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Q9Y4E8

- UBP15_HUMAN

UniProt

Q9Y4E8 - UBP15_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 15

Gene

USP15

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.7 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).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei298 – 2981Nucleophile
Active sitei891 – 8911Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. SMAD binding Source: UniProtKB
  4. transforming growth factor beta receptor binding Source: UniProtKB
  5. ubiquitin-specific protease activity Source: UniProtKB
  6. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. BMP signaling pathway Source: UniProtKB
  2. monoubiquitinated protein deubiquitination Source: UniProtKB
  3. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
  4. pathway-restricted SMAD protein phosphorylation Source: UniProtKB
  5. protein deubiquitination Source: UniProtKB
  6. transforming growth factor beta receptor signaling pathway Source: UniProtKB
  7. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_120727. Downregulation of TGF-beta receptor signaling.

Protein family/group databases

MEROPSiC19.022.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 15 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 15
Ubiquitin thioesterase 15
Ubiquitin-specific-processing protease 15
Unph-2
Unph4
Gene namesi
Name:USP15
Synonyms:KIAA0529
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:12613. USP15.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi298 – 2981C → A: Loss of enzyme activity. 3 Publications
Mutagenesisi812 – 8121C → A: Loss of activity towards polyubiquitin. 2 Publications

Organism-specific databases

PharmGKBiPA37239.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 981980Ubiquitin carboxyl-terminal hydrolase 15PRO_0000080641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei229 – 2291Phosphoserine5 Publications
Modified residuei242 – 2421Phosphoserine1 Publication
Modified residuei961 – 9611Phosphoserine2 Publications
Modified residuei965 – 9651Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated. Phosphorylation protects against ubiquitination and subsequent degradation by the proteasome.6 Publications
Ubiquitinated, leading to degradation by the proteasome.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y4E8.
PaxDbiQ9Y4E8.
PRIDEiQ9Y4E8.

PTM databases

PhosphoSiteiQ9Y4E8.

Expressioni

Tissue specificityi

Expressed in skeletal muscle, kidney, heart, placenta, liver, thymus, lung, and ovary, with little or no expression in other tissues.

Gene expression databases

BgeeiQ9Y4E8.
CleanExiHS_USP15.
ExpressionAtlasiQ9Y4E8. baseline and differential.
GenevestigatoriQ9Y4E8.

Organism-specific databases

HPAiHPA006237.

Interactioni

Subunit structurei

A homodimer structure has been reported; however it is unclear whether the protein form a homodimer in vivo (PubMed:22001210). Identified in a complex with the COP9 signalosome complex (CSN). Interacts with SMAD1, SMAD2 and SMAD3; the interaction is direct. Forms a complex with SMURF2 and SMAD7. Interacts with TGFBR1. Interacts with human papillomavirus type 16 protein E6.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-1043104,EBI-1043104

Protein-protein interaction databases

BioGridi115283. 122 interactions.
DIPiDIP-50239N.
IntActiQ9Y4E8. 35 interactions.
MINTiMINT-4542165.
STRINGi9606.ENSP00000258123.

Structurei

Secondary structure

1
981
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi9 – 1911Combined sources
Beta strandi29 – 346Combined sources
Helixi35 – 4511Combined sources
Turni46 – 483Combined sources
Turni53 – 564Combined sources
Helixi58 – 603Combined sources
Helixi68 – 703Combined sources
Beta strandi73 – 764Combined sources
Turni86 – 883Combined sources
Beta strandi89 – 935Combined sources
Helixi94 – 10411Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi134 – 1407Combined sources
Beta strandi143 – 15210Combined sources
Helixi158 – 16811Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi177 – 1848Combined sources
Beta strandi187 – 1904Combined sources
Helixi198 – 2014Combined sources
Beta strandi208 – 2136Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W6VNMR-A1-120[»]
3LMNX-ray2.15A/B1-133[»]
3PPAX-ray2.35A6-223[»]
3PV1X-ray2.60A/B1-223[»]
3T9LX-ray1.50A1-222[»]
4A3OX-ray2.20A/B4-223[»]
4A3PX-ray1.40A6-223[»]
ProteinModelPortaliQ9Y4E8.
SMRiQ9Y4E8. Positions 6-222, 285-470, 786-934.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y4E8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 118112DUSPPROSITE-ProRule annotationAdd
BLAST
Domaini289 – 933645USPAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 DUSP domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Phylogenomic databases

