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Q92995

- UBP13_HUMAN

UniProt

Q92995 - UBP13_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 13

Gene

USP13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data.6 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).

    Enzyme regulationi

    Specifically inhibited by spautin-1 (specific and potent autophagy inhibitor-1), a derivative of MBCQ that binds to USP13 and inhibits deubiquitinase activity. Regulated by PIK3C3/VPS34-containing complexes. The weak deubiquitinase activity in vitro suggests the existence of some mechanism that activates the enzyme.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei345 – 3451NucleophileCurated
    Active sitei823 – 8231Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri209 – 28173UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. omega peptidase activity Source: InterPro
    3. protein binding Source: UniProtKB
    4. ubiquitin binding Source: UniProtKB
    5. ubiquitin protein ligase binding Source: UniProtKB
    6. ubiquitin-specific protease activity Source: UniProtKB
    7. ubiquitin thiolesterase activity Source: UniProtKB
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. cell proliferation Source: UniProtKB
    3. melanocyte differentiation Source: UniProtKB
    4. protein K63-linked deubiquitination Source: UniProtKB
    5. protein stabilization Source: UniProtKB
    6. regulation of autophagy Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB
    8. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Autophagy, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC19.012.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 13 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 13
    Isopeptidase T-3
    Short name:
    ISOT-3
    Ubiquitin thioesterase 13
    Ubiquitin-specific-processing protease 13
    Gene namesi
    Name:USP13
    Synonyms:ISOT3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:12611. USP13.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi221 – 2211W → A: Does not abolish ability to stabilize SIAH2. 1 Publication
    Mutagenesisi233 – 2331K → A: Does not abolish ability to stabilize SIAH2. 1 Publication
    Mutagenesisi273 – 2731F → A: Impairs ability to stabilize SIAH2. 1 Publication
    Mutagenesisi345 – 3451C → A: Abolishes deubiquitinating activity. Does not abolish ability to stabilize SIAH2. Does not abolish ability to stabilize SIAH2; when associated with A-814 and A-823. 2 Publications
    Mutagenesisi664 – 6641M → E: Impairs ability to stabilize SIAH2. Abolishes ability to stabilize SIAH2; when associated with E-739. 1 Publication
    Mutagenesisi739 – 7391M → E: Impairs ability to stabilize SIAH2. Abolishes ability to stabilize SIAH2; when associated with E-664. 1 Publication
    Mutagenesisi814 – 8141H → A: Does not abolish ability to stabilize SIAH2; when associated with A-345 and A-823. 1 Publication
    Mutagenesisi823 – 8231H → A: Does not abolish ability to stabilize SIAH2; when associated with A-345 and A-814. 1 Publication

    Organism-specific databases

    PharmGKBiPA37237.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 863863Ubiquitin carboxyl-terminal hydrolase 13PRO_0000080635Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei114 – 1141Phosphoserine1 Publication
    Modified residuei122 – 1221Phosphothreonine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ92995.
    PaxDbiQ92995.
    PRIDEiQ92995.

    PTM databases

    PhosphoSiteiQ92995.

    Expressioni

    Tissue specificityi

    Highly expressed in ovary and testes.

    Gene expression databases

    ArrayExpressiQ92995.
    BgeeiQ92995.
    CleanExiHS_USP13.
    GenevestigatoriQ92995.

    Organism-specific databases

    HPAiHPA004827.

    Interactioni

    Subunit structurei

    Interacts with UFD1. Interacts (via UBA domains) with SIAH2 (when ubiquitinated).2 Publications

    Protein-protein interaction databases

    BioGridi114465. 37 interactions.
    IntActiQ92995. 27 interactions.
    MINTiMINT-1195142.
    STRINGi9606.ENSP00000263966.

    Structurei

    Secondary structure

    1
    863
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni191 – 1944
    Beta strandi212 – 2143
    Beta strandi217 – 2237
    Turni224 – 2263
    Beta strandi229 – 2313
    Helixi244 – 2518
    Beta strandi256 – 2605
    Beta strandi269 – 2724
    Turni273 – 2753
    Beta strandi277 – 2793
    Helixi284 – 2907
    Helixi296 – 2994
    Helixi656 – 6627
    Helixi669 – 67810
    Helixi683 – 69210
    Helixi693 – 6953
    Beta strandi697 – 7004
    Beta strandi710 – 7145
    Helixi730 – 73910
    Helixi743 – 75311
    Helixi757 – 7659

