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Protein

Ubiquitin carboxyl-terminal hydrolase 15

Gene

USP15

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

Functioni

Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. May also regulate gene expression and/or DNA repair through the deubiquitination of histone H2B (PubMed:24526689). Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.8 Publications

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei298 – 2981Nucleophile
Active sitei891 – 8911Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • SMAD binding Source: UniProtKB
  • thiol-dependent ubiquitin-specific protease activity Source: UniProtKB
  • transforming growth factor beta receptor binding Source: UniProtKB
  • ubiquitinated histone binding Source: UniProtKB

GO - Biological processi

  • BMP signaling pathway Source: UniProtKB
  • histone H2B conserved C-terminal lysine deubiquitination Source: UniProtKB
  • monoubiquitinated protein deubiquitination Source: UniProtKB
  • pathway-restricted SMAD protein phosphorylation Source: UniProtKB
  • protein deubiquitination Source: UniProtKB
  • transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-2173788. Downregulation of TGF-beta receptor signaling.

Protein family/group databases

MEROPSiC19.022.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 15 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 15
Ubiquitin thioesterase 15
Ubiquitin-specific-processing protease 15
Unph-2
Unph4
Gene namesi
Name:USP15
Synonyms:KIAA0529
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:12613. USP15.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi298 – 2981C → A: Loss of enzyme activity. 3 Publications
Mutagenesisi812 – 8121C → A: Loss of activity towards polyubiquitin. 2 Publications

Organism-specific databases

PharmGKBiPA37239.

Polymorphism and mutation databases

BioMutaiUSP15.
DMDMi28381406.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 981980Ubiquitin carboxyl-terminal hydrolase 15PRO_0000080641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei226 – 2261PhosphothreonineCombined sources
Modified residuei229 – 2291PhosphoserineCombined sources
Modified residuei242 – 2421PhosphoserineCombined sources
Modified residuei602 – 6021PhosphothreonineBy similarity
Modified residuei961 – 9611PhosphoserineCombined sources
Modified residuei965 – 9651PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated. Phosphorylation protects against ubiquitination and subsequent degradation by the proteasome.1 Publication
Ubiquitinated, leading to degradation by the proteasome.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y4E8.
MaxQBiQ9Y4E8.
PaxDbiQ9Y4E8.
PeptideAtlasiQ9Y4E8.
PRIDEiQ9Y4E8.

PTM databases

iPTMnetiQ9Y4E8.
PhosphoSiteiQ9Y4E8.

Expressioni

Tissue specificityi

Expressed in skeletal muscle, kidney, heart, placenta, liver, thymus, lung, and ovary, with little or no expression in other tissues.

Gene expression databases

BgeeiENSG00000135655.
CleanExiHS_USP15.
ExpressionAtlasiQ9Y4E8. baseline and differential.
GenevisibleiQ9Y4E8. HS.

Organism-specific databases

HPAiHPA006237.

Interactioni

Subunit structurei

A homodimer structure has been reported; however it is unclear whether the protein form a homodimer in vivo (PubMed:22001210). Identified in a complex with the COP9 signalosome complex (CSN). Interacts with SMAD1, SMAD2 and SMAD3; the interaction is direct. Forms a complex with SMURF2 and SMAD7. Interacts with TGFBR1. Interacts with SART3; the interaction is direct. May interact with RNF20 and RNF40. Interacts with human papillomavirus type 16 protein E6.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-1043104,EBI-1043104
CARD9Q9H2573EBI-1043104,EBI-751319
CCDC57Q2TAC23EBI-1043104,EBI-2808286
MAD1L1Q9Y6D93EBI-1043104,EBI-742610
SPDL1Q96EA43EBI-1043104,EBI-715381
TRIM21P194743EBI-1043104,EBI-81290

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • SMAD binding Source: UniProtKB
  • transforming growth factor beta receptor binding Source: UniProtKB
  • ubiquitinated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115283. 146 interactions.
DIPiDIP-50239N.
IntActiQ9Y4E8. 51 interactions.
MINTiMINT-4542165.
STRINGi9606.ENSP00000258123.

Structurei

Secondary structure

1
981
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi9 – 1911Combined sources
Beta strandi29 – 346Combined sources
Helixi35 – 4511Combined sources
Turni46 – 483Combined sources
Turni53 – 564Combined sources
Helixi58 – 603Combined sources
Helixi68 – 703Combined sources
Beta strandi73 – 764Combined sources
Turni86 – 883Combined sources
Beta strandi89 – 935Combined sources
Helixi94 – 10411Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi134 – 1407Combined sources
Beta strandi143 – 15210Combined sources
Helixi158 – 16811Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi177 – 1848Combined sources
Beta strandi187 – 1904Combined sources
Helixi198 – 2014Combined sources
Beta strandi208 – 2136Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W6VNMR-A1-120[»]
3LMNX-ray2.15A/B1-133[»]
3PPAX-ray2.35A6-223[»]
3PV1X-ray2.60A/B1-223[»]
3T9LX-ray1.50A1-222[»]
4A3OX-ray2.20A/B4-223[»]
4A3PX-ray1.40A6-223[»]
5JJWX-ray3.01B1-223[»]
ProteinModelPortaliQ9Y4E8.
SMRiQ9Y4E8. Positions 6-222, 285-470, 786-934.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y4E8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 118112DUSPPROSITE-ProRule annotationAdd
BLAST
Domaini289 – 933645USPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 223222Mediates interaction with SART31 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 DUSP domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiKOG1870. Eukaryota.
COG5560. LUCA.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000264375.
HOVERGENiHBG000864.
InParanoidiQ9Y4E8.
KOiK11835.
OMAiFEIAINR.
OrthoDBiEOG091G0157.
PhylomeDBiQ9Y4E8.
TreeFamiTF106276.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR028135. Ub_USP-typ.
IPR029071. Ubiquitin-rel_dom.
IPR029346. USP_C.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
PF14533. USP7_C2. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55205. SSF55205. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y4E8-1) [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
MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW
60 70 80 90 100
DKYQMGDQNV YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL
110 120 130 140 150
VSWYTLMEGQ EPIARKVVEQ GMFVKHCKVE VYLTELKLCE NGNMNNVVTR
160 170 180 190 200
RFSKADTIDT IEKEIRKIFS IPDEKETRLW NKYMSNTFEP LNKPDSTIQD
210 220 230 240 250
AGLYQGQVLV IEQKNEDGTW PRGPSTPKSP GASNFSTLPK ISPSSLSNNY
260 270 280 290 300
NNMNNRNVKN SNYCLPSYTA YKNYDYSEPG RNNEQPGLCG LSNLGNTCFM
310 320 330 340 350
NSAIQCLSNT PPLTEYFLND KYQEELNFDN PLGMRGEIAK SYAELIKQMW
360 370 380 390 400
SGKFSYVTPR AFKTQVGRFA PQFSGYQQQD CQELLAFLLD GLHEDLNRIR
410 420 430 440 450
KKPYIQLKDA DGRPDKVVAE EAWENHLKRN DSIIVDIFHG LFKSTLVCPE
460 470 480 490 500
CAKISVTFDP FCYLTLPLPM KKERTLEVYL VRMDPLTKPM QYKVVVPKIG
510 520 530 540 550
NILDLCTALS ALSGIPADKM IVTDIYNHRF HRIFAMDENL SSIMERDDIY
560 570 580 590 600
VFEININRTE DTEHVIIPVC LREKFRHSSY THHTGSSLFG QPFLMAVPRN
610 620 630 640 650
NTEDKLYNLL LLRMCRYVKI STETEETEGS LHCCKDQNIN GNGPNGIHEE
660 670 680 690 700
GSPSEMETDE PDDESSQDQE LPSENENSQS EDSVGGDNDS ENGLCTEDTC
710 720 730 740 750
KGQLTGHKKR LFTFQFNNLG NTDINYIKDD TRHIRFDDRQ LRLDERSFLA
760 770 780 790 800
LDWDPDLKKR YFDENAAEDF EKHESVEYKP PKKPFVKLKD CIELFTTKEK
810 820 830 840 850
LGAEDPWYCP NCKEHQQATK KLDLWSLPPV LVVHLKRFSY SRYMRDKLDT
860 870 880 890 900
LVDFPINDLD MSEFLINPNA GPCRYNLIAV SNHYGGMGGG HYTAFAKNKD
910 920 930 940 950
DGKWYYFDDS SVSTASEDQI VSKAAYVLFY QRQDTFSGTG FFPLDRETKG
960 970 980
ASAATGIPLE SDEDSNDNDN DIENENCMHT N
Length:981
Mass (Da):112,419
Last modified:February 12, 2003 - v3
Checksum:iE81FEB9DE57F7089
GO
Isoform 2 (identifier: Q9Y4E8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     228-256: Missing.