eggNOGiCOG5560.
GeneTreeiENSGT00670000097750.
HOGENOMiHOG000264375.
HOVERGENiHBG000864.
InParanoidiQ9Y4E8.
KOiK11835.
OMAiRYVKTCT.
OrthoDBiEOG77Q4VW.
PhylomeDBiQ9Y4E8.
TreeFamiTF106276.

Family and domain databases

Gene3Di3.30.2230.10. 1 hit.
InterProiIPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR028135. Ub_USP-typ.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00695. DUSP. 1 hit.
[Graphical view]
SUPFAMiSSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55205. SSF55205. 1 hit.
PROSITEiPS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y4E8-1) [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

        10         20         30         40         50
MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW
60 70 80 90 100
DKYQMGDQNV YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL
110 120 130 140 150
VSWYTLMEGQ EPIARKVVEQ GMFVKHCKVE VYLTELKLCE NGNMNNVVTR
160 170 180 190 200
RFSKADTIDT IEKEIRKIFS IPDEKETRLW NKYMSNTFEP LNKPDSTIQD
210 220 230 240 250
AGLYQGQVLV IEQKNEDGTW PRGPSTPKSP GASNFSTLPK ISPSSLSNNY
260 270 280 290 300
NNMNNRNVKN SNYCLPSYTA YKNYDYSEPG RNNEQPGLCG LSNLGNTCFM
310 320 330 340 350
NSAIQCLSNT PPLTEYFLND KYQEELNFDN PLGMRGEIAK SYAELIKQMW
360 370 380 390 400
SGKFSYVTPR AFKTQVGRFA PQFSGYQQQD CQELLAFLLD GLHEDLNRIR
410 420 430 440 450
KKPYIQLKDA DGRPDKVVAE EAWENHLKRN DSIIVDIFHG LFKSTLVCPE
460 470 480 490 500
CAKISVTFDP FCYLTLPLPM KKERTLEVYL VRMDPLTKPM QYKVVVPKIG
510 520 530 540 550
NILDLCTALS ALSGIPADKM IVTDIYNHRF HRIFAMDENL SSIMERDDIY
560 570 580 590 600
VFEININRTE DTEHVIIPVC LREKFRHSSY THHTGSSLFG QPFLMAVPRN
610 620 630 640 650
NTEDKLYNLL LLRMCRYVKI STETEETEGS LHCCKDQNIN GNGPNGIHEE
660 670 680 690 700
GSPSEMETDE PDDESSQDQE LPSENENSQS EDSVGGDNDS ENGLCTEDTC
710 720 730 740 750
KGQLTGHKKR LFTFQFNNLG NTDINYIKDD TRHIRFDDRQ LRLDERSFLA
760 770 780 790 800
LDWDPDLKKR YFDENAAEDF EKHESVEYKP PKKPFVKLKD CIELFTTKEK
810 820 830 840 850
LGAEDPWYCP NCKEHQQATK KLDLWSLPPV LVVHLKRFSY SRYMRDKLDT
860 870 880 890 900
LVDFPINDLD MSEFLINPNA GPCRYNLIAV SNHYGGMGGG HYTAFAKNKD
910 920 930 940 950
DGKWYYFDDS SVSTASEDQI VSKAAYVLFY QRQDTFSGTG FFPLDRETKG
960 970 980
ASAATGIPLE SDEDSNDNDN DIENENCMHT N
Length:981
Mass (Da):112,419
Last modified:February 12, 2003 - v3
Checksum:iE81FEB9DE57F7089
GO
Isoform 2 (identifier: Q9Y4E8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     228-256: Missing.

