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Q86T82

- UBP37_HUMAN

UniProt

Q86T82 - UBP37_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 37

Gene

USP37

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2).1 Publication

    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
    Active sitei350 – 3501NucleophileCurated
    Active sitei906 – 9061Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: UniProtKB
    4. ubiquitin-specific protease activity Source: UniProtKB

    GO - Biological processi

    1. G1/S transition of mitotic cell cycle Source: UniProtKB
    2. mitotic nuclear division Source: UniProtKB-KW
    3. protein deubiquitination Source: FlyBase
    4. protein K11-linked deubiquitination Source: UniProtKB
    5. protein K48-linked deubiquitination Source: UniProtKB
    6. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC19.053.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 37 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 37
    Ubiquitin thioesterase 37
    Ubiquitin-specific-processing protease 37
    Gene namesi
    Name:USP37
    Synonyms:KIAA1594
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:20063. USP37.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: LIFEdb

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 343KEN → AAA: No effect.
    Mutagenesisi71 – 744RLML → ALMA: No effect.
    Mutagenesisi96 – 994RLFL → ALFA: No effect.
    Mutagenesisi160 – 1634RKVL → AKVA: No effect.
    Mutagenesisi221 – 2233KEN → AAA: No effect.
    Mutagenesisi350 – 3501C → S: Abolishes deubiquitinase activity. 1 Publication
    Mutagenesisi628 – 6281S → A: Abolishes phosphorylation by CDK2, leading to lower deubiquitinase activity. 1 Publication
    Mutagenesisi782 – 7843KEN → AAA: Impaired interaction with FZR1/CDH1 and subsequent ubiquitination.

    Organism-specific databases

    PharmGKBiPA134928706.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 979979Ubiquitin carboxyl-terminal hydrolase 37PRO_0000080667Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei628 – 6281Phosphoserine; by CDK21 Publication
    Modified residuei650 – 6501Phosphoserine1 Publication
    Modified residuei652 – 6521Phosphoserine1 Publication

    Post-translational modificationi

    Polyubiquitinated via 'Lys-11'-linked ubiquitin by the APC(CDH1) complex during late mitosis, leading to its degradation. Able to mediate auto-deubiquitination.1 Publication
    Phosphorylated at Ser-628 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-628 is required for deubiquitinase activity. Also polyubiquitinated during early G1 phase, without leading to degradation.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ86T82.
    PaxDbiQ86T82.
    PRIDEiQ86T82.

    PTM databases

    PhosphoSiteiQ86T82.

    Expressioni

    Tissue specificityi

    Expressed in brain and prostate.1 Publication

    Developmental stagei

    Induced in G1 phase, accumulates at G1/S transition, and degraded in late mitosis following ubiquitination and degradation by the APC(CDH1) complex.1 Publication

    Inductioni

    Induced by E2F transcription factors in G1.1 Publication

    Gene expression databases

    ArrayExpressiQ86T82.
    BgeeiQ86T82.
    CleanExiHS_USP37.
    GenevestigatoriQ86T82.

    Organism-specific databases

    HPAiHPA045160.

    Interactioni

    Subunit structurei

    Interacts with FZR1/CDH1.1 Publication

    Protein-protein interaction databases

    BioGridi121720. 18 interactions.
    IntActiQ86T82. 3 interactions.
    MINTiMINT-4720282.
    STRINGi9606.ENSP00000258399.

    Structurei

    Secondary structure

    1
    979
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 1410
    Turni15 – 173
    Beta strandi23 – 3210
    Beta strandi35 – 428
    Beta strandi49 – 524
    Turni54 – 563
    Beta strandi57 – 648
    Beta strandi69 – 768
    Beta strandi81 – 888
    Helixi89 – 10315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3U12X-ray2.08A/B4-125[»]
    ProteinModelPortaliQ86T82.
    SMRiQ86T82. Positions 4-106, 337-598.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini341 – 951611USPAdd
    BLAST
    Repeati704 – 72320UIM 1Add
    BLAST
    Repeati806 – 82520UIM 2Add
    BLAST
    Repeati828 – 84720UIM 3Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi32 – 343KEN box 1
    Motifi71 – 799D-box 1
    Motifi96 – 10510D-box 2
    Motifi160 – 1689D-box 3
    Motifi221 – 2233KEN box 2
    Motifi782 – 7843KEN box 3

    Domaini

    The KEN box 3 is required for interaction with FZR1/CDH1 and is essential for APC(CDH1)-mediated ubiquitination.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 3 UIM (ubiquitin-interacting motif) repeats.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5207.
    HOVERGENiHBG055893.
    InParanoidiQ86T82.
    KOiK11850.
    OMAiLQEFNNS.
    OrthoDBiEOG7HMS09.
    PhylomeDBiQ86T82.
    TreeFamiTF323032.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR003903. Ubiquitin-int_motif.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    PF02809. UIM. 3 hits.
    [Graphical view]
    SMARTiSM00726. UIM. 4 hits.
    [Graphical view]
    PROSITEiPS50330. UIM. 3 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86T82-1) [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

    MSPLKIHGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI    50
    FQLSHNIKNV VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD 100
    AVHQNRLPAA MKPSQGSGSF GAILGSRTSQ KETSRQLSYS DNQASAKRGS 150
    LETKDDIPFR KVLGNPGRGS IKTVAGSGIA RTIPSLTSTS TPLRSGLLEN 200
    RTEKRKRMIS TGSELNEDYP KENDSSSNNK AMTDPSRKYL TSSREKQLSL 250
    KQSEENRTSG LLPLQSSSFY GSRAGSKEHS SGGTNLDRTN VSSQTPSAKR 300
    SLGFLPQPVP LSVKKLRCNQ DYTGWNKPRV PLSSHQQQQL QGFSNLGNTC 350
    YMNAILQSLF SLQSFANDLL KQGIPWKKIP LNALIRRFAH LLVKKDICNS 400
    ETKKDLLKKV KNAISATAER FSGYMQNDAH EFLSQCLDQL KEDMEKLNKT 450
    WKTEPVSGEE NSPDISATRA YTCPVITNLE FEVQHSIICK ACGEIIPKRE 500
    QFNDLSIDLP RRKKPLPPRS IQDSLDLFFR AEELEYSCEK CGGKCALVRH 550
    KFNRLPRVLI LHLKRYSFNV ALSLNNKIGQ QVIIPRYLTL SSHCTENTKP 600
    PFTLGWSAHM AISRPLKASQ MVNSCITSPS TPSKKFTFKS KSSLALCLDS 650
    DSEDELKRSV ALSQRLCEML GNEQQQEDLE KDSKLCPIEP DKSELENSGF 700
    DRMSEEELLA AVLEISKRDA SPSLSHEDDD KPTSSPDTGF AEDDIQEMPE 750
    NPDTMETEKP KTITELDPAS FTEITKDCDE NKENKTPEGS QGEVDWLQQY 800
    DMEREREEQE LQQALAQSLQ EQEAWEQKED DDLKRATELS LQEFNNSFVD 850
    ALGSDEDSGN EDVFDMEYTE AEAEELKRNA ETGNLPHSYR LISVVSHIGS 900
    TSSSGHYISD VYDIKKQAWF TYNDLEVSKI QEAAVQSDRD RSGYIFFYMH 950
    KEIFDELLET EKNSQSLSTE VGKTTRQAL 979
    Length:979
    Mass (Da):110,170
    Last modified:July 13, 2010 - v2
    Checksum:i9F47F06A744EA449
    GO
    Isoform 2 (identifier: Q86T82-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.
         612-634: ISRPLKASQMVNSCITSPSTPSK → M

    Show »
    Length:885
    Mass (Da):99,752
    Checksum:iD5D5E4077F1155B4
    GO

    Sequence cautioni

    The sequence AAY14887.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2242ND → DG in CAD89955. (PubMed:17974005)Curated
    Sequence conflicti345 – 3451N → K in CAD97970. (PubMed:17974005)Curated
    Sequence conflicti456 – 4561V → I in CAD89955. (PubMed:17974005)Curated
    Sequence conflicti552 – 5521F → I in AAI44250. (PubMed:15489334)Curated
    Sequence conflicti567 – 5671S → I in AAI44253. (PubMed:15489334)Curated
    Sequence conflicti576 – 5761N → Y in AAI44253. (PubMed:15489334)Curated
    Sequence conflicti731 – 7311K → E in CAD97970. (PubMed:17974005)Curated
    Sequence conflicti905 – 9051G → D in CAD97970. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti979 – 9791L → S.4 Publications
    Corresponds to variant rs6436058 [ dbSNP | Ensembl ].
    VAR_059752

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_041740Add
    BLAST
    Alternative sequencei612 – 63423ISRPL…STPSK → M in isoform 2. 1 PublicationVSP_041741Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL832645 mRNA. Translation: CAD89955.1.
    BX538024 mRNA. Translation: CAD97970.1.
    AC012510 Genomic DNA. No translation available.
    AC073838 Genomic DNA. Translation: AAY14887.1. Sequence problems.
    CH471063 Genomic DNA. Translation: EAW70621.1.
    BC112901 mRNA. Translation: AAI12902.1.
    BC133007 mRNA. Translation: AAI33008.1.
    BC133009 mRNA. Translation: AAI33010.1.
    BC144249 mRNA. Translation: AAI44250.1.
    BC144252 mRNA. Translation: AAI44253.1.
    AB046814 mRNA. Translation: BAB13420.1.
    RefSeqiNP_065986.2. NM_020935.2.
    XP_005246777.1. XM_005246720.1. [Q86T82-1]
    XP_005246778.1. XM_005246721.1. [Q86T82-1]
    XP_005246779.1. XM_005246722.1. [Q86T82-1]
    UniGeneiHs.166068.

    Genome annotation databases

    EnsembliENST00000258399; ENSP00000258399; ENSG00000135913. [Q86T82-1]
    ENST00000415516; ENSP00000400902; ENSG00000135913. [Q86T82-2]
    ENST00000418019; ENSP00000396585; ENSG00000135913. [Q86T82-1]
    ENST00000454775; ENSP00000393662; ENSG00000135913. [Q86T82-1]
    GeneIDi57695.
    KEGGihsa:57695.
    UCSCiuc002vie.2. human. [Q86T82-1]
    uc002vig.2. human. [Q86T82-2]

    Polymorphism databases

    DMDMi300669620.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL832645 mRNA. Translation: CAD89955.1 .
    BX538024 mRNA. Translation: CAD97970.1 .
    AC012510 Genomic DNA. No translation available.
    AC073838 Genomic DNA. Translation: AAY14887.1 . Sequence problems.
    CH471063 Genomic DNA. Translation: EAW70621.1 .
    BC112901 mRNA. Translation: AAI12902.1 .
    BC133007 mRNA. Translation: AAI33008.1 .
    BC133009 mRNA. Translation: AAI33010.1 .
    BC144249 mRNA. Translation: AAI44250.1 .
    BC144252 mRNA. Translation: AAI44253.1 .
    AB046814 mRNA. Translation: BAB13420.1 .
    RefSeqi NP_065986.2. NM_020935.2.
    XP_005246777.1. XM_005246720.1. [Q86T82-1 ]
    XP_005246778.1. XM_005246721.1. [Q86T82-1 ]
    XP_005246779.1. XM_005246722.1. [Q86T82-1 ]
    UniGenei Hs.166068.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3U12 X-ray 2.08 A/B 4-125 [» ]
    ProteinModelPortali Q86T82.
    SMRi Q86T82. Positions 4-106, 337-598.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121720. 18 interactions.
    IntActi Q86T82. 3 interactions.
    MINTi MINT-4720282.
    STRINGi 9606.ENSP00000258399.

    Protein family/group databases

    MEROPSi C19.053.

    PTM databases

    PhosphoSitei Q86T82.

    Polymorphism databases

    DMDMi 300669620.

    Proteomic databases

    MaxQBi Q86T82.
    PaxDbi Q86T82.
    PRIDEi Q86T82.

    Protocols and materials databases

    DNASUi 57695.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258399 ; ENSP00000258399 ; ENSG00000135913 . [Q86T82-1 ]
    ENST00000415516 ; ENSP00000400902 ; ENSG00000135913 . [Q86T82-2 ]
    ENST00000418019 ; ENSP00000396585 ; ENSG00000135913 . [Q86T82-1 ]
    ENST00000454775 ; ENSP00000393662 ; ENSG00000135913 . [Q86T82-1 ]
    GeneIDi 57695.
    KEGGi hsa:57695.
    UCSCi uc002vie.2. human. [Q86T82-1 ]
    uc002vig.2. human. [Q86T82-2 ]

    Organism-specific databases

    CTDi 57695.
    GeneCardsi GC02M219281.
    HGNCi HGNC:20063. USP37.
    HPAi HPA045160.
    neXtProti NX_Q86T82.
    PharmGKBi PA134928706.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5207.
    HOVERGENi HBG055893.
    InParanoidi Q86T82.
    KOi K11850.
    OMAi LQEFNNS.
    OrthoDBi EOG7HMS09.
    PhylomeDBi Q86T82.
    TreeFami TF323032.

    Miscellaneous databases

    ChiTaRSi USP37. human.
    GeneWikii USP37.
    GenomeRNAii 57695.
    NextBioi 64543.
    PROi Q86T82.

    Gene expression databases

    ArrayExpressi Q86T82.
    Bgeei Q86T82.
    CleanExi HS_USP37.
    Genevestigatori Q86T82.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR003903. Ubiquitin-int_motif.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    PF02809. UIM. 3 hits.
    [Graphical view ]
    SMARTi SM00726. UIM. 4 hits.
    [Graphical view ]
    PROSITEi PS50330. UIM. 3 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-979.
      Tissue: Spinal cord.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-979.
    4. "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 1 AND 2), VARIANT SER-979.
      Tissue: Testis.
    5. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
      DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-979 (ISOFORM 1), VARIANT SER-979.
      Tissue: Brain.
    6. "Cloning and enzymatic analysis of 22 novel human ubiquitin-specific proteases."
      Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S., Lopez-Otin C.
      Biochem. Biophys. Res. Commun. 314:54-62(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, ENZYME ACTIVITY.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650 AND SER-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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].
    9. "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry."
      Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G., Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.
      Mol. Cell 42:511-523(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION, PHOSPHORYLATION AT SER-628 BY CDK2, DOMAIN KEN BOX 3, DEVELOPMENTAL STAGE, INDUCTION, INTERACTION WITH FZR1, MUTAGENESIS OF 32-LYS--ASN-34; 71-ARG-LEU-74; 96-ARG-LEU-99; 160-ARG-LEU-163; 221-LYS--ASN-223; CYS-350; 782-LYS--ASN-784 AND SER-628.

    Entry informationi

    Entry nameiUBP37_HUMAN
    AccessioniPrimary (citable) accession number: Q86T82
    Secondary accession number(s): A2RUQ8
    , B7ZM38, B7ZM41, E9PHL3, Q2KHT2, Q53S10, Q7Z3A5, Q9HCH8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 103 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 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3