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HUMAN:SPIR1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) SPIRE1 (ECO:0000312 with EMBL:AAI25207.1) (synonyms: KIAA1135, SPIR1)
Protein Name(s) Protein spire homolog 1

Spir-1

External Links
UniProt Q08AE8
EMBL AB032961
AK290180
AL833817
AP001028
AP001029
AP005482
CH471113
BC115005
BC125206
BC125207
AJ277587
CCDS CCDS32790.2
CCDS45829.1
CCDS45830.1
RefSeq NP_001122098.1
NP_001122099.1
NP_064533.3
UniGene Hs.515283
PDB 2YLE
2YLF
3R7G
3RBW
PDBsum 2YLE
2YLF
3R7G
3RBW
ProteinModelPortal Q08AE8
SMR Q08AE8
BioGrid 121237
DIP DIP-42378N
IntAct Q08AE8
MINT MINT-3975323
STRING 9606.ENSP00000387266
iPTMnet Q08AE8
PhosphoSite Q08AE8
BioMuta SPIRE1
DMDM 425906061
EPD Q08AE8
MaxQB Q08AE8
PaxDb Q08AE8
PRIDE Q08AE8
Ensembl ENST00000409402
ENST00000410092
ENST00000440472
ENST00000453447
GeneID 56907
KEGG hsa:56907
UCSC uc002kre.4
CTD 56907
GeneCards SPIRE1
HGNC HGNC:30622
HPA HPA040737
HPA040942
MIM 609216
neXtProt NX_Q08AE8
PharmGKB PA134895885
eggNOG ENOG410IK9H
ENOG4111E0J
GeneTree ENSGT00390000003058
HOGENOM HOG000013039
HOVERGEN HBG058898
InParanoid Q08AE8
KO K02098
OMA STGHHRP
OrthoDB EOG77DJ5G
PhylomeDB Q08AE8
TreeFam TF326239
ChiTaRS SPIRE1
GenomeRNAi 56907
PRO PR:Q08AE8
Proteomes UP000005640
Bgee Q08AE8
CleanEx HS_SPIRE1
ExpressionAtlas Q08AE8
Genevisible Q08AE8
GO GO:0005938
GO:0030659
GO:0005856
GO:0048471
GO:0005886
GO:0030036
GO:0045010
GO:0036089
GO:0051295
GO:0070649
GO:0046907
GO:0040038
GO:0015031
GO:0016192
Gene3D 3.30.40.10
InterPro IPR011019
IPR029901
IPR029905
IPR011011
IPR013083
PANTHER PTHR21345
PTHR21345:SF2
Pfam PF16474
SMART SM00750
SUPFAM SSF57903
PROSITE PS51377

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0031307

integral component of mitochondrial outer membrane

PMID:26305500[1]

ECO:0000314

C

Figure 2A - Spire1C is localized at the periphery of the mitochondria. Figure 2D - fluorescence assay demonstrated that the N-terminus of Spire1C is exposed to the cytoplasm while the C-terminus is not

complete
CACAO 12176

GO:0090141

positive regulation of mitochondrial fission

PMID:26305500[1]

ECO:0000315

P

Figure 4

complete
CACAO 12177

GO:0090141

positive regulation of mitochondrial fission

PMID:26305500[1]

ECO:0000316

UniProtKB:Q27J81


P

Figure 6C and 6D - cells with overexpression of either Spire1C or INF2 or both display short mitochondria, while cells with knocked down expression of INF2 or mutant Spire1C display tubular mitochondria

complete
CACAO 12178

GO:0032233

positive regulation of actin filament bundle assembly

PMID:26305500[1]

ECO:0000315

P

Figure 3 - cells with overexpression of Spire1C show increased actin assembly on mitochondria as compared to control, while cells with overexpression of mutant Spire1C do not show increased actin assembly on mitochondria as compared to control

complete
CACAO 12180

GO:0051639

actin filament network formation

PMID:26305500[1]

ECO:0000315

P

Figure 3 - cells with overexpression of Spire1C show increased actin assembly on mitochondria as compared to control, while cells with overexpression of mutant Spire1C do not show increased actin assembly on mitochondria as compared to control

complete
CACAO 12181

involved_in

GO:2000781

positive regulation of double-strand break repair

PMID:26287480[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0070649

formin-nucleated actin cable assembly

PMID:26287480[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0070649

formin-nucleated actin cable assembly

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q52KF3

P

Seeded From UniProt

complete

involved_in

GO:0051295

establishment of meiotic spindle localization

PMID:21620703[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0046907

intracellular transport

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q52KF3

P

Seeded From UniProt

complete

involved_in

GO:0040038

polar body extrusion after meiotic divisions

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q52KF3

P

Seeded From UniProt

complete

involved_in

GO:0036089

cleavage furrow formation

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q52KF3

P

Seeded From UniProt

complete

colocalizes_with

GO:0032154

cleavage furrow

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q52KF3

C

Seeded From UniProt

complete

part_of

GO:0030659

cytoplasmic vesicle membrane

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q52KF3

C

Seeded From UniProt

complete

involved_in

GO:0030036

actin cytoskeleton organization

PMID:21620703[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016192

vesicle-mediated transport

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q52KF3

P

Seeded From UniProt

complete

part_of

GO:0005938

cell cortex

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q52KF3

C

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:0005654

nucleoplasm

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003779

actin binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR029901
InterPro:IPR029905

F

Seeded From UniProt

complete

involved_in

GO:0016192

vesicle-mediated transport

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR029901
InterPro:IPR029905

P

Seeded From UniProt

complete

involved_in

GO:0045010

actin nucleation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR029901
InterPro:IPR029905

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

Seeded From UniProt

complete

involved_in

GO:0015031

protein transport

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0653

P

Seeded From UniProt

complete

enables

GO:0003779

actin binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0009

F

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0206
UniProtKB-SubCell:SL-0090

C

Seeded From UniProt

complete

part_of

GO:0031410

cytoplasmic vesicle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0968

C

Seeded From UniProt

complete

part_of

GO:0030659

cytoplasmic vesicle membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0089

C

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0198

C

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 1.4 Manor, U et al. (2015) A mitochondria-anchored isoform of the actin-nucleating spire protein regulates mitochondrial division. Elife 4 PubMed GONUTS page
  2. 2.0 2.1 Belin, BJ et al. (2015) DNA damage induces nuclear actin filament assembly by Formin -2 and Spire-½ that promotes efficient DNA repair. [corrected]. Elife 4 e07735 PubMed GONUTS page
  3. 3.0 3.1 Pfender, S et al. (2011) Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric oocyte division. Curr. Biol. 21 955-60 PubMed GONUTS page