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A6NJA2 (A6NJA2_HUMAN) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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).

Sequence similarities

Belongs to the peptidase C19 family. RuleBase RU004434

Contains USP domain. SAAS SAAS001394

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSP00000373083

Ontologies

Keywords
   Biological processUbl conjugation pathway RuleBase RU004434
   Molecular functionHydrolase
Protease
Thiol protease RuleBase RU004434
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
A6NJA2 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 31759DCBECB8EEE1

FASTA44851,086
        10         20         30         40         50         60 
MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG GTLKMELPCG 

        70         80         90        100        110        120 
LTNLGNTCYM NATVQCIRSV PELKDALKRY AGALRASGEM ASAQYITAAL RDLFDSMDKT 

       130        140        150        160        170        180 
SSSIPPIILL QFLHMAFPQF AEKGEQGQYL QQDANECWIQ MMRVLQQKLE AIEDDSVKET 

       190        200        210        220        230        240 
DSSSASAATP SKKKSLIDQF FGVEFETTMK CTESEEEEVT KGKENQLQLS CFINQEVKYL 

       250        260        270        280        290        300 
FTGLKLRLQE EITKQSPTLQ RNALYIKSSK ISRLPAYLTI QMVRFFYKEK ESVNAKVLKD 

       310        320        330        340        350        360 
VKFPLMLDMY ELCTPELQEK MVSFRSKFKD LEDKKVNQQP NTSDKKSSPQ KEVKYEPFSF 

       370        380        390        400        410        420 
ADDIGSNNCG YYDLQAVLTH QGRSSSSGHY VSWVKRKQDE WIKFDDDKVS IVTPEDILRL 

       430        440 
SGGGDWHIAY VLLYGPRRVE IMEEESEQ 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., O'Neill K., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[3]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer 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].
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]Ensembl
Submitted (JUL-2011) to UniProtKB
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP000845 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalA6NJA2.
SMRA6NJA2. Positions 6-437.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

DNASU9097.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000383589; ENSP00000373083; ENSG00000101557.

Organism-specific databases

HGNCHGNC:12612. USP14.
PharmGKBPA37238.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000202292.
HOVERGENHBG054185.

Gene expression databases

ArrayExpressA6NJA2.
BgeeA6NJA2.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
PROSITEPS00972. UCH_2_1. 1 hit.
PS00973. UCH_2_2. 1 hit.
PS50235. UCH_2_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio34093.

Entry information

Entry nameA6NJA2_HUMAN
AccessionPrimary (citable) accession number: A6NJA2
Entry history
Integrated into UniProtKB/TrEMBL: July 24, 2007
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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.