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UniProtKB/Swiss-Prot entry Q9Y5T5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UBP16_HUMAN
Primary accession number Q9Y5T5
Secondary accession number Q8NEL3
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 71)
Name and origin of the protein
Protein name Ubiquitin carboxyl-terminal hydrolase 16
Synonyms EC 3.1.2.15
Ubiquitin thioesterase 16
Ubiquitin-specific-processing protease 16
Deubiquitinating enzyme 16
Ubiquitin-processing protease UBP-M
Gene name
Name: USP16
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.96.6.2828; PubMed=10077596 [NCBI, ExPASy, EBI, Israel, Japan]
Cai S.-Y., Babbitt R.W., Marchesi V.T.;
"A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division.";
Proc. Natl. Acad. Sci. U.S.A. 96:2828-2833(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/35012518; PubMed=10830953 [NCBI, ExPASy, EBI, Israel, Japan]
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-141.
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415 AND SER-552, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
  • FUNCTION: May deubiquitinate one or more critical proteins that are involved in the condensation of mitotic chromosomes, possibly acting selectively on histones H2A and H2B, the major ubiquitinated proteins of chromatin. It is able to deubiquitinate histone H2A in vitro, the phosphorylated form of the protein is also enzymatically active.
  • CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.
  • TISSUE SPECIFICITY: Present in all the tissues examined including fetal brain, lung, liver, kidney, and adult heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
  • PTM: Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition.
  • SIMILARITY: Belongs to the peptidase C19 family [view classification].
  • SIMILARITY: Contains 1 UBP-type zinc finger.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF126736; AAD20949.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL163249; CAB90432.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030777; AAH30777.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001001992.1; -.
NP_001027582.1; -.
NP_006438.1; -.
UniGene Hs.99819
3D structure databases
PDB
2I50; NMR; -; A=22-143.[ExPASy / RCSB / EBI]
PDBsum 2I50; -.
ModBase Q9Y5T5.
Protein family/group databases
MEROPS C19.021; -.
PTM databases
PhosphoSite Q9Y5T5; -.
Organism-specific databases
H-InvDB HIX0023011; -.
HGNC HGNC:12614; USP16.
GenAtlas USP16.
MIM 604735; gene. [NCBI / EBI]
PharmGKB PA38475; -.
GeneCards Q9Y5T5.
Gene expression databases
ArrayExpress Q9Y5T5; -.
CleanEx HS_USP16; -.
GermOnline ENSG00000156256; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0004197; Molecular function: cysteine-type endopeptidase activity (traceable author statement from ProtInc).
GO:0004221; Molecular function: ubiquitin thiolesterase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0007049; Biological process: cell cycle (traceable author statement from ProtInc).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001394; Peptidase_C19.
IPR001607; Znf_UBP.
Graphical view of domain structure.
Pfam PF00443; UCH; 1.
PF02148; zf-UBP; 1.
Pfam graphical view of domain structure.
PROSITE PS00972; UCH_2_1; 1.
PS00973; UCH_2_2; 1.
PS50235; UCH_2_3; 1.
PS50271; ZF_UBP; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9Y5T5.
Genome annotation databases
Ensembl ENSG00000156256; Homo sapiens. [Contig view]
GeneID 10600; -.
KEGG hsa:10600; -.
Phylogenomic databases
HOGENOM Q9Y5T5; -.
HOVERGEN Q9Y5T5; -.
Other
NextBio 40254; -.
SOURCE USP16; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Hydrolase; Metal-binding; Phosphoprotein; Polymorphism; Protease; Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   823  823     Ubiquitin carboxyl-terminal hydrolase 16. PRO_0000080643
ZN_FING   60   125  66     UBP-type. 
ACT_SITE   205   205        By similarity. 
ACT_SITE   750   750        By similarity. 
ACT_SITE   758   758        By similarity. 
MOD_RES   415   415        Phosphoserine. 
MOD_RES   552   552        Phosphoserine. 
VARIANT   141   141  1     Q -> H (in dbSNP:rs2274802 [NCBI]). VAR_020388 
MUTAGEN   205   205        C->S: Unable to deubiquitinate H2A/H2B. 
CONFLICT   150   150        Missing (in Ref. 3; AAH30777). 
CONFLICT   480   481        EY -> DN (in Ref. 3; AAH30777). 
Sequence information
Length: 823 AA [This is the length of the unprocessed precursor] Molecular weight: 93570 Da [This is the MW of the unprocessed precursor] CRC64: C7D4175649BA3E31 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGKKRTKGKT VPIDDSSETL EPVCRHIRKG LEQGNLKKAL VNVEWNICQD CKTDNKVKDK 

        70         80         90        100        110        120 
AEEETEEKPS VWLCLKCGHQ GCGRNSQEQH ALKHYLTPRS EPHCLVLSLD NWSVWCYVCD 

       130        140        150        160        170        180 
NEVQYCSSNQ LGQVVDYVRK QASITTPKPA EKDNGNIELE NKKLEKESKN EQEREKKENM 

       190        200        210        220        230        240 
AKENPPMNSP CQITVKGLSN LGNTCFFNAV MQNLSQTPVL RELLKEVKMS GTIVKIEPPD 

       250        260        270        280        290        300 
LALTEPLEIN LEPPGPLTLA MSQFLNEMQE TKKGVVTPKE LFSQVCKKAV RFKGYQQQDS 

       310        320        330        340        350        360 
QELLRYLLDG MRAEEHQRVS KGILKAFGNS TEKLDEELKN KVKDYEKKKS MPSFVDRIFG 

       370        380        390        400        410        420 
GELTSMIMCD QCRTVSLVHE SFLDLSLPVL DDQSGKKSVN DKNLKKTVED EDQDSEEEKD 

       430        440        450        460        470        480 
NDSYIKERSD IPSGTSKHLQ KKAKKQAKKQ AKNQRRQQKI QGKVLHLNDI CTIDHPEDSE 

       490        500        510        520        530        540 
YEAEMSLQGE VNIKSNHISQ EGVMHKEYCV NQKDLNGQAK MIESVTDNQK STEEVDMKNI 

       550        560        570        580        590        600 
NMDNDLEVLT SSPTRNLNGA YLTEGSNGEV DISNGFKNLN LNAALHPDEI NIEILNDSHT 

       610        620        630        640        650        660 
PGTKVYEVVN EDPETAFCTL ANREVFNTDE CSIQHCLYQF TRNEKLRDAN KLLCEVCTRR 

       670        680        690        700        710        720 
QCNGPKANIK GERKHVYTNA KKQMLISLAP PVLTLHLKRF QQAGFNLRKV NKHIKFPEIL 

       730        740        750        760        770        780 
DLAPFCTLKC KNVAEENTRV LYSLYGVVEH SGTMRSGHYT AYAKARTANS HLSNLVLHGD 

       790        800        810        820 
IPQDFEMESK GQWFHISDTH VQAVPTTKVL NSQAYLLFYE RIL 

Q9Y5T5 in FASTA format

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View entry in raw text format (no links)
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