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L80NMR-A188-301[»]
    2LBCNMR-A652-777[»]
    ProteinModelPortaliQ92995.
    SMRiQ92995. Positions 26-863.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini336 – 861526USPAdd
    BLAST
    Domaini652 – 69342UBA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini727 – 76741UBA 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The UBP-type zinc finger has lost its ability to bind ubiquitin and USP13 is not activated by unanchored ubiquitin. Swapping with the UBP-type zinc finger from USP5 restores ability to bind unanchored ubiquitin and subsequent activation of the protein (PubMed:22216260).1 Publication
    The UBA domains mediate binding to ubiquitin.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 2 UBA domains.PROSITE-ProRule annotation
    Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri209 – 28173UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5207.
    HOGENOMiHOG000162311.
    HOVERGENiHBG002833.
    InParanoidiQ92995.
    KOiK11836.
    OMAiPRMFKAF.
    OrthoDBiEOG7CNZF3.
    PhylomeDBiQ92995.
    TreeFamiTF300576.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR016652. Ubiquitinyl_hydrolase.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view]
    PfamiPF00627. UBA. 2 hits.
    PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016308. UBP. 1 hit.
    SMARTiSM00165. UBA. 2 hits.
    SM00290. ZnF_UBP. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    PROSITEiPS50030. UBA. 2 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92995-1) [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

    MQRRGALFGM PGGSGGRKMA AGDIGELLVP HMPTIRVPRS GDRVYKNECA    50
    FSYDSPNSEG GLYVCMNTFL AFGREHVERH FRKTGQSVYM HLKRHVREKV 100
    RGASGGALPK RRNSKIFLDL DTDDDLNSDD YEYEDEAKLV IFPDHYEIAL 150
    PNIEELPALV TIACDAVLSS KSPYRKQDPD TWENELPVSK YANNLTQLDN 200
    GVRIPPSGWK CARCDLRENL WLNLTDGSVL CGKWFFDSSG GNGHALEHYR 250
    DMGYPLAVKL GTITPDGADV YSFQEEEPVL DPHLAKHLAH FGIDMLHMHG 300
    TENGLQDNDI KLRVSEWEVI QESGTKLKPM YGPGYTGLKN LGNSCYLSSV 350
    MQAIFSIPEF QRAYVGNLPR IFDYSPLDPT QDFNTQMTKL GHGLLSGQYS 400
    KPPVKSELIE QVMKEEHKPQ QNGISPRMFK AFVSKSHPEF SSNRQQDAQE 450
    FFLHLVNLVE RNRIGSENPS DVFRFLVEER IQCCQTRKVR YTERVDYLMQ 500
    LPVAMEAATN KDELIAYELT RREAEANRRP LPELVRAKIP FSACLQAFSE 550
    PENVDDFWSS ALQAKSAGVK TSRFASFPEY LVVQIKKFTF GLDWVPKKFD 600
    VSIDMPDLLD INHLRARGLQ PGEEELPDIS PPIVIPDDSK DRLMNQLIDP 650
    SDIDESSVMQ LAEMGFPLEA CRKAVYFTGN MGAEVAFNWI IVHMEEPDFA 700
    EPLTMPGYGG AASAGASVFG ASGLDNQPPE EIVAIITSMG FQRNQAIQAL 750
    RATNNNLERA LDWIFSHPEF EEDSDFVIEM ENNANANIIS EAKPEGPRVK 800
    DGSGTYELFA FISHMGTSTM SGHYICHIKK EGRWVIYNDH KVCASERPPK 850
    DLGYMYFYRR IPS 863
    Length:863
    Mass (Da):97,327
    Last modified:October 14, 2008 - v2
    Checksum:i988713ADF8C0B938
    GO
    Isoform 2 (identifier: Q92995-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-65: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:798
    Mass (Da):90,383
    Checksum:i5F9943C19D16FE4F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961V → A in AAC63405. (PubMed:9841226)Curated
    Sequence conflicti293 – 2931I → V in BAF83027. (PubMed:14702039)Curated
    Sequence conflicti305 – 3051L → F in BAF83027. (PubMed:14702039)Curated
    Sequence conflicti325 – 3251T → A in BAF83027. (PubMed:14702039)Curated
    Sequence conflicti338 – 3381L → P in BAF83027. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6565Missing in isoform 2. 1 PublicationVSP_043954Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U75362 mRNA. Translation: AAC63405.1.
    AK290338 mRNA. Translation: BAF83027.1.
    AK302404 mRNA. Translation: BAG63715.1.
    AC007687 Genomic DNA. No translation available.
    AC125604 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78383.1.
    CH471052 Genomic DNA. Translation: EAW78384.1.
    BC016146 mRNA. Translation: AAH16146.1.
    CCDSiCCDS3235.1. [Q92995-1]
    RefSeqiNP_003931.2. NM_003940.2. [Q92995-1]
    UniGeneiHs.175322.

    Genome annotation databases

    EnsembliENST00000263966; ENSP00000263966; ENSG00000058056. [Q92995-1]
    ENST00000496897; ENSP00000417146; ENSG00000058056. [Q92995-2]
    GeneIDi8975.
    KEGGihsa:8975.
    UCSCiuc003fkh.3. human. [Q92995-1]

    Polymorphism databases

    DMDMi209572692.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U75362 mRNA. Translation: AAC63405.1 .
    AK290338 mRNA. Translation: BAF83027.1 .
    AK302404 mRNA. Translation: BAG63715.1 .
    AC007687 Genomic DNA. No translation available.
    AC125604 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78383.1 .
    CH471052 Genomic DNA. Translation: EAW78384.1 .
    BC016146 mRNA. Translation: AAH16146.1 .
    CCDSi CCDS3235.1. [Q92995-1 ]
    RefSeqi NP_003931.2. NM_003940.2. [Q92995-1 ]
    UniGenei Hs.175322.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L80 NMR - A 188-301 [» ]
    2LBC NMR - A 652-777 [» ]
    ProteinModelPortali Q92995.
    SMRi Q92995. Positions 26-863.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114465. 37 interactions.
    IntActi Q92995. 27 interactions.
    MINTi MINT-1195142.
    STRINGi 9606.ENSP00000263966.

    Protein family/group databases

    MEROPSi C19.012.

    PTM databases

    PhosphoSitei Q92995.

    Polymorphism databases

    DMDMi 209572692.

    Proteomic databases

    MaxQBi Q92995.
    PaxDbi Q92995.
    PRIDEi Q92995.

    Protocols and materials databases

    DNASUi 8975.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263966 ; ENSP00000263966 ; ENSG00000058056 . [Q92995-1 ]
    ENST00000496897 ; ENSP00000417146 ; ENSG00000058056 . [Q92995-2 ]
    GeneIDi 8975.
    KEGGi hsa:8975.
    UCSCi uc003fkh.3. human. [Q92995-1 ]

    Organism-specific databases

    CTDi 8975.
    GeneCardsi GC03P179370.
    H-InvDB HIX0003883.
    HGNCi HGNC:12611. USP13.
    HPAi HPA004827.
    MIMi 603591. gene.
    neXtProti NX_Q92995.
    PharmGKBi PA37237.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5207.
    HOGENOMi HOG000162311.
    HOVERGENi HBG002833.
    InParanoidi Q92995.
    KOi K11836.
    OMAi PRMFKAF.
    OrthoDBi EOG7CNZF3.
    PhylomeDBi Q92995.
    TreeFami TF300576.

    Miscellaneous databases

    GeneWikii USP13.
    GenomeRNAii 8975.
    NextBioi 33685.
    PROi Q92995.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92995.
    Bgeei Q92995.
    CleanExi HS_USP13.
    Genevestigatori Q92995.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    IPR016652. Ubiquitinyl_hydrolase.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view ]
    Pfami PF00627. UBA. 2 hits.
    PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016308. UBP. 1 hit.
    SMARTi SM00165. UBA. 2 hits.
    SM00290. ZnF_UBP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    PROSITEi PS50030. UBA. 2 hits.
    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

    1. "The genomic organization of Isopeptidase T-3 (ISOT-3), a new member of the ubiquitin specific protease family (UBP)."
      Timms K.M., Ansari-Lari M.A., Morris W., Brown S.N., Gibbs R.A.
      Gene 217:101-106(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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 1 AND 2).
      Tissue: Testis and Tongue.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 1).
      Tissue: Uterus.
    6. Cited for: FUNCTION.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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-114 AND THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13."
      Liu J., Xia H., Kim M., Xu L., Li Y., Zhang L., Cai Y., Norberg H.V., Zhang T., Furuya T., Jin M., Zhu Z., Wang H., Yu J., Li Y., Hao Y., Choi A., Ke H., Ma D., Yuan J.
      Cell 147:223-234(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    11. "USP13 enzyme regulates Siah2 ligase stability and activity via noncatalytic ubiquitin-binding domains."
      Scortegagna M., Subtil T., Qi J., Kim H., Zhao W., Gu W., Kluger H., Ronai Z.A.
      J. Biol. Chem. 286:27333-27341(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SIAH2, MUTAGENESIS OF TRP-221; LYS-233; PHE-273; CYS-345; MET-664; MET-739; HIS-814 AND HIS-823.
    12. "Regulation of MITF stability by the USP13 deubiquitinase."
      Zhao X., Fiske B., Kawakami A., Li J., Fisher D.E.
      Nat. Commun. 2:414-414(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-345.
    13. "Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control."
      Chen M., Gutierrez G.J., Ronai Z.A.
      Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UFD1.
    14. "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 THR-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin."
      Zhang Y.H., Zhou C.J., Zhou Z.R., Song A.X., Hu H.Y.
      PLoS ONE 6:E29362-E29362(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 188-301 AND 652-777, FUNCTION, DOMAIN, UBIQUITIN-BINDING.

    Entry informationi

    Entry nameiUBP13_HUMAN
    AccessioniPrimary (citable) accession number: Q92995
    Secondary accession number(s): A8K2S3
    , B4DYF3, D3DNS2, Q96B25
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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