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Q92995 (UBP13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 13

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 13
Isopeptidase T-3
Short name=ISOT-3
Ubiquitin thioesterase 13
Ubiquitin-specific-processing protease 13
Gene names
Name:USP13
Synonyms:ISOT3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length863 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data. Ref.6 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Catalytic activity

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).

Enzyme regulation

Specifically inhibited by spautin-1 (specific and potent autophagy inhibitor-1), a derivative of MBCQ that binds to USP13 and inhibits deubiquitinase activity. Regulated by PIK3C3/VPS34-containing complexes. The weak deubiquitinase activity in vitro suggests the existence of some mechanism that activates the enzyme. Ref.10

Subunit structure

Interacts with UFD1. Interacts (via UBA domains) with SIAH2 (when ubiquitinated). Ref.11 Ref.13

Tissue specificity

Highly expressed in ovary and testes.

Domain

The UBP-type zinc finger has lost its ability to bind ubiquitin and USP13 is not activated by unanchored ubiquitin. Swapping with the UBP-type zinc finger from USP5 restores ability to bind unanchored ubiquitin and subsequent activation of the protein (Ref.15). Ref.15

The UBA domains mediate binding to ubiquitin (Ref.15). Ref.15

Sequence similarities

Belongs to the peptidase C19 family.

Contains 2 UBA domains.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Ontologies

Keywords
   Biological processAutophagy
Ubl conjugation pathway
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processautophagy

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from mutant phenotype Ref.12. Source: UniProtKB

melanocyte differentiation

Traceable author statement Ref.12. Source: UniProtKB

protein K63-linked deubiquitination

Inferred from direct assay Ref.15. Source: UniProtKB

protein stabilization

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of autophagy

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.12. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncysteine-type endopeptidase activity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

omega peptidase activity

Inferred from electronic annotation. Source: InterPro

ubiquitin binding

Inferred from direct assay Ref.11Ref.12Ref.15. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.11. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from direct assay Ref.12Ref.10Ref.15. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.12Ref.10Ref.15. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92995-1)

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.
Isoform 2 (identifier: Q92995-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 863863Ubiquitin carboxyl-terminal hydrolase 13
PRO_0000080635

Regions

Domain336 – 861526USP
Domain652 – 69342UBA 1
Domain727 – 76741UBA 2
Zinc finger209 – 28173UBP-type

Sites

Active site3451Nucleophile Probable
Active site8231Proton acceptor By similarity

Amino acid modifications

Modified residue1141Phosphoserine Ref.8
Modified residue1221Phosphothreonine Ref.7 Ref.8 Ref.14

Natural variations

Alternative sequence1 – 6565Missing in isoform 2.
VSP_043954

Experimental info

Mutagenesis2211W → A: Does not abolish ability to stabilize SIAH2. Ref.11
Mutagenesis2331K → A: Does not abolish ability to stabilize SIAH2. Ref.11
Mutagenesis2731F → A: Impairs ability to stabilize SIAH2. Ref.11
Mutagenesis3451C → A: Abolishes deubiquitinating activity. Does not abolish ability to stabilize SIAH2. Does not abolish ability to stabilize SIAH2; when associated with A-814 and A-823. Ref.11 Ref.12
Mutagenesis6641M → E: Impairs ability to stabilize SIAH2. Abolishes ability to stabilize SIAH2; when associated with E-739. Ref.11
Mutagenesis7391M → E: Impairs ability to stabilize SIAH2. Abolishes ability to stabilize SIAH2; when associated with E-664. Ref.11
Mutagenesis8141H → A: Does not abolish ability to stabilize SIAH2; when associated with A-345 and A-823. Ref.11 Ref.12
Mutagenesis8231H → A: Does not abolish ability to stabilize SIAH2; when associated with A-345 and A-814. Ref.11 Ref.12
Sequence conflict961V → A in AAC63405. Ref.1
Sequence conflict2931I → V in BAF83027. Ref.2
Sequence conflict3051L → F in BAF83027. Ref.2
Sequence conflict3251T → A in BAF83027. Ref.2
Sequence conflict3381L → P in BAF83027. Ref.2

Secondary structure

........................................ 863
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 988713ADF8C0B938

FASTA86397,327
        10         20         30         40         50         60 
MQRRGALFGM PGGSGGRKMA AGDIGELLVP HMPTIRVPRS GDRVYKNECA FSYDSPNSEG 

        70         80         90        100        110        120 
GLYVCMNTFL AFGREHVERH FRKTGQSVYM HLKRHVREKV RGASGGALPK RRNSKIFLDL 

       130        140        150        160        170        180 
DTDDDLNSDD YEYEDEAKLV IFPDHYEIAL PNIEELPALV TIACDAVLSS KSPYRKQDPD 

       190        200        210        220        230        240 
TWENELPVSK YANNLTQLDN GVRIPPSGWK CARCDLRENL WLNLTDGSVL CGKWFFDSSG 

       250        260        270        280        290        300 
GNGHALEHYR DMGYPLAVKL GTITPDGADV YSFQEEEPVL DPHLAKHLAH FGIDMLHMHG 

       310        320        330        340        350        360 
TENGLQDNDI KLRVSEWEVI QESGTKLKPM YGPGYTGLKN LGNSCYLSSV MQAIFSIPEF 

       370        380        390        400        410        420 
QRAYVGNLPR IFDYSPLDPT QDFNTQMTKL GHGLLSGQYS KPPVKSELIE QVMKEEHKPQ 

       430        440        450        460        470        480 
QNGISPRMFK AFVSKSHPEF SSNRQQDAQE FFLHLVNLVE RNRIGSENPS DVFRFLVEER 