Show »
Length:952
Mass (Da):109,297
Checksum:i852ED3768FB5725A
GO
Isoform 3 (identifier: Q9Y4E8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     217-256: DGTWPRGPSTPKSPGASNFSTLPKISPSSLSNNYNNMNNR → QKNEDGTWPRGPSTP

Show »
Length:956
Mass (Da):109,796
Checksum:iF9F83D3886404B11
GO
Isoform 4 (identifier: Q9Y4E8-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-235: SPGASNF → KPLEQSC
     236-981: Missing.

Show »
Length:235
Mass (Da):27,094
Checksum:iF69B0D2783E2A443
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti559 – 5591T → A in AAG28973. 1 PublicationCurated
Sequence conflicti747 – 7471S → F in AAI25124. (PubMed:15489334)Curated
Sequence conflicti968 – 9681N → H in AAG28973. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei217 – 25640DGTWP…NMNNR → QKNEDGTWPRGPSTP in isoform 3. 1 PublicationVSP_005260Add
BLAST
Alternative sequencei228 – 25629Missing in isoform 2. 3 PublicationsVSP_005261Add
BLAST
Alternative sequencei229 – 2357SPGASNF → KPLEQSC in isoform 4. 2 PublicationsVSP_045165
Alternative sequencei236 – 981746Missing in isoform 4. 2 PublicationsVSP_045166Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106069 mRNA. Translation: AAD52099.1.
AB011101 mRNA. Translation: BAA25455.2.
AF153604 mRNA. Translation: AAD41086.1.
AK023703 mRNA. Translation: BAB14648.1.
AK292337 mRNA. Translation: BAF85026.1.
AC048342 Genomic DNA. No translation available.
AC079035 Genomic DNA. No translation available.
AC117370 Genomic DNA. No translation available.
BC020688 mRNA. Translation: AAH20688.1.
BC063454 mRNA. Translation: AAH63454.1.
BC125123 mRNA. Translation: AAI25124.1.
AF013990 mRNA. Translation: AAG28973.1.
CCDSiCCDS58250.1. [Q9Y4E8-4]
CCDS58251.1. [Q9Y4E8-1]
CCDS8963.1. [Q9Y4E8-2]
RefSeqiNP_001239007.1. NM_001252078.1. [Q9Y4E8-1]
NP_001239008.1. NM_001252079.1. [Q9Y4E8-4]
NP_006304.1. NM_006313.2. [Q9Y4E8-2]
UniGeneiHs.434951.

Genome annotation databases

EnsembliENST00000280377; ENSP00000280377; ENSG00000135655. [Q9Y4E8-1]
ENST00000312635; ENSP00000309240; ENSG00000135655. [Q9Y4E8-4]
ENST00000353364; ENSP00000258123; ENSG00000135655. [Q9Y4E8-2]
GeneIDi9958.
KEGGihsa:9958.
UCSCiuc001sra.3. human.
uc001srb.2. human. [Q9Y4E8-2]
uc001src.2. human. [Q9Y4E8-1]

Polymorphism databases

DMDMi28381406.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106069 mRNA. Translation: AAD52099.1 .
AB011101 mRNA. Translation: BAA25455.2 .
AF153604 mRNA. Translation: AAD41086.1 .
AK023703 mRNA. Translation: BAB14648.1 .
AK292337 mRNA. Translation: BAF85026.1 .
AC048342 Genomic DNA. No translation available.
AC079035 Genomic DNA. No translation available.
AC117370 Genomic DNA. No translation available.
BC020688 mRNA. Translation: AAH20688.1 .
BC063454 mRNA. Translation: AAH63454.1 .
BC125123 mRNA. Translation: AAI25124.1 .
AF013990 mRNA. Translation: AAG28973.1 .
CCDSi CCDS58250.1. [Q9Y4E8-4 ]
CCDS58251.1. [Q9Y4E8-1 ]
CCDS8963.1. [Q9Y4E8-2 ]
RefSeqi NP_001239007.1. NM_001252078.1. [Q9Y4E8-1 ]
NP_001239008.1. NM_001252079.1. [Q9Y4E8-4 ]
NP_006304.1. NM_006313.2. [Q9Y4E8-2 ]
UniGenei Hs.434951.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W6V NMR - A 1-120 [» ]
3LMN X-ray 2.15 A/B 1-133 [» ]
3PPA X-ray 2.35 A 6-223 [» ]
3PV1 X-ray 2.60 A/B 1-223 [» ]
3T9L X-ray 1.50 A 1-222 [» ]
4A3O X-ray 2.20 A/B 4-223 [» ]
4A3P X-ray 1.40 A 6-223 [» ]
ProteinModelPortali Q9Y4E8.
SMRi Q9Y4E8. Positions 6-222, 285-470, 786-934.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115283. 122 interactions.
DIPi DIP-50239N.
IntActi Q9Y4E8. 35 interactions.
MINTi MINT-4542165.
STRINGi 9606.ENSP00000258123.

