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Q9UPU5

- UBP24_HUMAN

UniProt

Q9UPU5 - UBP24_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 24

Gene

USP24

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Deubiquitinates DDB2, preventing its proteasomal degradation.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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1698 – 16981NucleophilePROSITE-ProRule annotation
    Active sitei1970 – 19701Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type peptidase activity Source: UniProtKB-KW
    2. ubiquitinyl hydrolase activity Source: InterPro

    GO - Biological processi

    1. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC19.047.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 24 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 24
    Ubiquitin thioesterase 24
    Ubiquitin-specific-processing protease 24
    Gene namesi
    Name:USP24
    Synonyms:KIAA1057
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12623. USP24.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37248.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 26202620Ubiquitin carboxyl-terminal hydrolase 24PRO_0000080652Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631Phosphoserine2 Publications
    Modified residuei942 – 9421PhosphotyrosineBy similarity
    Modified residuei1141 – 11411Phosphoserine1 Publication
    Modified residuei2047 – 20471Phosphoserine7 Publications
    Modified residuei2077 – 20771PhosphoserineBy similarity
    Modified residuei2561 – 25611Phosphoserine1 Publication
    Modified residuei2565 – 25651Phosphothreonine3 Publications
    Modified residuei2604 – 26041Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UPU5.
    PaxDbiQ9UPU5.
    PRIDEiQ9UPU5.

    PTM databases

    PhosphoSiteiQ9UPU5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UPU5.
    BgeeiQ9UPU5.
    CleanExiHS_USP24.
    GenevestigatoriQ9UPU5.

    Organism-specific databases

    HPAiHPA026723.
    HPA028428.

