SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P15374

- UCHL3_HUMAN

UniProt

P15374 - UCHL3_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Ubiquitin carboxyl-terminal hydrolase isozyme L3
Gene
UCHL3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.5 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).3 Publications

Enzyme regulationi

Inhibited by monoubiquitin and diubiquitin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Nucleophile
Active sitei169 – 1691Proton donor Inferred
Sitei184 – 1841Important for enzyme activity By similarity

GO - Molecular functioni

  1. peptidase activity Source: UniProtKB
  2. protein binding Source: IntAct
  3. ubiquitin binding Source: UniProtKB
  4. ubiquitin thiolesterase activity Source: UniProtKB
  5. ubiquitin-specific protease activity Source: InterPro

GO - Biological processi

  1. protein catabolic process Source: UniProtKB
  2. 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

SABIO-RKP15374.

Protein family/group databases

MEROPSiC12.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase isozyme L3 (EC:3.4.19.12)
Short name:
UCH-L3
Alternative name(s):
Ubiquitin thioesterase L3
Gene namesi
Name:UCHL3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:12515. UCHL3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProt
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331D → A: Decreased interaction with diubiquitin. No accumulation of free diubiquitin. Decreased levels of polyubiquitinated lysozyme. 2 Publications
Mutagenesisi95 – 951C → A: Increased interaction with diubiquitin. 3 Publications
Mutagenesisi95 – 951C → S: Abolishes enzymatic activity. Increased interaction with diubiquitin. 3 Publications

Organism-specific databases

PharmGKBiPA37162.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 230230Ubiquitin carboxyl-terminal hydrolase isozyme L3
PRO_0000211061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15374.
PaxDbiP15374.
PeptideAtlasiP15374.
PRIDEiP15374.

2D gel databases

OGPiP15374.
REPRODUCTION-2DPAGEIPI00011250.

PTM databases

PhosphoSiteiP15374.

Expressioni

Tissue specificityi

Highly expressed in heart, skeletal muscle, and testis.1 Publication

Gene expression databases

BgeeiP15374.
CleanExiHS_UCHL3.
GenevestigatoriP15374.

Organism-specific databases

HPAiHPA019678.

Interactioni

Subunit structurei

Preferentially binds diubiquitin; the interaction does not hydrolyze diubiquitin but, in vitro, inhibits the hydrolyzing activity on other substrates.

Binary interactionsi

WithEntry#Exp.IntActNotes
SMAD1Q157972EBI-954554,EBI-1567153

Protein-protein interaction databases

BioGridi113194. 56 interactions.
DIPiDIP-29135N.
IntActiP15374. 10 interactions.
MINTiMINT-2863935.
STRINGi9606.ENSP00000366819.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2210
Beta strandi29 – 335
Helixi39 – 424
Beta strandi49 – 579
Helixi60 – 7617
Helixi92 – 943
Helixi95 – 10511
Helixi106 – 1105
Helixi118 – 1269
Helixi131 – 1399
Helixi142 – 15211
Beta strandi155 – 1573
Beta strandi168 – 1769
Beta strandi179 – 1835
Beta strandi187 – 1893
Beta strandi191 – 1955
Turni198 – 2003
Helixi201 – 21515
Beta strandi223 – 2297

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UCHX-ray1.80A1-230[»]
1XD3X-ray1.45A/C1-230[»]
ProteinModelPortaliP15374.
SMRiP15374. Positions 2-230.

Miscellaneous databases

EvolutionaryTraceiP15374.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 136Interaction with ubiquitin
Regioni152 – 1598Interaction with ubiquitin
Regioni219 – 2246Interaction with ubiquitin

Sequence similaritiesi

Belongs to the peptidase C12 family.

Phylogenomic databases

eggNOGiNOG327708.
HOGENOMiHOG000182400.
HOVERGENiHBG075483.
KOiK05609.
OMAiYETFRTE.
OrthoDBiEOG7S7SFK.
PhylomeDBiP15374.
TreeFamiTF316166.

