair. Proc. Natl. Acad. Sci. U.S.A. 110 10646-51 PubMed GONUTS page

[PMID:11433031-8] 8.0 ^8.1 ^8.2 Mohaghegh, P et al. (2001) The Bloom's and Werner's syndrome proteins are DNA structure-specific helicases. Nucleic Acids Res. 29 2843-9 PubMed GONUTS page

[PMID:11781842-9] 9.0 ^9.1 ^9.2 Garkavtsev, IV et al. (2001) The Bloom syndrome protein interacts and cooperates with p53 in regulation of transcription and cell growth control. Oncogene 20 8276-80 PubMed GONUTS page

[PMID:10359700-10] Karow, JK et al. (1999) Oligomeric ring structure of the Bloom's syndrome helicase. Curr. Biol. 9 597-600 PubMed GONUTS page

[PMID:10779560-11] 11.0 ^11.1 ^11.2 ^11.3 Yankiwski, V et al. (2000) Nuclear structure in normal and Bloom syndrome cells. Proc. Natl. Acad. Sci. U.S.A. 97 5214-9 PubMed GONUTS page

[PMID:9671747-12] Yamagata, K et al. (1998) Bloom's and Werner's syndrome genes suppress hyperrecombination in yeast sgs1 mutant: implication for genomic instability in human diseases. Proc. Natl. Acad. Sci. U.S.A. 95 8733-8 PubMed GONUTS page

[PMID:17878217-13] 13.0 ^13.1 ^13.2 ^13.3 Guo, RB et al. (2007) Structural and functional analyses of disease-causing missense mutations in Bloom syndrome protein. Nucleic Acids Res. 35 6297-310 PubMed GONUTS page

[PMID:11309417-14] 14.0 ^14.1 ^14.2 ^14.3 Bischof, O et al. (2001) Regulation and localization of the Bloom syndrome protein in response to DNA damage. J. Cell Biol. 153 367-80 PubMed GONUTS page

[PMID:17115688-15] Machwe, A et al. (2006) The Werner and Bloom syndrome proteins catalyze regression of a model replication fork. Biochemistry 45 13939-46 PubMed GONUTS page

[PMID:10728666-16] 16.0 ^16.1 ^16.2 Johnson, FB et al. (2000) Association of the Bloom syndrome protein with topoisomerase IIIalpha in somatic and meiotic cells. Cancer Res. 60 1162-7 PubMed GONUTS page

[PMID:12818200-17] 17.0 ^17.1 ^17.2 ^17.3 Janscak, P et al. (2003) Characterization and mutational analysis of the RecQ core of the bloom syndrome protein. J. Mol. Biol. 330 29-42 PubMed GONUTS page

[PMID:7585968-18] 18.0 ^18.1 Ellis, NA et al. (1995) The Bloom's syndrome gene product is homologous to RecQ helicases. Cell 83 655-66 PubMed GONUTS page

[PMID:9388480-19] Kaneko, H et al. (1997) BLM (the causative gene of Bloom syndrome) protein translocation into the nucleus by a nuclear localization signal. Biochem. Biophys. Res. Commun. 240 348-53 PubMed GONUTS page

[PMID:11500040-20] Suzuki, H et al. (2001) The N-terminal internal region of BLM is required for the formation of dots/rod-like structures which are associated with SUMO-1. Biochem. Biophys. Res. Commun. 286 322-7 PubMed GONUTS page

[PMID:12181313-21] Opresko, PL et al. (2002) Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases. J. Biol. Chem. 277 41110-9 PubMed GONUTS page

[PMID:10871376-22] Brosh, RM Jr et al. (2000) Potent inhibition of werner and bloom helicases by DNA minor groove binding drugs. Nucleic Acids Res. 28 2420-30 PubMed GONUTS page

[PMID:21325134-23] 23.0 ^23.1 Nimonkar, AV et al. (2011) BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair. Genes Dev. 25 350-62 PubMed GONUTS page

[PMID:9388193-24] Karow, JK et al. (1997) The Bloom's syndrome gene product is a 3'-5' DNA helicase. J. Biol. Chem. 272 30611-4 PubMed GONUTS page

[PMID:15604258-25] Bayart, E et al. (2004) A major role for mitotic CDC2 kinase inactivation in the establishment of the mitotic DNA damage checkpoint. Cancer Res. 64 8954-9 PubMed GONUTS page

[PMID:21873635-26] 26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 ^26.6 ^26.7 ^26.8 ^26.9 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:27918544-27] Rivera, T et al. (2017) A balance between elongation and trimming regulates telomere stability in stem cells. Nat. Struct. Mol. Biol. 24 30-39 PubMed GONUTS page

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