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Q9H0E7

- UBP44_HUMAN

UniProt

Q9H0E7 - UBP44_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 44

Gene

USP44

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (13 Jul 2010)
      Previous versions | rss
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    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.2 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).3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei282 – 2821Nucleophile
    Active sitei636 – 6361Proton acceptorPROSITE-ProRule annotation

    Regions

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

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. ubiquitin-specific protease activity Source: UniProtKB
    3. ubiquitin thiolesterase activity Source: UniProtKB
    4. 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

    Protein family/group databases

    MEROPSiC19.057.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:20064. USP44.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Peaks in interphase, with relatively low levels maintained throughout mitosis.By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi282 – 2821C → S or A: Abolishes deubiquitinase activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA134931457.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 712712Ubiquitin carboxyl-terminal hydrolase 44PRO_0000080673Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei169 – 1691Phosphoserine2 Publications
    Modified residuei239 – 2391Phosphoserine2 Publications
    Modified residuei269 – 2691Phosphothreonine2 Publications
    Modified residuei401 – 4011Phosphoserine2 Publications

    Post-translational modificationi

    Dephosphorylated by CTDP1.
    Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9H0E7.
    PRIDEiQ9H0E7.

    PTM databases

    PhosphoSiteiQ9H0E7.

    Expressioni

    Tissue specificityi

    Expressed in testis. Expressed at high levels in T-cell acute lymphoblastic leukemia.2 Publications

    Developmental stagei

    Elevated in mitosis; levels increase in mitotic cells and rapidly decrease once cells have completed chromosome attachment and exit from mitosis.1 Publication

    Inductioni

    Transcriptionally regulated by POU5F1/OCT4 in embryonic stem cells and embryonal carcinoma cells.1 Publication

    Gene expression databases

    ArrayExpressiQ9H0E7.
    BgeeiQ9H0E7.
    CleanExiHS_USP44.
    GenevestigatoriQ9H0E7.

    Organism-specific databases

    HPAiHPA026543.

    Interactioni

    Protein-protein interaction databases

    BioGridi123890. 12 interactions.
    IntActiQ9H0E7. 11 interactions.
    MINTiMINT-4719317.
    STRINGi9606.ENSP00000258499.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H0E7.
    SMRiQ9H0E7. Positions 29-86, 268-678.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini273 – 678406USPAdd
    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

    eggNOGiCOG5077.
    HOGENOMiHOG000015084.
    HOVERGENiHBG018027.
    InParanoidiQ9H0E7.
    KOiK11834.
    OMAiAIKSQNY.
    OrthoDBiEOG7JX33S.
    PhylomeDBiQ9H0E7.
    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.

    Q9H0E7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLAMDTCKHV GQLQLAQDHS SLNPQKWHCV DCNTTESIWA CLSCSHVACG    50
    RYIEEHALKH FQESSHPVAL EVNEMYVFCY LCDDYVLNDN TTGDLKLLRR 100
    TLSAIKSQNY HCTTRSGRFL RSMGTGDDSY FLHDGAQSLL QSEDQLYTAL 150
    WHRRRILMGK IFRTWFEQSP IGRKKQEEPF QEKIVVKREV KKRRQELEYQ 200
    VKAELESMPP RKSLRLQGLA QSTIIEIVSV QVPAQTPASP AKDKVLSTSE 250
    NEISQKVSDS SVKRRPIVTP GVTGLRNLGN TCYMNSVLQV LSHLLIFRQC 300
    FLKLDLNQWL AMTASEKTRS CKHPPVTDTV VYQMNECQEK DTGFVCSRQS 350
    SLSSGLSGGA SKGRKMELIQ PKEPTSQYIS LCHELHTLFQ VMWSGKWALV 400
    SPFAMLHSVW RLIPAFRGYA QQDAQEFLCE LLDKIQRELE TTGTSLPALI 450
    PTSQRKLIKQ VLNVVNNIFH GQLLSQVTCL ACDNKSNTIE PFWDLSLEFP 500
    ERYQCSGKDI ASQPCLVTEM LAKFTETEAL EGKIYVCDQC NSKRRRFSSK 550
    PVVLTEAQKQ LMICHLPQVL RLHLKRFRWS GRNNREKIGV HVGFEEILNM 600
    EPYCCRETLK SLRPECFIYD LSAVVMHHGK GFGSGHYTAY CYNSEGGFWV 650
    HCNDSKLSMC TMDEVCKAQA YILFYTQRVT ENGHSKLLPP ELLLGSQHPN 700
    EDADTSSNEI LS 712
    Length:712
    Mass (Da):81,185
    Last modified:July 13, 2010 - v2
    Checksum:iA8211DFAD78EE731
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti91 – 911T → A.3 Publications
    Corresponds to variant rs3812813 [ dbSNP | Ensembl ].
    VAR_017125
    Natural varianti316 – 3161E → Q.
    Corresponds to variant rs7305024 [ dbSNP | Ensembl ].
    VAR_057043
    Natural varianti348 – 3481R → G.
    Corresponds to variant rs7135642 [ dbSNP | Ensembl ].
    VAR_057044

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136825 mRNA. Translation: CAB66759.1.
    AK315697 mRNA. Translation: BAG38060.1.
    AC018475 Genomic DNA. No translation available.
    BC030704 mRNA. Translation: AAH30704.1.
    CCDSiCCDS9053.1.
    RefSeqiNP_001035862.1. NM_001042403.2.
    NP_001265322.1. NM_001278393.1.
    NP_115523.2. NM_032147.3.
    UniGeneiHs.646421.
    Hs.710121.

    Genome annotation databases

    EnsembliENST00000258499; ENSP00000258499; ENSG00000136014.
    ENST00000393091; ENSP00000376806; ENSG00000136014.
    ENST00000537435; ENSP00000442629; ENSG00000136014.
    GeneIDi84101.
    KEGGihsa:84101.
    UCSCiuc001teg.3. human.

    Polymorphism databases

    DMDMi300669621.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136825 mRNA. Translation: CAB66759.1 .
    AK315697 mRNA. Translation: BAG38060.1 .
    AC018475 Genomic DNA. No translation available.
    BC030704 mRNA. Translation: AAH30704.1 .
    CCDSi CCDS9053.1.
    RefSeqi NP_001035862.1. NM_001042403.2.
    NP_001265322.1. NM_001278393.1.
    NP_115523.2. NM_032147.3.
    UniGenei Hs.646421.
    Hs.710121.

    3D structure databases

    ProteinModelPortali Q9H0E7.
    SMRi Q9H0E7. Positions 29-86, 268-678.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123890. 12 interactions.
    IntActi Q9H0E7. 11 interactions.
    MINTi MINT-4719317.
    STRINGi 9606.ENSP00000258499.

    Protein family/group databases

    MEROPSi C19.057.

    PTM databases

    PhosphoSitei Q9H0E7.

    Polymorphism databases

    DMDMi 300669621.

    Proteomic databases

    PaxDbi Q9H0E7.
    PRIDEi Q9H0E7.

    Protocols and materials databases

    DNASUi 84101.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258499 ; ENSP00000258499 ; ENSG00000136014 .
    ENST00000393091 ; ENSP00000376806 ; ENSG00000136014 .
    ENST00000537435 ; ENSP00000442629 ; ENSG00000136014 .
    GeneIDi 84101.
    KEGGi hsa:84101.
    UCSCi uc001teg.3. human.

    Organism-specific databases

    CTDi 84101.
    GeneCardsi GC12M095910.
    H-InvDB HIX0010895.
    HGNCi HGNC:20064. USP44.
    HPAi HPA026543.
    MIMi 610993. gene.
    neXtProti NX_Q9H0E7.
    PharmGKBi PA134931457.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5077.
    HOGENOMi HOG000015084.
    HOVERGENi HBG018027.
    InParanoidi Q9H0E7.
    KOi K11834.
    OMAi AIKSQNY.
    OrthoDBi EOG7JX33S.
    PhylomeDBi Q9H0E7.
    TreeFami TF315281.

    Miscellaneous databases

    GeneWikii USP44.
    GenomeRNAii 84101.
    NextBioi 73349.
    PROi Q9H0E7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H0E7.
    Bgeei Q9H0E7.
    CleanExi HS_USP44.
    Genevestigatori Q9H0E7.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-91.
      Tissue: Testis.
    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], VARIANT ALA-91.
      Tissue: Testis.
    3. "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].
    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], VARIANT ALA-91.
      Tissue: Testis.
    5. "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.
    6. "Anaphase initiation is regulated by antagonistic ubiquitination and deubiquitination activities."
      Stegmeier F., Rape M., Draviam V.M., Nalepa G., Sowa M.E., Ang X.L., McDonald E.R. III, Li M.Z., Hannon G.J., Sorger P.K., Kirschner M.W., Harper J.W., Elledge S.J.
      Nature 446:876-881(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-282.
    7. "K48- and K63-linked polyubiquitination of deubiquitinating enzyme USP44."
      Suresh B., Ramakrishna S., Lee H.J., Choi J.H., Kim J.Y., Ahn W.S., Baek K.H.
      Cell Biol. Int. 34:799-808(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF CYS-282.
    8. "A data integration approach to mapping OCT4 gene regulatory networks operative in embryonic stem cells and embryonal carcinoma cells."
      Jung M., Peterson H., Chavez L., Kahlem P., Lehrach H., Vilo J., Adjaye J.
      PLoS ONE 5:E10709-E10709(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "Overexpression of ubiquitin specific protease 44 (USP44) induces chromosomal instability and is frequently observed in human T-cell leukemia."
      Zhang Y., van Deursen J., Galardy P.J.
      PLoS ONE 6:E23389-E23389(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. Cited for: FUNCTION.
    11. "Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit."
      Visconti R., Palazzo L., Della Monica R., Grieco D.
      Nat. Commun. 3:894-894(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-169; SER-239; THR-269 AND SER-401, DEPHOSPHORYLATION.

    Entry informationi

    Entry nameiUBP44_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0E7
    Secondary accession number(s): B2RDW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 116 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3