Family and domain databases

Gene3Di3.40.532.10. 1 hit.
InterProiIPR001578. Peptidase_C12_UCH.
[Graphical view]
PANTHERiPTHR10589. PTHR10589. 1 hit.
PfamiPF01088. Peptidase_C12. 1 hit.
[Graphical view]
PRINTSiPR00707. UBCTHYDRLASE.
PROSITEiPS00140. UCH_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15374-1 [UniParc]FASTAAdd to Basket

« Hide

MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMDPE LLSMVPRPVC    50
AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL 100
IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERARYLEN YDAIRVTHET 150
SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGETSDET 200
LLEDAIEVCK KFMERDPDEL RFNAIALSAA 230
Length:230
Mass (Da):26,183
Last modified:April 1, 1990 - v1
Checksum:i8ACACE6E1D86FD55
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30496 mRNA. Translation: AAA36791.1.
BT019359 mRNA. Translation: AAV38166.1.
CR456855 mRNA. Translation: CAG33136.1.
AK313665 mRNA. Translation: BAG36417.1.
AL137244 Genomic DNA. Translation: CAI12419.1.
CH471093 Genomic DNA. Translation: EAW80542.1.
BC018125 mRNA. Translation: AAH18125.1.
CCDSiCCDS9453.1.
PIRiA40085.
RefSeqiNP_001257881.1. NM_001270952.1.
NP_005993.1. NM_006002.4.
UniGeneiHs.162241.

Genome annotation databases

EnsembliENST00000377595; ENSP00000366819; ENSG00000118939.
GeneIDi7347.
KEGGihsa:7347.
UCSCiuc001vjq.4. human.

Polymorphism databases

DMDMi136682.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30496 mRNA. Translation: AAA36791.1 .
BT019359 mRNA. Translation: AAV38166.1 .
CR456855 mRNA. Translation: CAG33136.1 .
AK313665 mRNA. Translation: BAG36417.1 .
AL137244 Genomic DNA. Translation: CAI12419.1 .
CH471093 Genomic DNA. Translation: EAW80542.1 .
BC018125 mRNA. Translation: AAH18125.1 .
CCDSi CCDS9453.1.
PIRi A40085.
RefSeqi NP_001257881.1. NM_001270952.1.
NP_005993.1. NM_006002.4.
UniGenei Hs.162241.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UCH X-ray 1.80 A 1-230 [» ]
1XD3 X-ray 1.45 A/C 1-230 [» ]
ProteinModelPortali P15374.
SMRi P15374. Positions 2-230.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113194. 56 interactions.
DIPi DIP-29135N.
IntActi P15374. 10 interactions.
MINTi MINT-2863935.
STRINGi 9606.ENSP00000366819.

Chemistry

BindingDBi P15374.
ChEMBLi CHEMBL6195.

Protein family/group databases

MEROPSi C12.003.

PTM databases

PhosphoSitei P15374.

Polymorphism databases

DMDMi 136682.

2D gel databases

OGPi P15374.
REPRODUCTION-2DPAGE IPI00011250.

Proteomic databases

MaxQBi P15374.
PaxDbi P15374.
PeptideAtlasi P15374.
PRIDEi P15374.

Protocols and materials databases

DNASUi 7347.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377595 ; ENSP00000366819 ; ENSG00000118939 .
GeneIDi 7347.
KEGGi hsa:7347.
UCSCi uc001vjq.4. human.

Organism-specific databases

CTDi 7347.
GeneCardsi GC13P076123.
HGNCi HGNC:12515. UCHL3.
HPAi HPA019678.
MIMi 603090. gene.
neXtProti NX_P15374.
PharmGKBi PA37162.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG327708.
HOGENOMi HOG000182400.
HOVERGENi HBG075483.
KOi K05609.
OMAi YETFRTE.
OrthoDBi EOG7S7SFK.
PhylomeDBi P15374.
TreeFami TF316166.

