HUMAN:1433B

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	YWHAB
Protein Name(s)	14-3-3 protein beta/alpha Protein 1054 Protein kinase C inhibitor protein 1 KCIP-1 14-3-3 protein beta/alpha, N-terminally processed
External Links
UniProt	P31946
EMBL	X57346 AK292717 AL008725 CH471077 CH471077 CH471077 BC001359
CCDS	CCDS13339.1
PIR	S34755
RefSeq	NP_003395.1 NP_647539.1
UniGene	Hs.643544
PDB	2BQ0 2C23 4DNK
PDBsum	2BQ0 2C23 4DNK
ProteinModelPortal	P31946
SMR	P31946
BioGrid	113361
DIP	DIP-743N
IntAct	P31946
MINT	MINT-99570
STRING	9606.ENSP00000300161
PhosphoSite	P31946
DMDM	1345590
OGP	P31946
REPRODUCTION-2DPAGE	IPI00216318
MaxQB	P31946
PaxDb	P31946
PRIDE	P31946
DNASU	7529
Ensembl	ENST00000353703 ENST00000372839
GeneID	7529
KEGG	hsa:7529
UCSC	uc002xmt.3
CTD	7529
GeneCards	GC20P043515
HGNC	HGNC:12849
HPA	CAB003759 HPA007925 HPA011212
MIM	601289
neXtProt	NX_P31946
PharmGKB	PA37438
eggNOG	COG5040
HOGENOM	HOG000240379
HOVERGEN	HBG050423
InParanoid	P31946
KO	K16197
OMA	MGREYRE
OrthoDB	EOG7HHWT3
PhylomeDB	P31946
TreeFam	TF102003
Reactome	REACT_118607 REACT_12002 REACT_12076 REACT_147867 REACT_2077 REACT_23898 REACT_24915 REACT_25064 REACT_614 REACT_962
SignaLink	P31946
ChiTaRS	YWHAB
EvolutionaryTrace	P31946
GeneWiki	YWHAB
GenomeRNAi	7529
NextBio	29453
PRO	PR:P31946
Proteomes	UP000005640
Bgee	P31946
CleanEx	HS_YWHAB
ExpressionAtlas	P31946
Genevestigator	P31946
GO	GO:0005737 GO:0030659 GO:0005829 GO:0070062 GO:0005925 GO:0042470 GO:0016020 GO:0005634 GO:0048471 GO:0017053 GO:0019899 GO:0042826 GO:0051219 GO:0050815 GO:0019904 GO:0003714 GO:0000186 GO:0006915 GO:0007411 GO:0051220 GO:0007173 GO:0038095 GO:0008543 GO:0010467 GO:0035329 GO:0045087 GO:0008286 GO:0097193 GO:0000165 GO:0061024 GO:0016071 GO:0035308 GO:0045892 GO:0048011 GO:0043085 GO:1900740 GO:0051291 GO:0006605 GO:0007265 GO:0016070 GO:0007264
InterPro	IPR000308 IPR023409 IPR023410
PANTHER	PTHR18860
Pfam	PF00244
PIRSF	PIRSF000868
PRINTS	PR00305
SMART	SM00101
SUPFAM	SSF48445
PROSITE	PS00796 PS00797

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0045296	cadherin binding	PMID:25468996^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045744	negative regulation of G protein-coupled receptor signaling pathway	PMID:21224381^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
involved_in	GO:0051220	cytoplasmic sequestering of protein	PMID:10869435^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051219	phosphoprotein binding	PMID:10869435^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UQL6	F		Seeded From UniProt	complete
enables	GO:0050815	phosphoserine residue binding	PMID:10869435^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P56524	F		Seeded From UniProt	complete
involved_in	GO:0043085	positive regulation of catalytic activity	PMID:17255105^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	PMID:10869435^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P56524	F		Seeded From UniProt	complete
enables	GO:0042826	histone deacetylase binding	PMID:10869435^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UQL6	F		Seeded From UniProt	complete
involved_in	GO:0035308	negative regulation of protein dephosphorylation	PMID:17255105^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:17255105^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13370	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:10869435^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:12963375^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:11984006^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q99698	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12963375^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23622247^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P31946	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17085597^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P31946	F		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:0005739	mitochondrion	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:1900740	C		Seeded From UniProt	complete
involved_in	GO:0051291	protein heterooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35213 ensembl:ENSRNOP00000016981	P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35213 ensembl:ENSRNOP00000016981	P		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35213 ensembl:ENSRNOP00000016981	F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35213 ensembl:ENSRNOP00000016981	C		Seeded From UniProt	complete
part_of	GO:0017053	transcriptional repressor complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35213 ensembl:ENSRNOP00000016981	C		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35213 ensembl:ENSRNOP00000016981	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35213 ensembl:ENSRNOP00000016981	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P35213 ensembl:ENSRNOP00000016981	C		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CQV8 ensembl:ENSMUSP00000018470	F		Seeded From UniProt	complete
involved_in	GO:0006605	protein targeting	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9CQV8 ensembl:ENSMUSP00000018470	P		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000308	F		Seeded From UniProt	complete
involved_in	GO:1900740	positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway	Reactome:R-HSA-111447	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061024	membrane organization	Reactome:R-HSA-199991	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043488	regulation of mRNA stability	Reactome:R-HSA-450513 Reactome:R-HSA-450385	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035329	hippo signaling	Reactome:R-HSA-2028269	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-9614423 Reactome:R-HSA-913993 Reactome:R-HSA-8936731 Reactome:R-HSA-8936676 Reactome:R-HSA-75016 Reactome:R-HSA-6803240 Reactome:R-HSA-6803234 Reactome:R-HSA-6803233 Reactome:R-HSA-6803230 Reactome:R-HSA-6802943 Reactome:R-HSA-6802942 Reactome:R-HSA-6802941 Reactome:R-HSA-6802926 Reactome:R-HSA-6802925 Reactome:R-HSA-6802924 Reactome:R-HSA-6802922 Reactome:R-HSA-6802921 Reactome:R-HSA-6802919 Reactome:R-HSA-6802918 Reactome:R-HSA-6802916 Reactome:R-HSA-6802914 Reactome:R-HSA-6802908 Reactome:R-HSA-5675433 Reactome:R-HSA-5675431 Reactome:R-HSA-5675417 Reactome:R-HSA-5672980 Reactome:R-HSA-5672978 Reactome:R-HSA-5672973 Reactome:R-HSA-5672972 Reactome:R-HSA-5672969 Reactome:R-HSA-5672966 Reactome:R-HSA-5672961 Reactome:R-HSA-5672960 Reactome:R-HSA-5672958 Reactome:R-HSA-5672957 Reactome:R-HSA-5672954 Reactome:R-HSA-5672951 Reactome:R-HSA-5672950 Reactome:R-HSA-5672828 Reactome:R-HSA-5672824 Reactome:R-HSA-5632738 Reactome:R-HSA-5632732 Reactome:R-HSA-482788 Reactome:R-HSA-450406 Reactome:R-HSA-450394 Reactome:R-HSA-2028644 Reactome:R-HSA-1454689 Reactome:R-HSA-139906 Reactome:R-HSA-139899	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000165	MAPK cascade	Reactome:R-HSA-5673001	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		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:0005773	vacuole	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0926	C		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0042470	melanosome	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0161	C		Seeded From UniProt	complete
part_of	GO:0005774	vacuolar membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0271	C		Seeded From UniProt	complete
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Notes

References

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

↑ Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page
↑ Cariolato, L et al. (2011) A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling complex involved in α1-adrenergic receptor-induced p38 activation. J. Biol. Chem. 286 7925-37 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 Grozinger, CM & Schreiber, SL (2000) Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc. Natl. Acad. Sci. U.S.A. 97 7835-40 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Palmer, D et al. (2007) Protein kinase A phosphorylation of human phosphodiesterase 3B promotes 14-3-3 protein binding and inhibits phosphatase-catalyzed inactivation. J. Biol. Chem. 282 9411-9 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^9.0 ^9.1 Boutros, R et al. (2003) Alternative splicing as a mechanism for regulating 14-3-3 binding: interactions between hD53 (TPD52L1) and 14-3-3 proteins. J. Mol. Biol. 332 675-87 PubMed GONUTS page
↑ Tchernev, VT et al. (2002) The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins. Mol. Med. 8 56-64 PubMed GONUTS page
↑ Riou, P et al. (2013) 14-3-3 proteins interact with a hybrid prenyl-phosphorylation motif to inhibit G proteins. Cell 153 640-53 PubMed GONUTS page
↑ Yang, X et al. (2006) Structural basis for protein-protein interactions in the 14-3-3 protein family. Proc. Natl. Acad. Sci. U.S.A. 103 17237-42 PubMed GONUTS page

[PMID:25468996-1] Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page

[PMID:21224381-2] Cariolato, L et al. (2011) A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling complex involved in α1-adrenergic receptor-induced p38 activation. J. Biol. Chem. 286 7925-37 PubMed GONUTS page

[PMID:21423176-3] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:19946888-4] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:19199708-5] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:10869435-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 ^6.5 Grozinger, CM & Schreiber, SL (2000) Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc. Natl. Acad. Sci. U.S.A. 97 7835-40 PubMed GONUTS page

[PMID:17255105-7] 7.0 ^7.1 ^7.2 Palmer, D et al. (2007) Protein kinase A phosphorylation of human phosphodiesterase 3B promotes 14-3-3 protein binding and inhibits phosphatase-catalyzed inactivation. J. Biol. Chem. 282 9411-9 PubMed GONUTS page

[PMID:20458337-8] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:12963375-9] 9.0 ^9.1 Boutros, R et al. (2003) Alternative splicing as a mechanism for regulating 14-3-3 binding: interactions between hD53 (TPD52L1) and 14-3-3 proteins. J. Mol. Biol. 332 675-87 PubMed GONUTS page

[PMID:11984006-10] Tchernev, VT et al. (2002) The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins. Mol. Med. 8 56-64 PubMed GONUTS page

[PMID:23622247-11] Riou, P et al. (2013) 14-3-3 proteins interact with a hybrid prenyl-phosphorylation motif to inhibit G proteins. Cell 153 640-53 PubMed GONUTS page

[PMID:17085597-12] Yang, X et al. (2006) Structural basis for protein-protein interactions in the 14-3-3 protein family. Proc. Natl. Acad. Sci. U.S.A. 103 17237-42 PubMed GONUTS page

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HUMAN:1433B

Contents

Annotations

Notes

References

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