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Q9Y5T5 (UBP16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 16

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 16
Ubiquitin thioesterase 16
Ubiquitin-processing protease UBP-M
Ubiquitin-specific-processing protease 16
Gene names
Name:USP16
ORF Names:MSTP039
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length823 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. Ref.1 Ref.9 Ref.10

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). Ref.10

Subunit structure

Homotetramer. Ref.10

Subcellular location

Nucleus Probable Ref.10.

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. Ref.1

Domain

The UBP-type zinc finger binds 3 zinc ions that form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. It recognizes the C-terminal tail of free ubiquitin. HAMAP-Rule MF_03062

Post-translational modification

Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. Phosphorylation by AURKB enhances the deubiquitinase activity. Ref.1

Involvement in disease

A chromosomal aberration involving USP16 is a cause of Chronic myelomonocytic leukemia. Inversion inv21 (q21;q22) with RUNX1/AML1.

Miscellaneous

USP16 may contribute to somatic stem cell defects observed in Down syndrome. USP16 is triplicated in Down syndrome and its overexpression may contribute to proliferation defects in stem cells. Reduction of USP16 levels results in increased proliferation capacity of Down syndrome fibroblasts (Ref.18).

Sequence similarities

Belongs to the peptidase C19 family. USP16 subfamily.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Sequence caution

The sequence AAG39290.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAG51175.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Chromatin regulator
Hydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Traceable author statement Ref.1. Source: ProtInc

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 20550933. Source: UniProtKB

histone H2A K63-linked deubiquitination

Inferred from mutant phenotype PubMed 20550933. Source: UniProtKB

histone deubiquitination

Inferred from direct assay Ref.10. Source: UniProtKB

mitotic nuclear division

Inferred from direct assay Ref.10. Source: UniProtKB

monoubiquitinated histone H2A deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of translational elongation

Inferred from mutant phenotype PubMed 20550933. Source: UniProtKB

protein homotetramerization

Inferred from physical interaction Ref.10. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Traceable author statement Ref.1. Source: ProtInc

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functioncysteine-type endopeptidase activity

Inferred from mutant phenotype Ref.10. Source: UniProtKB

histone binding

Inferred from direct assay Ref.10. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.10. Source: UniProtKB

ubiquitin binding

Inferred from direct assay Ref.19. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from direct assay Ref.10. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.10. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.19. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5T5-1)

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: Q9Y5T5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     150-150: Missing.
Isoform 3 (identifier: Q9Y5T5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MGKKRTKGKTVPIDDSSETL → MGSVAV
     150-150: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9Y5T5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-310: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q9Y5T5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     394-823: SGKKSVNDKN...AYLLFYERIL → VRLLNLFYSSRFFFL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 823823Ubiquitin carboxyl-terminal hydrolase 16 HAMAP-Rule MF_03062
PRO_0000080643

Regions

Domain196 – 822627USP
Zinc finger60 – 12566UBP-type HAMAP-Rule MF_03062

Sites

Active site2051Nucleophile
Active site7581Proton acceptor By similarity
Metal binding241Zinc 1
Metal binding261Zinc 1
Metal binding481Zinc 2
Metal binding511Zinc 2
Metal binding741Zinc 3
Metal binding771Zinc 3
Metal binding821Zinc 2
Metal binding901Zinc 2
Metal binding941Zinc 3
Metal binding1031Zinc 3
Metal binding1161Zinc 1
Metal binding1191Zinc 1

Amino acid modifications

Modified residue4151Phosphoserine Ref.12 Ref.17
Modified residue5521Phosphoserine Ref.12 Ref.14 Ref.15
Modified residue5541Phosphothreonine Ref.15

Natural variations

Alternative sequence1 – 310310Missing in isoform 4.
VSP_036713
Alternative sequence1 – 2020MGKKR…SSETL → MGSVAV in isoform 3.
VSP_036714
Alternative sequence1501Missing in isoform 2 and isoform 3.
VSP_036715
Alternative sequence394 – 823430SGKKS…YERIL → VRLLNLFYSSRFFFL in isoform 5.
VSP_036716
Natural variant1411Q → H. Ref.3 Ref.7
Corresponds to variant rs2274802 [ dbSNP | Ensembl ].
VAR_020388

Experimental info

Mutagenesis2051C → S: Loss of enzyme activity. Ref.1 Ref.9 Ref.10
Sequence conflict1411Q → E in AAG39290. Ref.8
Sequence conflict2971Q → R in BAG51175. Ref.3
Sequence conflict3481K → E in BAD96604. Ref.4
Sequence conflict3501S → P in BAD96401. Ref.4
Sequence conflict480 – 4812EY → DN in AAH30777. Ref.7

Secondary structure

............................. 823
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1999. Version 1.
Checksum: C7D4175649BA3E31

FASTA82393,570
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 36FD67E22FA078AB
Show »

FASTA82293,499
Isoform 3 [UniParc].

Checksum: E4528720234CB7B7
Show »

FASTA80891,870
Isoform 4 [UniParc].

Checksum: 9AD260CF2FE530A9
Show »

FASTA51358,397
Isoform 5 [UniParc].