       490        500        510        520        530        540 
IQCCQTRKVR YTERVDYLMQ LPVAMEAATN KDELIAYELT RREAEANRRP LPELVRAKIP 

       550        560        570        580        590        600 
FSACLQAFSE PENVDDFWSS ALQAKSAGVK TSRFASFPEY LVVQIKKFTF GLDWVPKKFD 

       610        620        630        640        650        660 
VSIDMPDLLD INHLRARGLQ PGEEELPDIS PPIVIPDDSK DRLMNQLIDP SDIDESSVMQ 

       670        680        690        700        710        720 
LAEMGFPLEA CRKAVYFTGN MGAEVAFNWI IVHMEEPDFA EPLTMPGYGG AASAGASVFG 

       730        740        750        760        770        780 
ASGLDNQPPE EIVAIITSMG FQRNQAIQAL RATNNNLERA LDWIFSHPEF EEDSDFVIEM 

       790        800        810        820        830        840 
ENNANANIIS EAKPEGPRVK DGSGTYELFA FISHMGTSTM SGHYICHIKK EGRWVIYNDH 

       850        860 
KVCASERPPK DLGYMYFYRR IPS 

« Hide

Isoform 2 [UniParc].

Checksum: 5F9943C19D16FE4F
Show »

FASTA79890,383

References

« Hide 'large scale' references
[1]"The genomic organization of Isopeptidase T-3 (ISOT-3), a new member of the ubiquitin specific protease family (UBP)."
Timms K.M., Ansari-Lari M.A., Morris W., Brown S.N., Gibbs R.A.
Gene 217:101-106(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Tissue: Testis and Tongue.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Uterus.
[6]"Screen for ISG15-crossreactive deubiquitinases."
Catic A., Fiebiger E., Korbel G.A., Blom D., Galardy P.J., Ploegh H.L.
PLoS ONE 2:E679-E679(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13."
Liu J., Xia H., Kim M., Xu L., Li Y., Zhang L., Cai Y., Norberg H.V., Zhang T., Furuya T., Jin M., Zhu Z., Wang H., Yu J., Li Y., Hao Y., Choi A., Ke H., Ma D., Yuan J.
Cell 147:223-234(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[11]"USP13 enzyme regulates Siah2 ligase stability and activity via noncatalytic ubiquitin-binding domains."
Scortegagna M., Subtil T., Qi J., Kim H., Zhao W., Gu W., Kluger H., Ronai Z.A.
J. Biol. Chem. 286:27333-27341(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SIAH2, MUTAGENESIS OF TRP-221; LYS-233; PHE-273; CYS-345; MET-664; MET-739; HIS-814 AND HIS-823.
[12]"Regulation of MITF stability by the USP13 deubiquitinase."
Zhao X., Fiske B., Kawakami A., Li J., Fisher D.E.
Nat. Commun. 2:414-414(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-345.
[13]"Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control."
Chen M., Gutierrez G.J., Ronai Z.A.
Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UFD1.
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin."
Zhang Y.H., Zhou C.J., Zhou Z.R., Song A.X., Hu H.Y.
PLoS ONE 6:E29362-E29362(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 188-301 AND 652-777, FUNCTION, DOMAIN, UBIQUITIN-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U75362 mRNA. Translation: AAC63405.1.
AK290338 mRNA. Translation: BAF83027.1.
AK302404 mRNA. Translation: BAG63715.1.
AC007687 Genomic DNA. No translation available.
AC125604 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78383.1.
CH471052 Genomic DNA. Translation: EAW78384.1.
BC016146 mRNA. Translation: AAH16146.1.
RefSeqNP_003931.2. NM_003940.2.
UniGeneHs.175322.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L80NMR-A188-301[»]
2LBCNMR-A652-777[»]
ProteinModelPortalQ92995.
SMRQ92995. Positions 26-863.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114465. 36 interactions.
IntActQ92995. 27 interactions.
MINTMINT-1195142.
STRING9606.ENSP00000263966.

Protein family/group databases

MEROPSC19.012.

PTM databases

PhosphoSiteQ92995.

Polymorphism databases

DMDM209572692.

Proteomic databases

PaxDbQ92995.
PRIDEQ92995.

Protocols and materials databases

DNASU8975.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263966; ENSP00000263966; ENSG00000058056. [Q92995-1]
ENST00000496897; ENSP00000417146; ENSG00000058056. [Q92995-2]
GeneID8975.
KEGGhsa:8975.
UCSCuc003fkh.3. human. [Q92995-1]

Organism-specific databases

CTD8975.
GeneCardsGC03P179370.
H-InvDBHIX0003883.
HGNCHGNC:12611. USP13.
HPAHPA004827.
MIM603591. gene.
neXtProtNX_Q92995.
PharmGKBPA37237.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5207.
HOGENOMHOG000162311.
HOVERGENHBG002833.
InParanoidQ92995.
KOK11836.
OMAPQQNGIS.
OrthoDBEOG7CNZF3.
PhylomeDBQ92995.
TreeFamTF300576.

Gene expression databases

ArrayExpressQ92995.
BgeeQ92995.
CleanExHS_USP13.
GenevestigatorQ92995.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR016652. Ubiquitinyl_hydrolase.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PIRSFPIRSF016308. UBP. 1 hit.
SMARTSM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS50030. UBA. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiUSP13.
GenomeRNAi8975.
NextBio33685.
PROQ92995.
SOURCESearch...

Entry information

Entry nameUBP13_HUMAN
AccessionPrimary (citable) accession number: Q92995
Secondary accession number(s): A8K2S3 expand/collapse secondary AC list , B4DYF3, D3DNS2, Q96B25
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2008
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM