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Q9Y5T5

- UBP16_HUMAN

UniProt

Q9Y5T5 - UBP16_HUMAN

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Protein
Ubiquitin carboxyl-terminal hydrolase 16
Gene
USP16, MSTP039
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi24 – 241Zinc 1
Metal bindingi26 – 261Zinc 1
Metal bindingi48 – 481Zinc 2
Metal bindingi51 – 511Zinc 2
Metal bindingi74 – 741Zinc 3
Metal bindingi77 – 771Zinc 3
Metal bindingi82 – 821Zinc 2
Metal bindingi90 – 901Zinc 2
Metal bindingi94 – 941Zinc 3
Metal bindingi103 – 1031Zinc 3
Metal bindingi116 – 1161Zinc 1
Metal bindingi119 – 1191Zinc 1
Active sitei205 – 2051Nucleophile
Active sitei758 – 7581Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri60 – 12566UBP-typeUniRule annotation
Add
BLAST

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. histone binding Source: UniProtKB
  3. transcription coactivator activity Source: UniProtKB
  4. ubiquitin binding Source: UniProtKB
  5. ubiquitin thiolesterase activity Source: UniProtKB
  6. ubiquitin-specific protease activity Source: UniProtKB
  7. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: ProtInc
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. histone H2A K63-linked deubiquitination Source: UniProtKB
  4. histone deubiquitination Source: UniProtKB
  5. mitotic nuclear division Source: UniProtKB
  6. monoubiquitinated histone H2A deubiquitination Source: UniProtKB
  7. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  8. positive regulation of transcription, DNA-templated Source: UniProtKB
  9. positive regulation of translational elongation Source: UniProtKB
  10. protein homotetramerization Source: UniProtKB
  11. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  12. transcription, DNA-templated Source: UniProtKB-KW
  13. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC19.021.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:USP16
ORF Names:MSTP039
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:12614. USP16.

Subcellular locationi

Nucleus Inferred 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving USP16 is a cause of Chronic myelomonocytic leukemia. Inversion inv(21) (q21;q22) with RUNX1/AML1.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi205 – 2051C → S: Loss of enzyme activity. 3 Publications

Organism-specific databases

PharmGKBiPA37240.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 823823Ubiquitin carboxyl-terminal hydrolase 16UniRule annotation
PRO_0000080643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei415 – 4151Phosphoserine2 Publications
Modified residuei552 – 5521Phosphoserine3 Publications
Modified residuei554 – 5541Phosphothreonine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y5T5.
PaxDbiQ9Y5T5.
PRIDEiQ9Y5T5.

PTM databases

PhosphoSiteiQ9Y5T5.

Expressioni

Tissue specificityi

Present in all the tissues examined including fetal brain, lung, liver, kidney, and adult heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

ArrayExpressiQ9Y5T5.
BgeeiQ9Y5T5.
CleanExiHS_USP16.
GenevestigatoriQ9Y5T5.

Organism-specific databases

HPAiHPA021140.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi115848. 14 interactions.
IntActiQ9Y5T5. 4 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 304
Helixi33 – 408
Beta strandi45 – 473
Helixi49 – 524
Turni63 – 653
Beta strandi71 – 744
Turni75 – 773
Beta strandi80 – 823
Beta strandi86 – 883
Helixi90 – 967
Beta strandi105 – 1084
Turni109 – 1113
Beta strandi114 – 1163
Turni117 – 1204
Beta strandi121 – 1233
Helixi130 – 14213

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I50NMR-A22-143[»]
ProteinModelPortaliQ9Y5T5.
SMRiQ9Y5T5. Positions 22-427, 629-819.