Show »
Length:952
Mass (Da):109,297
Checksum:i852ED3768FB5725A
GO
Isoform 3 (identifier: Q9Y4E8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     217-256: DGTWPRGPSTPKSPGASNFSTLPKISPSSLSNNYNNMNNR → QKNEDGTWPRGPSTP

Show »
Length:956
Mass (Da):109,796
Checksum:iF9F83D3886404B11
GO
Isoform 4 (identifier: Q9Y4E8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-235: SPGASNF → KPLEQSC
     236-981: Missing.

Show »
Length:235
Mass (Da):27,094
Checksum:iF69B0D2783E2A443
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti559 – 5591T → A in AAG28973 (Ref. 9) Curated
Sequence conflicti747 – 7471S → F in AAI25124 (PubMed:15489334).Curated
Sequence conflicti968 – 9681N → H in AAG28973 (Ref. 9) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei217 – 25640DGTWP…NMNNR → QKNEDGTWPRGPSTP in isoform 3. 1 PublicationVSP_005260Add
BLAST
Alternative sequencei228 – 25629Missing in isoform 2. 3 PublicationsVSP_005261Add
BLAST
Alternative sequencei229 – 2357SPGASNF → KPLEQSC in isoform 4. 2 PublicationsVSP_045165
Alternative sequencei236 – 981746Missing in isoform 4. 2 PublicationsVSP_045166Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106069 mRNA. Translation: AAD52099.1.
AB011101 mRNA. Translation: BAA25455.2.
AF153604 mRNA. Translation: AAD41086.1.
AK023703 mRNA. Translation: BAB14648.1.
AK292337 mRNA. Translation: BAF85026.1.
AC048342 Genomic DNA. No translation available.
AC079035 Genomic DNA. No translation available.
AC117370 Genomic DNA. No translation available.
BC020688 mRNA. Translation: AAH20688.1.
BC063454 mRNA. Translation: AAH63454.1.
BC125123 mRNA. Translation: AAI25124.1.
AF013990 mRNA. Translation: AAG28973.1.
CCDSiCCDS58250.1. [Q9Y4E8-4]
CCDS58251.1. [Q9Y4E8-1]
CCDS8963.1. [Q9Y4E8-2]
RefSeqiNP_001239007.1. NM_001252078.1. [Q9Y4E8-1]
NP_001239008.1. NM_001252079.1. [Q9Y4E8-4]
NP_006304.1. NM_006313.2. [Q9Y4E8-2]
UniGeneiHs.434951.

Genome annotation databases

EnsembliENST00000280377; ENSP00000280377; ENSG00000135655. [Q9Y4E8-1]
ENST00000312635; ENSP00000309240; ENSG00000135655. [Q9Y4E8-4]
ENST00000353364; ENSP00000258123; ENSG00000135655. [Q9Y4E8-2]
GeneIDi9958.
KEGGihsa:9958.
UCSCiuc001sra.4. human. [Q9Y4E8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106069 mRNA. Translation: AAD52099.1.
AB011101 mRNA. Translation: BAA25455.2.
AF153604 mRNA. Translation: AAD41086.1.
AK023703 mRNA. Translation: BAB14648.1.
AK292337 mRNA. Translation: BAF85026.1.
AC048342 Genomic DNA. No translation available.
AC079035 Genomic DNA. No translation available.
AC117370 Genomic DNA. No translation available.
BC020688 mRNA. Translation: AAH20688.1.
BC063454 mRNA. Translation: AAH63454.1.
BC125123 mRNA. Translation: AAI25124.1.
AF013990 mRNA. Translation: AAG28973.1.
CCDSiCCDS58250.1. [Q9Y4E8-4]
CCDS58251.1. [Q9Y4E8-1]
CCDS8963.1. [Q9Y4E8-2]
RefSeqiNP_001239007.1. NM_001252078.1. [Q9Y4E8-1]
NP_001239008.1. NM_001252079.1. [Q9Y4E8-4]
NP_006304.1. NM_006313.2. [Q9Y4E8-2]
UniGeneiHs.434951.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W6VNMR-A1-120[»]
3LMNX-ray2.15A/B1-133[»]
3PPAX-ray2.35A6-223[»]
3PV1X-ray2.60A/B1-223[»]
3T9LX-ray1.50A1-222[»]
4A3OX-ray2.20A/B4-223[»]
4A3PX-ray1.40A6-223[»]
5JJWX-ray3.01B1-223[»]
ProteinModelPortaliQ9Y4E8.
SMRiQ9Y4E8. Positions 6-222, 285-470, 786-934.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115283. 146 interactions.
DIPiDIP-50239N.
IntActiQ9Y4E8. 51 interactions.
MINTiMINT-4542165.
STRINGi9606.ENSP00000258123.

Protein family/group databases

MEROPSiC19.022.

PTM databases

iPTMnetiQ9Y4E8.
PhosphoSiteiQ9Y4E8.

Polymorphism and mutation databases

BioMutaiUSP15.
DMDMi28381406.

Proteomic databases

EPDiQ9Y4E8.
MaxQBiQ9Y4E8.
PaxDbiQ9Y4E8.
PeptideAtlasiQ9Y4E8.
PRIDEiQ9Y4E8.

Protocols and materials databases

DNASUi9958.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000280377; ENSP00000280377; ENSG00000135655. [Q9Y4E8-1]
ENST00000312635; ENSP00000309240; ENSG00000135655. [Q9Y4E8-4]
ENST00000353364; ENSP00000258123; ENSG00000135655. [Q9Y4E8-2]
GeneIDi9958.
KEGGihsa:9958.
UCSCiuc001sra.4. human. [Q9Y4E8-1]

Organism-specific databases

CTDi9958.
GeneCardsiUSP15.
H-InvDBHIX0010773.
HGNCiHGNC:12613. USP15.
HPAiHPA006237.
MIMi604731. gene.
neXtProtiNX_Q9Y4E8.
PharmGKBiPA37239.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1870. Eukaryota.
COG5560. LUCA.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000264375.
HOVERGENiHBG000864.
InParanoidiQ9Y4E8.
KOiK11835.
OMAiFEIAINR.
OrthoDBiEOG091G0157.
PhylomeDBiQ9Y4E8.
TreeFamiTF106276.

Enzyme and pathway databases

ReactomeiR-HSA-2173788. Downregulation of TGF-beta receptor signaling.

Miscellaneous databases

ChiTaRSiUSP15. human.
EvolutionaryTraceiQ9Y4E8.
GeneWikiiUSP15.
GenomeRNAii9958.
PROiQ9Y4E8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000135655.
CleanExiHS_USP15.
ExpressionAtlasiQ9Y4E8. baseline and differential.
GenevisibleiQ9Y4E8. HS.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR001394. Peptidase_C19_UCH.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR028135. Ub_USP-typ.
IPR029071. Ubiquitin-rel_dom.
IPR029346. USP_C.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
PF14533. USP7_C2. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55205. SSF55205. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBP15_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4E8
Secondary accession number(s): Q08AL5
, Q9H8G9, Q9HCA6, Q9UNP0, Q9Y5B5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 12, 2003
Last modified: September 7, 2016
This is version 164 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. 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.