Checksum: 5B3EB300F72F4E04
Show »

FASTA40846,599

References

« Hide 'large scale' references
[1]"A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division."
Cai S.-Y., Babbitt R.W., Marchesi V.T.
Proc. Natl. Acad. Sci. U.S.A. 96:2828-2833(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF CYS-205.
[2]Grimbert P., Pawlak A., Sahali D.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[3]"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 3 AND 4), VARIANT HIS-141.
Tissue: Amygdala, Teratocarcinoma and Testis.
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Liver.
[5]"The DNA sequence of human chromosome 21."
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. expand/collapse author list , 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.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[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] (ISOFORM 2), VARIANT HIS-141.
Tissue: Testis.
[8]Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., Liu L.S., Ding J.F. expand/collapse author list , Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-823.
Tissue: Aorta.
[9]"Caspase-dependent deubiquitination of monoubiquitinated nucleosomal histone H2A induced by diverse apoptogenic stimuli."
Mimnaugh E.G., Kayastha G., McGovern N.B., Hwang S.G., Marcu M.G., Trepel J., Cai S.-Y., Marchesi V.T., Neckers L.
Cell Death Differ. 8:1182-1196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY FUNCTION, MUTAGENESIS OF CYS-205.
[10]"Regulation of cell cycle progression and gene expression by H2A deubiquitination."
Joo H.-Y., Zhai L., Yang C., Nie S., Erdjument-Bromage H., Tempst P., Chang C., Wang H.
Nature 449:1068-1072(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-205.
[11]"Genome profiling of chronic myelomonocytic leukemia: frequent alterations of RAS and RUNX1 genes."
Gelsi-Boyer V., Trouplin V., Adelaide J., Aceto N., Remy V., Pinson S., Houdayer C., Arnoulet C., Sainty D., Bentires-Alj M., Olschwang S., Vey N., Mozziconacci M.-J., Birnbaum D., Chaffanet M.
BMC Cancer 8:299-299(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL REARRANGEMENT.
[12]"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 SER-415 AND SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND THR-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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 SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Usp16 contributes to somatic stem-cell defects in Down's syndrome."
Adorno M., Sikandar S., Mitra S.S., Kuo A., Nicolis Di Robilant B., Haro-Acosta V., Ouadah Y., Quarta M., Rodriguez J., Qian D., Reddy V.M., Cheshier S., Garner C.C., Clarke M.F.
Nature 501:380-384(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN DOWN SYNDROME.
[19]"Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin."
Pai M.-T., Tzeng S.-R., Kovacs J.J., Keaton M.A., Li S.S.-C., Yao T.-P., Zhou P.
J. Mol. Biol. 370:290-302(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 22-143, ZINC-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF126736 mRNA. Translation: AAD20949.1.
AY333928 mRNA. Translation: AAR13293.1.
AK023247 mRNA. Translation: BAG51175.1. Different initiation.
AK302247 mRNA. Translation: BAG63599.1.
AK294284 mRNA. Translation: BAG57569.1.
AK222681 mRNA. Translation: BAD96401.1.
AK222884 mRNA. Translation: BAD96604.1.
AL163249 Genomic DNA. Translation: CAB90432.1.
AF129075 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09927.1.
CH471079 Genomic DNA. Translation: EAX09929.1.
BC030777 mRNA. Translation: AAH30777.1.
AF113219 mRNA. Translation: AAG39290.1. Different initiation.
CCDSCCDS13583.1. [Q9Y5T5-1]
CCDS42912.1. [Q9Y5T5-2]
RefSeqNP_001001992.1. NM_001001992.1. [Q9Y5T5-2]
NP_001027582.1. NM_001032410.1. [Q9Y5T5-1]
NP_006438.1. NM_006447.2. [Q9Y5T5-1]
UniGeneHs.99819.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I50NMR-A22-143[»]
ProteinModelPortalQ9Y5T5.
SMRQ9Y5T5. Positions 22-427, 629-819.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115848. 14 interactions.
IntActQ9Y5T5. 4 interactions.

Protein family/group databases

MEROPSC19.021.

PTM databases

PhosphoSiteQ9Y5T5.

Polymorphism databases

DMDM6686071.

Proteomic databases

MaxQBQ9Y5T5.
PaxDbQ9Y5T5.
PRIDEQ9Y5T5.

Protocols and materials databases

DNASU10600.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334352; ENSP00000334808; ENSG00000156256. [Q9Y5T5-1]
ENST00000399975; ENSP00000382857; ENSG00000156256. [Q9Y5T5-2]
ENST00000399976; ENSP00000382858; ENSG00000156256. [Q9Y5T5-1]
GeneID10600.
KEGGhsa:10600.
UCSCuc002ymw.3. human. [Q9Y5T5-1]
uc002ymx.3. human. [Q9Y5T5-2]
uc011acm.2. human. [Q9Y5T5-3]

Organism-specific databases

CTD10600.
GeneCardsGC21P030396.
H-InvDBHIX0023011.
HGNCHGNC:12614. USP16.
HPAHPA021140.
MIM604735. gene.
neXtProtNX_Q9Y5T5.
PharmGKBPA37240.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5560.
HOVERGENHBG062704.
InParanoidQ9Y5T5.
KOK11844.
OMAECSIQHC.
OrthoDBEOG7J9VNZ.
PhylomeDBQ9Y5T5.
TreeFamTF326075.

Gene expression databases

ArrayExpressQ9Y5T5.
BgeeQ9Y5T5.
CleanExHS_USP16.
GenevestigatorQ9Y5T5.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
HAMAPMF_03062. UBP16.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP16. human.
EvolutionaryTraceQ9Y5T5.
GeneWikiUSP16.
GenomeRNAi10600.
NextBio40254.
PROQ9Y5T5.
SOURCESearch...

Entry information

Entry nameUBP16_HUMAN
AccessionPrimary (citable) accession number: Q9Y5T5
Secondary accession number(s): A8MU43 expand/collapse secondary AC list , B3KN13, B4DFV8, B4DY37, D3DSD9, Q53GP7, Q53HA0, Q5VKN8, Q8NEL3, Q9H3E6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 129 of the entry and version 1 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM