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Protein

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

Gene

PPP2R5C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation.2 Publications

GO - Molecular functioni

  • protein phosphatase type 2A regulator activity Source: UniProtKB

GO - Biological processi

  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • signal transduction Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000078304-MONOMER.
ReactomeiR-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5673000. RAF activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-68877. Mitotic Prometaphase.
SignaLinkiQ13362.
SIGNORiQ13362.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
Alternative name(s):
PP2A B subunit isoform B'-gamma
PP2A B subunit isoform B56-gamma
PP2A B subunit isoform PR61-gamma
PP2A B subunit isoform R5-gamma
Renal carcinoma antigen NY-REN-29
Gene namesi
Name:PPP2R5C
Synonyms:KIAA0044
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9311. PPP2R5C.

Subcellular locationi

GO - Cellular componenti

  • chromosome, centromeric region Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein phosphatase type 2A complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5527.
OpenTargetsiENSG00000078304.
PharmGKBiPA33674.

Polymorphism and mutation databases

BioMutaiPPP2R5C.
DMDMi116241235.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000714571 – 524Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoformAdd BLAST524

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1

Post-translational modificationi

Isoform Gamma-3 is phosphorylated on serine residues. Isoform Gamma-1 phosphorylation by ERK2 is IER3-dependent and inhibits ERK dephosphorylation by PP2A-PPP2R5C.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13362.
PaxDbiQ13362.
PeptideAtlasiQ13362.
PRIDEiQ13362.

PTM databases

iPTMnetiQ13362.
PhosphoSitePlusiQ13362.

Miscellaneous databases

PMAP-CutDBQ13362.

Expressioni

Tissue specificityi

Highest levels in heart, skeletal muscle and brain. Lower levels in pancreas, kidney, lung and placenta. Very low levels in liver.

Inductioni

Up-regulated upon DNA damage.1 Publication

Gene expression databases

BgeeiENSG00000078304.
CleanExiHS_PPP2R5C.
ExpressionAtlasiQ13362. baseline and differential.
GenevisibleiQ13362. HS.

Organism-specific databases

HPAiHPA027553.

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with PPP2CA AND PPP2R1A; the interaction is direct. Interacts with SGO1; the interaction is direct. Isoform 1 and isoform 2 interact with TP53 (phosphorylated at Ser-15 by ATM); increased upon DNA damage it drives PP2A-mediated dephosphorylation of TP53 at Thr-55. Interacts with IER3 and/or ERK kinases; regulates ERK dephosphorylation.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHEK2O960174EBI-1266176,EBI-1180783
IER3P466952EBI-1266156,EBI-1748945
MDM2Q009875EBI-1266156,EBI-389668
PPP2CAP677757EBI-1266156,EBI-712311
PPP2R1AP301537EBI-1266156,EBI-302388
PPP2R1BP301542EBI-1266156,EBI-357094
TP53P046374EBI-1266156,EBI-366083

Protein-protein interaction databases

BioGridi111519. 36 interactors.
DIPiDIP-39401N.
IntActiQ13362. 19 interactors.
MINTiMINT-2835438.
STRINGi9606.ENSP00000412324.

Structurei

Secondary structure

1524
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 32Combined sources3
Turni35 – 37Combined sources3
Helixi38 – 48Combined sources11
Beta strandi55 – 57Combined sources3
Turni59 – 62Combined sources4
Helixi63 – 82Combined sources20
Beta strandi83 – 85Combined sources3
Helixi91 – 103Combined sources13
Beta strandi115 – 118Combined sources4
Helixi120 – 122Combined sources3
Helixi131 – 146Combined sources16
Helixi152 – 155Combined sources4
Turni156 – 158Combined sources3
Helixi161 – 169Combined sources9
Helixi170 – 172Combined sources3
Helixi176 – 192Combined sources17
Helixi194 – 196Combined sources3
Helixi197 – 213Combined sources17
Helixi221 – 233Combined sources13
Helixi241 – 249Combined sources9
Turni250 – 252Combined sources3
Helixi253 – 256Combined sources4
Helixi260 – 262Combined sources3
Helixi264 – 277Combined sources14
Helixi279 – 281Combined sources3
Helixi282 – 292Combined sources11
Helixi301 – 313Combined sources13
Helixi317 – 335Combined sources19
Helixi340 – 347Combined sources8
Helixi348 – 351Combined sources4
Helixi353 – 360Combined sources8
Helixi363 – 370Combined sources8
Turni372 – 374Combined sources3
Helixi384 – 398Combined sources15
Helixi409 – 430Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IAEX-ray3.50B/E30-436[»]
2JAKX-ray2.60A11-380[»]
2NPPX-ray3.30B/E1-442[»]
2NYLX-ray3.80B/E38-425[»]
2NYMX-ray3.60B/E38-425[»]
3FGAX-ray2.70B34-436[»]
5JJAX-ray2.35A/B30-380[»]
ProteinModelPortaliQ13362.
SMRiQ13362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13362.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi416 – 422Nuclear localization signalSequence analysis7

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2085. Eukaryota.
ENOG410XQJW. LUCA.
GeneTreeiENSGT00550000074525.
HOGENOMiHOG000067326.
HOVERGENiHBG000009.
InParanoidiQ13362.
KOiK11584.
OMAiEECLKKF.
OrthoDBiEOG091G06HU.
PhylomeDBiQ13362.
TreeFamiTF105556.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 2 hits.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Gamma-3 (identifier: Q13362-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLTCNKAGSR MVVDAANSNG PFQPVVLLHI RDVPPADQEK LFIQKLRQCC
60 70 80 90 100
VLFDFVSDPL SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA
110 120 130 140 150
VNMFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF
160 170 180 190 200
QPNIAKKYID QKFVLQLLEL FDSEDPRERD FLKTTLHRIY GKFLGLRAYI
210 220 230 240 250
RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKIFLLKV
260 270 280 290 300
LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK
310 320 330 340 350
EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW
360 370 380 390 400
NNEYIMSLIS DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM
410 420 430 440 450
NQKLFDDCTQ QFKAEKLKEK LKMKEREEAW VKIENLAKAN PQYTVYSQAS
460 470 480 490 500
TMSIPVAMET DGPLFEDVQM LRKTVKDEAH QAQKDPKKDR PLARRKSELP
510 520
QDPHTKKALE AHCRADELAS QDGR
Length:524
Mass (Da):61,061
Last modified:October 17, 2006 - v3
Checksum:iB9CBF54550D713F8
GO
Isoform Gamma-1 (identifier: Q13362-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     443-524: YTVYSQASTM...ADELASQDGR → VLKKRIT

Show »
Length:449
Mass (Da):52,625
Checksum:i73CE22E378289FE8
GO
Isoform Gamma-2 (identifier: Q13362-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     443-481: Missing.

Show »
Length:485
Mass (Da):56,661
Checksum:i64F2D9D78F9D35B6
GO
Isoform 4 (identifier: Q13362-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: MLTCNKAGSRMVVDAANSNGPFQPVVLLHIR → MPNKNKKEKE...RELQKLPSLK
     443-481: Missing.

Note: No experimental confirmation available.
Show »
Length:540
Mass (Da):62,755
Checksum:i30B98C5AED1A4466
GO
Isoform 5 (identifier: Q13362-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MLTCNKAGSRMVVDAANSNGPFQPVVLLHI → MPNKNKKEKE...LVLIFGGLQG

Note: No experimental confirmation available.Curated
Show »
Length:555
Mass (Da):64,292
Checksum:i1C4C9780CF86FF71
GO

Sequence cautioni

The sequence AAC50387 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG63760 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti494R → L in AAC50387 (PubMed:8617797).Curated1
Isoform 5 (identifier: Q13362-5)
Sequence conflicti3N → K in BAG63760 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051745515A → P.Corresponds to variant rs3742424dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0436451 – 31MLTCN…LLHIR → MPNKNKKEKESPKAGKSGKS SKEGQDTVESEQISVRKNSL VAVPSTVSAKIKVPVSQPIV KKDKRQNSSRFSASNNRELQ KLPSLK in isoform 4. 1 PublicationAdd BLAST31
Alternative sequenceiVSP_0467681 – 30MLTCN…VLLHI → MPNKNKKEKESPKAGKSGKS SKEGQDTVESEGTSPEEPSS PKVPPPLLPELLVLIFGGLQ G in isoform 5. CuratedAdd BLAST30
Alternative sequenceiVSP_005112443 – 524YTVYS…SQDGR → VLKKRIT in isoform Gamma-1. 2 PublicationsAdd BLAST82
Alternative sequenceiVSP_005113443 – 481Missing in isoform Gamma-2 and isoform 4. 2 PublicationsAdd BLAST39

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37352 mRNA. Translation: AAC50387.1. Different initiation.
Z69030 mRNA. Translation: CAA93154.1.
AK131391 mRNA. Translation: BAD18542.1.
AK302470 mRNA. Translation: BAG63760.1. Different initiation.
AB451341 mRNA. Translation: BAG70155.1.
AL118558 Genomic DNA. No translation available.
AL137779 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81756.1.
D26445 mRNA. Translation: BAA05465.1.
L42375 mRNA. Translation: AAC37603.1.
CCDSiCCDS45163.1. [Q13362-2]
CCDS53911.1. [Q13362-4]
CCDS53912.1. [Q13362-5]
CCDS9964.1. [Q13362-1]
CCDS9965.1. [Q13362-3]
RefSeqiNP_001155197.1. NM_001161725.1. [Q13362-5]
NP_001155198.1. NM_001161726.1. [Q13362-4]
NP_002710.2. NM_002719.3. [Q13362-1]
NP_848701.1. NM_178586.2. [Q13362-3]
NP_848702.1. NM_178587.2. [Q13362-2]
XP_005267884.1. XM_005267827.1.
XP_011535222.1. XM_011536920.1.
UniGeneiHs.368264.

Genome annotation databases

EnsembliENST00000328724; ENSP00000329009; ENSG00000078304. [Q13362-4]
ENST00000334743; ENSP00000333905; ENSG00000078304. [Q13362-1]
ENST00000350249; ENSP00000262239; ENSG00000078304. [Q13362-3]
ENST00000422945; ENSP00000412324; ENSG00000078304. [Q13362-5]
ENST00000445439; ENSP00000408389; ENSG00000078304. [Q13362-2]
GeneIDi5527.
KEGGihsa:5527.
UCSCiuc001ykk.4. human. [Q13362-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37352 mRNA. Translation: AAC50387.1. Different initiation.
Z69030 mRNA. Translation: CAA93154.1.
AK131391 mRNA. Translation: BAD18542.1.
AK302470 mRNA. Translation: BAG63760.1. Different initiation.
AB451341 mRNA. Translation: BAG70155.1.
AL118558 Genomic DNA. No translation available.
AL137779 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81756.1.
D26445 mRNA. Translation: BAA05465.1.
L42375 mRNA. Translation: AAC37603.1.
CCDSiCCDS45163.1. [Q13362-2]
CCDS53911.1. [Q13362-4]
CCDS53912.1. [Q13362-5]
CCDS9964.1. [Q13362-1]
CCDS9965.1. [Q13362-3]
RefSeqiNP_001155197.1. NM_001161725.1. [Q13362-5]
NP_001155198.1. NM_001161726.1. [Q13362-4]
NP_002710.2. NM_002719.3. [Q13362-1]
NP_848701.1. NM_178586.2. [Q13362-3]
NP_848702.1. NM_178587.2. [Q13362-2]
XP_005267884.1. XM_005267827.1.
XP_011535222.1. XM_011536920.1.
UniGeneiHs.368264.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IAEX-ray3.50B/E30-436[»]
2JAKX-ray2.60A11-380[»]
2NPPX-ray3.30B/E1-442[»]
2NYLX-ray3.80B/E38-425[»]
2NYMX-ray3.60B/E38-425[»]
3FGAX-ray2.70B34-436[»]
5JJAX-ray2.35A/B30-380[»]
ProteinModelPortaliQ13362.
SMRiQ13362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111519. 36 interactors.
DIPiDIP-39401N.
IntActiQ13362. 19 interactors.
MINTiMINT-2835438.
STRINGi9606.ENSP00000412324.

PTM databases

iPTMnetiQ13362.
PhosphoSitePlusiQ13362.

Polymorphism and mutation databases

BioMutaiPPP2R5C.
DMDMi116241235.

Proteomic databases

MaxQBiQ13362.
PaxDbiQ13362.
PeptideAtlasiQ13362.
PRIDEiQ13362.

Protocols and materials databases

DNASUi5527.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328724; ENSP00000329009; ENSG00000078304. [Q13362-4]
ENST00000334743; ENSP00000333905; ENSG00000078304. [Q13362-1]
ENST00000350249; ENSP00000262239; ENSG00000078304. [Q13362-3]
ENST00000422945; ENSP00000412324; ENSG00000078304. [Q13362-5]
ENST00000445439; ENSP00000408389; ENSG00000078304. [Q13362-2]
GeneIDi5527.
KEGGihsa:5527.
UCSCiuc001ykk.4. human. [Q13362-1]

Organism-specific databases

CTDi5527.
DisGeNETi5527.
GeneCardsiPPP2R5C.
HGNCiHGNC:9311. PPP2R5C.
HPAiHPA027553.
MIMi601645. gene.
neXtProtiNX_Q13362.
OpenTargetsiENSG00000078304.
PharmGKBiPA33674.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2085. Eukaryota.
ENOG410XQJW. LUCA.
GeneTreeiENSGT00550000074525.
HOGENOMiHOG000067326.
HOVERGENiHBG000009.
InParanoidiQ13362.
KOiK11584.
OMAiEECLKKF.
OrthoDBiEOG091G06HU.
PhylomeDBiQ13362.
TreeFamiTF105556.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000078304-MONOMER.
ReactomeiR-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5673000. RAF activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-68877. Mitotic Prometaphase.
SignaLinkiQ13362.
SIGNORiQ13362.

Miscellaneous databases

ChiTaRSiPPP2R5C. human.
EvolutionaryTraceiQ13362.
GeneWikiiPPP2R5C.
GenomeRNAii5527.
PMAP-CutDBQ13362.
PROiQ13362.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000078304.
CleanExiHS_PPP2R5C.
ExpressionAtlasiQ13362. baseline and differential.
GenevisibleiQ13362. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERiPTHR10257. PTHR10257. 2 hits.
PfamiPF01603. B56. 1 hit.
[Graphical view]
PIRSFiPIRSF028043. PP2A_B56. 1 hit.
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry namei2A5G_HUMAN
AccessioniPrimary (citable) accession number: Q13362
Secondary accession number(s): B4DYJ8
, B5BUA5, F5GWP3, Q14391, Q15060, Q15174, Q6ZN33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.