Miscellaneous databases

EvolutionaryTraceiQ9Y5T5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini196 – 822627USP
Add
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Contains 1 USP domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5560.
HOVERGENiHBG062704.
InParanoidiQ9Y5T5.
KOiK11844.
OMAiECSIQHC.
OrthoDBiEOG7J9VNZ.
PhylomeDBiQ9Y5T5.
TreeFamiTF326075.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
HAMAPiMF_03062. UBP16.
InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y5T5-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGKKRTKGKT VPIDDSSETL EPVCRHIRKG LEQGNLKKAL VNVEWNICQD    50
CKTDNKVKDK AEEETEEKPS VWLCLKCGHQ GCGRNSQEQH ALKHYLTPRS 100
EPHCLVLSLD NWSVWCYVCD NEVQYCSSNQ LGQVVDYVRK QASITTPKPA 150
EKDNGNIELE NKKLEKESKN EQEREKKENM AKENPPMNSP CQITVKGLSN 200
LGNTCFFNAV MQNLSQTPVL RELLKEVKMS GTIVKIEPPD LALTEPLEIN 250
LEPPGPLTLA MSQFLNEMQE TKKGVVTPKE LFSQVCKKAV RFKGYQQQDS 300
QELLRYLLDG MRAEEHQRVS KGILKAFGNS TEKLDEELKN KVKDYEKKKS 350
MPSFVDRIFG GELTSMIMCD QCRTVSLVHE SFLDLSLPVL DDQSGKKSVN 400
DKNLKKTVED EDQDSEEEKD NDSYIKERSD IPSGTSKHLQ KKAKKQAKKQ 450
AKNQRRQQKI QGKVLHLNDI CTIDHPEDSE YEAEMSLQGE VNIKSNHISQ 500
EGVMHKEYCV NQKDLNGQAK MIESVTDNQK STEEVDMKNI NMDNDLEVLT 550
SSPTRNLNGA YLTEGSNGEV DISNGFKNLN LNAALHPDEI NIEILNDSHT 600
PGTKVYEVVN EDPETAFCTL ANREVFNTDE CSIQHCLYQF TRNEKLRDAN 650
KLLCEVCTRR QCNGPKANIK GERKHVYTNA KKQMLISLAP PVLTLHLKRF 700
QQAGFNLRKV NKHIKFPEIL DLAPFCTLKC KNVAEENTRV LYSLYGVVEH 750
SGTMRSGHYT AYAKARTANS HLSNLVLHGD IPQDFEMESK GQWFHISDTH 800
VQAVPTTKVL NSQAYLLFYE RIL 823
Length:823
Mass (Da):93,570
Last modified:November 1, 1999 - v1
Checksum:iC7D4175649BA3E31
GO
Isoform 2 (identifier: Q9Y5T5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-150: Missing.

Show »
Length:822
Mass (Da):93,499
Checksum:i36FD67E22FA078AB
GO
Isoform 3 (identifier: Q9Y5T5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MGKKRTKGKTVPIDDSSETL → MGSVAV
     150-150: Missing.

Note: No experimental confirmation available.

Show »
Length:808
Mass (Da):91,870
Checksum:iE4528720234CB7B7
GO
Isoform 4 (identifier: Q9Y5T5-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-310: Missing.

Note: No experimental confirmation available.

Show »
Length:513
Mass (Da):58,397
Checksum:i9AD260CF2FE530A9
GO
Isoform 5 (identifier: Q9Y5T5-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:408
Mass (Da):46,599
Checksum:i5B3EB300F72F4E04
GO

Sequence cautioni

The sequence AAG39290.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAG51175.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411Q → H.2 Publications
Corresponds to variant rs2274802 [ dbSNP | Ensembl ].
VAR_020388

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 310310Missing in isoform 4.
VSP_036713Add
BLAST
Alternative sequencei1 – 2020MGKKR…SSETL → MGSVAV in isoform 3.
VSP_036714Add
BLAST
Alternative sequencei150 – 1501Missing in isoform 2 and isoform 3.
VSP_036715
Alternative sequencei394 – 823430SGKKS…YERIL → VRLLNLFYSSRFFFL in isoform 5.
VSP_036716Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411Q → E in AAG39290. 1 Publication
Sequence conflicti297 – 2971Q → R in BAG51175. 1 Publication
Sequence conflicti348 – 3481K → E in BAD96604. 1 Publication
Sequence conflicti350 – 3501S → P in BAD96401. 1 Publication
Sequence conflicti480 – 4812EY → DN in AAH30777. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13583.1. [Q9Y5T5-1]
CCDS42912.1. [Q9Y5T5-2]
RefSeqiNP_001001992.1. NM_001001992.1. [Q9Y5T5-2]
NP_001027582.1. NM_001032410.1. [Q9Y5T5-1]
NP_006438.1. NM_006447.2. [Q9Y5T5-1]
UniGeneiHs.99819.

