Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

D2HBJ8

- UBP44_AILME

UniProt

D2HBJ8 - UBP44_AILME

Protein

Ubiquitin carboxyl-terminal hydrolase 44

Gene

USP44

Organism
Ailuropoda melanoleuca (Giant panda)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 31 (01 Oct 2014)
      Sequence version 1 (09 Feb 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Acts as a negative regulator of histone H2B (H2BK120ub1) ubiquitination By similarity.By similarity

    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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei281 – 2811NucleophilePROSITE-ProRule annotation
    Active sitei635 – 6351Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri27 – 8862UBP-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ubiquitin-specific protease activity Source: UniProtKB
    2. ubiquitin thiolesterase activity Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. anaphase Source: UniProtKB
    2. mitotic nuclear division Source: UniProtKB-KW
    3. negative regulation of mitotic anaphase-promoting complex activity Source: UniProtKB
    4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    5. protein deubiquitination Source: UniProtKB
    6. regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
    7. regulation of spindle checkpoint Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 44 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 44
    Ubiquitin thioesterase 44
    Ubiquitin-specific-processing protease 44
    Gene namesi
    Name:USP44
    ORF Names:PANDA_007904
    OrganismiAiluropoda melanoleuca (Giant panda)
    Taxonomic identifieri9646 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaUrsidaeAiluropoda
    ProteomesiUP000008912: Unplaced

    Subcellular locationi

    Nucleus By similarity
    Note: Peaks in interphase, with relatively low levels maintained throughout mitosis.By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 711711Ubiquitin carboxyl-terminal hydrolase 44PRO_0000395810Add
    BLAST

    Post-translational modificationi

    Dephosphorylated by CTDP1.By similarity
    Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome.By similarity

    Keywords - PTMi

    Ubl conjugation

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini272 – 677406USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family. USP44 subfamily.Curated
    Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri27 – 8862UBP-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    GeneTreeiENSGT00750000117363.
    HOGENOMiHOG000015084.
    KOiK11834.
    OMAiAIKSQNY.
    OrthoDBiEOG7JX33S.
    TreeFamiTF315281.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    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]
    SMARTiSM00290. ZnF_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]

    Sequencei

    Sequence statusi: Complete.

    D2HBJ8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTMDKCKHI GQLRLAQDHS ILNPQKWHCV DCNTTESIWA CLSCSHVACG    50
    RYIEEHALKH FQESSHPVAL EVNEMYVFCY LCDDYVLNDN ATGDLKLLRS 100
    MLSAIKSQNY QCTTRSGRVL RSMGTSDDTY YLHDGTQSLL QNEDQMYTAL 150
    WHRRRILMSK IFRTWFEQSP TGRKRQEEQF QEKIAKREVK KRRQELEYQV 200
    KAELETIHPR KSLRLQGLAQ STTVEIVPVQ VPLQTPASPA KDKVVSTSED 250
    VRLKKASDSS GKRRPIVTPG VTGLRNLGNT CYMNSVLQVL SHLLIFRQCF 300
    LKLDLNQWLA VTASDKTRSP YKHPSITDTV YQMNECQETD TGSAPSRHPS 350
    LSLGLSGGAS KSRKMELIQP REPSSQYISL CHELHTLFQV MWSGKWALVS 400
    PFAMLHSVWR LIPAFRGYAQ QDAQEFLCEL LDKIQHELET TGTRLPALIP 450
    TSQRKLIKQV LNVVNNIFHG QLLSQVTCLA CDNKSNTIEP FWDLSLEFPE 500
    RYQCNGKDIA SQPCRVTEML AKFTETEALE GKIYVCDHCN SKRRRFSSKS 550
    VVLTEAQKQL MICHLPQVLR LHLKRFRWSG RNNREKIGVH VGFEEILNME 600
    PYCCRESLKS LRPECFIYDL SAVVMHHGKG FGSGHYTAYC YNSEGGFWVH 650
    CNDSKLSMCT MDEVCKAQAY ILFYTQRVTE NGHSKLLPPE LLSGSQHPNE 700
    EADTSSNEIL S 711
    Length:711
    Mass (Da):81,364
    Last modified:February 9, 2010 - v1
    Checksum:i00C0350EA2E949E1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GL192660 Genomic DNA. Translation: EFB15980.1.
    RefSeqiXP_002919284.1. XM_002919238.1.

    Genome annotation databases

    EnsembliENSAMET00000002387; ENSAMEP00000002292; ENSAMEG00000002189.
    GeneIDi100470180.
    KEGGiaml:100470180.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GL192660 Genomic DNA. Translation: EFB15980.1 .
    RefSeqi XP_002919284.1. XM_002919238.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSAMET00000002387 ; ENSAMEP00000002292 ; ENSAMEG00000002189 .
    GeneIDi 100470180.
    KEGGi aml:100470180.

    Organism-specific databases

    CTDi 84101.

    Phylogenomic databases

    GeneTreei ENSGT00750000117363.
    HOGENOMi HOG000015084.
    KOi K11834.
    OMAi AIKSQNY.
    OrthoDBi EOG7JX33S.
    TreeFami TF315281.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    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 ]
    SMARTi SM00290. ZnF_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

    1. "The sequence and de novo assembly of the giant panda genome."
      Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.
      , Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J., Wang J.
      Nature 463:311-317(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiUBP44_AILME
    AccessioniPrimary (citable) accession number: D2HBJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 31 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3