Protein family/group databases

MEROPSi C19.022.

PTM databases

PhosphoSitei Q9Y4E8.

Polymorphism databases

DMDMi 28381406.

Proteomic databases

MaxQBi Q9Y4E8.
PaxDbi Q9Y4E8.
PRIDEi Q9Y4E8.

Protocols and materials databases

DNASUi 9958.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000280377 ; ENSP00000280377 ; ENSG00000135655 . [Q9Y4E8-1 ]
ENST00000312635 ; ENSP00000309240 ; ENSG00000135655 . [Q9Y4E8-4 ]
ENST00000353364 ; ENSP00000258123 ; ENSG00000135655 . [Q9Y4E8-2 ]
GeneIDi 9958.
KEGGi hsa:9958.
UCSCi uc001sra.3. human.
uc001srb.2. human. [Q9Y4E8-2 ]
uc001src.2. human. [Q9Y4E8-1 ]

Organism-specific databases

CTDi 9958.
GeneCardsi GC12P062706.
H-InvDB HIX0010773.
HGNCi HGNC:12613. USP15.
HPAi HPA006237.
MIMi 604731. gene.
neXtProti NX_Q9Y4E8.
PharmGKBi PA37239.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5560.
GeneTreei ENSGT00670000097750.
HOGENOMi HOG000264375.
HOVERGENi HBG000864.
InParanoidi Q9Y4E8.
KOi K11835.
OMAi RYVKTCT.
OrthoDBi EOG77Q4VW.
PhylomeDBi Q9Y4E8.
TreeFami TF106276.

Enzyme and pathway databases

Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.

Miscellaneous databases

ChiTaRSi USP15. human.
EvolutionaryTracei Q9Y4E8.
GeneWikii USP15.
GenomeRNAii 9958.
NextBioi 37576.
PROi Q9Y4E8.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y4E8.
CleanExi HS_USP15.
ExpressionAtlasi Q9Y4E8. baseline and differential.
Genevestigatori Q9Y4E8.