Enzyme and pathway databases

SABIO-RK P15374.

Miscellaneous databases

ChiTaRSi UCHL3. human.
EvolutionaryTracei P15374.
GeneWikii UCHL3.
GenomeRNAii 7347.
NextBioi 28762.
PROi P15374.
SOURCEi Search...

Gene expression databases

Bgeei P15374.
CleanExi HS_UCHL3.
Genevestigatori P15374.

Family and domain databases

Gene3Di 3.40.532.10. 1 hit.
InterProi IPR001578. Peptidase_C12_UCH.
[Graphical view ]
PANTHERi PTHR10589. PTHR10589. 1 hit.
Pfami PF01088. Peptidase_C12. 1 hit.
[Graphical view ]
PRINTSi PR00707. UBCTHYDRLASE.
PROSITEi PS00140. UCH_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The neuron-specific protein PGP 9.5 is a ubiquitin carboxyl-terminal hydrolase."
    Wilkinson K.D., Lee K., Deshpande S., Duerksen-Hughes P., Boss J.M., Pohl J.
    Science 246:670-673(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  8. Cited for: FUNCTION, ENZYME ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-95.
  9. "Molecular profiling of the immune response in colon cancer using protein microarrays: occurrence of autoantibodies to ubiquitin C-terminal hydrolase L3."
    Nam M.J., Madoz-Gurpide J., Wang H., Lescure P., Schmalbach C.E., Zhao R., Misek D.E., Kuick R., Brenner D.E., Hanash S.M.
    Proteomics 3:2108-2115(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS TUMOR-ASSOCIATED ANTIGEN BY MASS SPECTROMETRY.
  10. "Substrate profiling of deubiquitin hydrolases with a positional scanning library and mass spectrometry."
    Mason D.E., Ek J., Peters E.C., Harris J.L.
    Biochemistry 43:6535-6544(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Ubiquitin dimers control the hydrolase activity of UCH-L3."
    Setsuie R., Sakurai M., Sakaguchi Y., Wada K.
    Neurochem. Int. 54:314-321(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH UBIQUITIN, FUNCTION, ENZYME REGULATION, MUTAGENESIS OF ASP-33 AND CYS-95.
  14. "Skeletal muscles of Uchl3 knockout mice show polyubiquitinated protein accumulation and stress responses."
    Setsuie R., Suzuki M., Tsuchiya Y., Wada K.
    Neurochem. Int. 56:911-918(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, MUTAGENESIS OF ASP-33 AND CYS-95.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Mutant ubiquitin (UBB(+1)) associated with neurodegenerative disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3)."
    Dennissen F.J., Kholod N., Hermes D.J., Kemmerling N., Steinbusch H.W., Dantuma N.P., van Leeuwen F.W.
    FEBS Lett. 585:2568-2574(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes."
    Iphofer A., Kummer A., Nimtz M., Ritter A., Arnold T., Frank R., van den Heuvel J., Kessler B.M., Jansch L., Franke R.
    ChemBioChem 13:1416-1420(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, LINKAGE SPECIFICITY.
  18. "Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8-A resolution."
    Johnston S.C., Larsen C.N., Cook W.J., Wilkinson K.D., Hill C.P.
    EMBO J. 16:3787-3796(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  19. "Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate."
    Misaghi S., Galardy P.J., Meester W.J.N., Ovaa H., Ploegh H.L., Gaudet R.
    J. Biol. Chem. 280:1512-1520(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH UBIQUITIN VINYLMETHYLESTER, ENZYME ACTIVITY.

Entry informationi

Entry nameiUCHL3_HUMAN
AccessioniPrimary (citable) accession number: P15374
Secondary accession number(s): B2R970, Q5TBK8, Q6IBE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 146 of the entry and version 1 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

Miscellaneous

Identified as a tumor-specific antigen in colon cancer.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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

External Data

Dasty 3

Similar proteinsi