Genome annotation databases

EnsembliENST00000334352; ENSP00000334808; ENSG00000156256. [Q9Y5T5-1]
ENST00000399975; ENSP00000382857; ENSG00000156256. [Q9Y5T5-2]
ENST00000399976; ENSP00000382858; ENSG00000156256. [Q9Y5T5-1]
GeneIDi10600.
KEGGihsa:10600.
UCSCiuc002ymw.3. human. [Q9Y5T5-1]
uc002ymx.3. human. [Q9Y5T5-2]
uc011acm.2. human. [Q9Y5T5-3]

Polymorphism databases

DMDMi6686071.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS13583.1. [Q9Y5T5-1 ]
CCDS42912.1. [Q9Y5T5-2 ]
RefSeqi NP_001001992.1. NM_001001992.1. [Q9Y5T5-2 ]
NP_001027582.1. NM_001032410.1. [Q9Y5T5-1 ]
NP_006438.1. NM_006447.2. [Q9Y5T5-1 ]
UniGenei Hs.99819.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2I50 NMR - A 22-143 [» ]
ProteinModelPortali Q9Y5T5.
SMRi Q9Y5T5. Positions 22-427, 629-819.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115848. 14 interactions.
IntActi Q9Y5T5. 4 interactions.

Protein family/group databases

MEROPSi C19.021.

PTM databases

PhosphoSitei Q9Y5T5.

Polymorphism databases

DMDMi 6686071.

Proteomic databases

MaxQBi Q9Y5T5.
PaxDbi Q9Y5T5.
PRIDEi Q9Y5T5.

Protocols and materials databases

DNASUi 10600.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334352 ; ENSP00000334808 ; ENSG00000156256 . [Q9Y5T5-1 ]
ENST00000399975 ; ENSP00000382857 ; ENSG00000156256 . [Q9Y5T5-2 ]
ENST00000399976 ; ENSP00000382858 ; ENSG00000156256 . [Q9Y5T5-1 ]
GeneIDi 10600.
KEGGi hsa:10600.
UCSCi uc002ymw.3. human. [Q9Y5T5-1 ]
uc002ymx.3. human. [Q9Y5T5-2 ]
uc011acm.2. human. [Q9Y5T5-3 ]

Organism-specific databases

CTDi 10600.
GeneCardsi GC21P030396.
H-InvDB HIX0023011.
HGNCi HGNC:12614. USP16.
HPAi HPA021140.
MIMi 604735. gene.
neXtProti NX_Q9Y5T5.
PharmGKBi PA37240.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5560.
HOVERGENi HBG062704.
InParanoidi Q9Y5T5.
KOi K11844.
OMAi ECSIQHC.
OrthoDBi EOG7J9VNZ.
PhylomeDBi Q9Y5T5.
TreeFami TF326075.

Miscellaneous databases

ChiTaRSi USP16. human.
EvolutionaryTracei Q9Y5T5.
GeneWikii USP16.
GenomeRNAii 10600.
NextBioi 40254.
PROi Q9Y5T5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y5T5.
Bgeei Q9Y5T5.
CleanExi HS_USP16.
Genevestigatori Q9Y5T5.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
HAMAPi MF_03062. UBP16.
InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view ]
Pfami PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view ]
PROSITEi PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. Cited for: CHROMOSOMAL REARRANGEMENT.
  12. 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. 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. 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.

Entry informationi

Entry nameiUBP16_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5T5
Secondary accession number(s): A8MU43
, B3KN13, B4DFV8, B4DY37, D3DSD9, Q53GP7, Q53HA0, Q5VKN8, Q8NEL3, Q9H3E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 130 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

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 (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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