Family and domain databases

Gene3Di 3.30.2230.10. 1 hit.
InterProi IPR006615. Pept_C19_DUSP.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR028135. Ub_USP-typ.
IPR029071. Ubiquitin-rel_dom.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF06337. DUSP. 1 hit.
PF14836. Ubiquitin_3. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view ]
SMARTi SM00695. DUSP. 1 hit.
[Graphical view ]
SUPFAMi SSF143791. SSF143791. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF55205. SSF55205. 1 hit.
PROSITEi PS51283. DUSP. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a new human deubiquitinating enzyme Unph4."
    Kim K.I., Nagase T., Chung C.H.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "A catalogue of genes in the human dermal papilla cells as identified by expressed sequence tags."
    Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y., Im S.U., Jung E.J., Lee J.H., Kim J.C.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hair follicle dermal papilla.
  5. "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] (ISOFORM 4).
    Tissue: Placenta.
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., 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., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORMS 2 AND 4).
    Tissue: Brain and Lung.
  8. Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-21; 475-482 AND 924-932, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Mammary carcinoma.
  9. "Cloning and identification of human Unph-2."
    Kimura Y., Saya H., Nakao M.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-981 (ISOFORM 3).
    Tissue: Fetal brain.
  10. "Identification, functional characterization, and chromosomal localization of USP15, a novel human ubiquitin-specific protease related to the UNP oncoprotein, and a systematic nomenclature for human ubiquitin-specific proteases."
    Baker R.T., Wang X.-W., Woollatt E., White J.A., Sutherland G.R.
    Genomics 59:264-274(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION (ISOFORM 2), CATALYTIC ACTIVITY.
  11. "Isolation and characterization of the mouse ubiquitin-specific protease Usp15."
    Angelats C., Wang X.-W., Jermiin L.S., Copeland N.G., Jenkins N.A., Baker R.T.
    Mamm. Genome 14:31-46(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
  12. "The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1."
    Hetfeld B.K., Helfrich A., Kapelari B., Scheel H., Hofmann K., Guterman A., Glickman M., Schade R., Kloetzel P.M., Dubiel W.
    Curr. Biol. 15:1217-1221(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-812, IDENTIFICATION IN A COMPLEX WITH THE COP9 SIGNALOSOME, PHOSPHORYLATION, UBIQUITINATION.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha."
    Schweitzer K., Bozko P.M., Dubiel W., Naumann M.
    EMBO J. 26:1532-1541(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-961 AND SER-965, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "COP9 signalosome interacts ATP-dependently with p97/valosin-containing protein (VCP) and controls the ubiquitination status of proteins bound to p97/VCP."
    Cayli S., Klug J., Chapiro J., Frohlich S., Krasteva G., Orel L., Meinhardt A.
    J. Biol. Chem. 284:34944-34953(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "The COP9 signalosome mediates beta-catenin degradation by deneddylation and blocks adenomatous polyposis coli destruction via USP15."
    Huang X., Langelotz C., Hetfeld-Pechoc B.K., Schwenk W., Dubiel W.
    J. Mol. Biol. 391:691-702(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-812.
  19. "The ubiquitin-specific peptidase USP15 regulates human papillomavirus type 16 E6 protein stability."
    Vos R.M., Altreuter J., White E.A., Howley P.M.
    J. Virol. 83:8885-8892(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-298, INTERACTION WITH HUMAN PAPILLOMAVIRUS TYPE 16 PROTEIN E6.
  20. "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-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "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-229; SER-242; SER-961 AND SER-965, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH SMAD1; SMAD2 AND SMAD3, MUTAGENESIS OF CYS-298.
  24. "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-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "USP15 stabilizes TGF-beta receptor I and promotes oncogenesis through the activation of TGF-beta signaling in glioblastoma."
    Eichhorn P.J., Rodon L., Gonzalez-Junca A., Dirac A., Gili M., Martinez-Saez E., Aura C., Barba I., Peg V., Prat A., Cuartas I., Jimenez J., Garcia-Dorado D., Sahuquillo J., Bernards R., Baselga J., Seoane J.
    Nat. Med. 18:429-435(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TGFBR1 AND SMAD7, MUTAGENESIS OF CYS-298.
  27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Solution structure of the human ubiquitin-specific protease 15 DUSP domain."
    de Jong R.N., Ab E., Diercks T., Truffault V., Danieels M., Kaptein R., Folkers G.E.
    J. Biol. Chem. 281:5026-5031(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-120.
  29. "Structure of the USP15 N-terminal domains: a beta-hairpin mediates close association between the DUSP and UBL domains."
    Harper S., Besong T.M., Emsley J., Scott D.J., Dreveny I.
    Biochemistry 50:7995-8004(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-222.
  30. "Structural variability of the ubiquitin specific protease DUSP-UBL double domains."
    Elliott P.R., Liu H., Pastok M.W., Grossmann G.J., Rigden D.J., Clague M.J., Urbe S., Barsukov I.L.
    FEBS Lett. 585:3385-3390(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-223.
  31. "Crystal structure of the human ubiquitin-specific protease 15 DUSP domain."
    Structural genomics consortium (SGC)
    Submitted (APR-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-133.

Entry informationi

Entry nameiUBP15_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4E8
Secondary accession number(s): Q08AL5
, Q9H8G9, Q9HCA6, Q9UNP0, Q9Y5B5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 12, 2003
Last modified: November 26, 2014
This is version 146 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3