    Interactioni

    Protein-protein interaction databases

    BioGridi116939. 9 interactions.
    IntActiQ9UPU5. 5 interactions.
    MINTiMINT-7945132.
    STRINGi9606.ENSP00000385700.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UPU5.
    SMRiQ9UPU5. Positions 1677-2043.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 4442UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini1689 – 2042354USPAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi47 – 9448Gly-richAdd
    BLAST
    Compositional biasi1035 – 106228Ser-richAdd
    BLAST
    Compositional biasi1132 – 116433Ser-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5077.
    HOGENOMiHOG000068011.
    HOVERGENiHBG105784.
    InParanoidiQ9UPU5.
    KOiK11840.
    OMAiCMEYFDL.
    OrthoDBiEOG712TV9.
    PhylomeDBiQ9UPU5.
    TreeFamiTF323966.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR029071. Ubiquitin-rel_dom.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    SSF48371. SSF48371. 2 hits.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50030. UBA. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UPU5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESEEEQHMT TLLCMGFSDP ATIRKALRLA KNDINEAVAL LTNERPGLDY     50
    GGYEPMDSGG GPSPGPGGGP RGDGGGDGGG GGPSRGGSTG GGGGFDPPPA 100
    YHEVVDAEKN DENGNCSGEG IEFPTTNLYE LESRVLTDHW SIPYKREESL 150
    GKCLLASTYL ARLGLSESDE NCRRFMDRCM PEAFKKLLTS SAVHKWGTEI 200
    HEGIYNMLML LIELVAERIK QDPIPTGLLG VLTMAFNPDN EYHFKNRMKV 250
    SQRNWAEVFG EGNMFAVSPV STFQKEPHGW VVDLVNKFGE LGGFAAIQAK 300
    LHSEDIELGA VSALIQPLGV CAEYLNSSVV QPMLDPVILT TIQDVRSVEE 350
    KDLKDKRLVS IPELLSAVKL LCMRFQPDLV TIVDDLRLDI LLRMLKSPHF 400
    SAKMNSLKEV TKLIEDSTLS KSVKNAIDTD RLLDWLVENS VLSIALEGNI 450
    DQAQYCDRIK GIIELLGSKL SLDELTKIWK IQSGQSSTVI ENIHTIIAAA 500
    AVKFNSDQLN HLFVLIQKSW ETESDRVRQK LLSLIGRIGR EARFETTSGK 550
    VLDVLWELAH LPTLPSSLIQ QALEEHLTIL SDAYAVKEAI KRSYIIKCIE 600
    DIKRPGEWSG LEKNKKDGFK SSQLNNPQFV WVVPALRQLH EITRSFIKQT 650
    YQKQDKSIIQ DLKKNFEIVK LVTGSLIACH RLAAAVAGPG GLSGSTLVDG 700
    RYTYREYLEA HLKFLAFFLQ EATLYLGWNR AKEIWECLVT GQDVCELDRE 750
    MCFEWFTKGQ HDLESDVQQQ LFKEKILKLE SYEITMNGFN LFKTFFENVN 800
    LCDHRLKRQG AQLYVEKLEL IGMDFIWKIA MESPDEEIAN EAIQLIINYS 850
    YINLNPRLKK DSVSLHKKFI ADCYTRLEAA SSALGGPTLT HAVTRATKML 900
    TATAMPTVAT SVQSPYRSTK LVIIERLLLL AERYVITIED FYSVPRTILP 950
    HGASFHGHLL TLNVTYESTK DTFTVEAHSN ETIGSVRWKI AKQLCSPVDN 1000
    IQIFTNDSLL TVNKDQKLLH QLGFSDEQIL TVKTSGSGTP SGSSADSSTS 1050
    SSSSSSGVFS SSYAMEQEKS LPGVVMALVC NVFDMLYQLA NLEEPRITLR 1100
    VRKLLLLIPT DPAIQEALDQ LDSLGRKKTL LSESSSQSSK SPSLSSKQQH 1150
    QPSASSILES LFRSFAPGMS TFRVLYNLEV LSSKLMPTAD DDMARSCAKS 1200
    FCENFLKAGG LSLVVNVMQR DSIPSEVDYE TRQGVYSICL QLARFLLVGQ 1250
    TMPTLLDEDL TKDGIEALSS RPFRNVSRQT SRQMSLCGTP EKSSYRQLSV 1300
    SDRSSIRVEE IIPAARVAIQ TMEVSDFTST VACFMRLSWA AAAGRLDLVG 1350
    SSQPIKESNS LCPAGIRNRL SSSGSNCSSG SEGEPVALHA GICVRQQSVS 1400
    TKDSLIAGEA LSLLVTCLQL RSQQLASFYN LPCVADFIID ILLGSPSAEI 1450
    RRVACDQLYT LSQTDTSAHP DVQKPNQFLL GVILTAQLPL WSPTSIMRGV 1500
    NQRLLSQCME YFDLRCQLLD DLTTSEMEQL RISPATMLED EITWLDNFEP 1550
    NRTAECETSE ADNILLAGHL RLIKTLLSLC GAEKEMLGSS LIKPLLDDFL 1600
    FRASRIILNS HSPAGSAAIS QQDFHPKCST ANSRLAAYEV LVMLADSSPS 1650
    NLQIIIKELL SMHHQPDPAL TKEFDYLPPV DSRSSSGFVG LRNGGATCYM 1700
    NAVFQQLYMQ PGLPESLLSV DDDTDNPDDS VFYQVQSLFG HLMESKLQYY 1750
    VPENFWKIFK MWNKELYVRE QQDAYEFFTS LIDQMDEYLK KMGRDQIFKN 1800
    TFQGIYSDQK ICKDCPHRYE REEAFMALNL GVTSCQSLEI SLDQFVRGEV 1850
    LEGSNAYYCE KCKEKRITVK RTCIKSLPSV LVIHLMRFGF DWESGRSIKY 1900
    DEQIRFPWML NMEPYTVSGM ARQDSSSEVG ENGRSVDQGG GGSPRKKVAL 1950
    TENYELVGVI VHSGQAHAGH YYSFIKDRRG CGKGKWYKFN DTVIEEFDLN 2000
    DETLEYECFG GEYRPKVYDQ TNPYTDVRRR YWNAYMLFYQ RVSDQNSPVL 2050
    PKKSRVSVVR QEAEDLSLSA PSSPEISPQS SPRPHRPNND RLSILTKLVK 2100
    KGEKKGLFVE KMPARIYQMV RDENLKFMKN RDVYSSDYFS FVLSLASLNA 2150
    TKLKHPYYPC MAKVSLQLAI QFLFQTYLRT KKKLRVDTEE WIATIEALLS 2200
    KSFDACQWLV EYFISSEGRE LIKIFLLECN VREVRVAVAT ILEKTLDSAL 2250
    FYQDKLKSLH QLLEVLLALL DKDVPENCKN CAQYFFLFNT FVQKQGIRAG 2300
    DLLLRHSALR HMISFLLGAS RQNNQIRRWS SAQAREFGNL HNTVALLVLH 2350
    SDVSSQRNVA PGIFKQRPPI SIAPSSPLLP LHEEVEALLF MSEGKPYLLE 2400
    VMFALRELTG SLLALIEMVV YCCFCNEHFS FTMLHFIKNQ LETAPPHELK 2450
    NTFQLLHEIL VIEDPIQVER VKFVFETENG LLALMHHSNH VDSSRCYQCV 2500
    KFLVTLAQKC PAAKEYFKEN SHHWSWAVQW LQKKMSEHYW TPQSNVSNET 2550
    STGKTFQRTI SAQDTLAYAT ALLNEKEQSG SSNGSESSPA NENGDRHLQQ 2600
    GSESPMMIGE LRSDLDDVDP 2620
    Length:2,620
    Mass (Da):294,365
    Last modified:November 4, 2008 - v3
    Checksum:i2773B7857A8B6633
    GO

    Sequence cautioni

    The sequence AAH29660.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA91084.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti840 – 8401N → S in BAC86814. (PubMed:14702039)Curated
    Sequence conflicti990 – 9901I → L in BAC86814. (PubMed:14702039)Curated
    Sequence conflicti1253 – 12531P → S in BAC86814. (PubMed:14702039)Curated
    Sequence conflicti1776 – 17761E → G in BAC86814. (PubMed:14702039)Curated
    Sequence conflicti2576 – 25761K → R in BAA91084. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti226 – 2261T → I.
    Corresponds to variant rs1165222 [ dbSNP | Ensembl ].
    VAR_047154
    Natural varianti1940 – 19401G → S.
    Corresponds to variant rs2274540 [ dbSNP | Ensembl ].
    VAR_047155
    Natural varianti2134 – 21341Y → S.
    Corresponds to variant rs12753590 [ dbSNP | Ensembl ].
    VAR_047156
    Natural varianti2468 – 24681V → A.2 Publications
    Corresponds to variant rs487230 [ dbSNP | Ensembl ].
    VAR_047157

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC091609 Genomic DNA. No translation available.
    AK000321 mRNA. Translation: BAA91084.1. Different initiation.
    AK127075 mRNA. Translation: BAC86814.1.
    AB028980 mRNA. Translation: BAA83009.1.
    BC029660 mRNA. Translation: AAH29660.1. Different initiation.
    CCDSiCCDS44154.2.
    RefSeqiNP_056121.2. NM_015306.2.
    UniGeneiHs.477009.

    Genome annotation databases

    EnsembliENST00000294383; ENSP00000294383; ENSG00000162402.
    GeneIDi23358.
    KEGGihsa:23358.
    UCSCiuc021onw.1. human.

    Polymorphism databases

    DMDMi212276491.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC091609 Genomic DNA. No translation available.
    AK000321 mRNA. Translation: BAA91084.1 . Different initiation.
    AK127075 mRNA. Translation: BAC86814.1 .
    AB028980 mRNA. Translation: BAA83009.1 .
    BC029660 mRNA. Translation: AAH29660.1 . Different initiation.
    CCDSi CCDS44154.2.
    RefSeqi NP_056121.2. NM_015306.2.
    UniGenei Hs.477009.

    3D structure databases

    ProteinModelPortali Q9UPU5.
    SMRi Q9UPU5. Positions 1677-2043.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116939. 9 interactions.
    IntActi Q9UPU5. 5 interactions.
    MINTi MINT-7945132.
    STRINGi 9606.ENSP00000385700.

    Protein family/group databases

    MEROPSi C19.047.

    PTM databases

    PhosphoSitei Q9UPU5.

    Polymorphism databases

    DMDMi 212276491.

    Proteomic databases

    MaxQBi Q9UPU5.
    PaxDbi Q9UPU5.
    PRIDEi Q9UPU5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000294383 ; ENSP00000294383 ; ENSG00000162402 .
    GeneIDi 23358.
    KEGGi hsa:23358.
    UCSCi uc021onw.1. human.

    Organism-specific databases

    CTDi 23358.
    GeneCardsi GC01M055536.
    H-InvDB HIX0000626.
    HGNCi HGNC:12623. USP24.
    HPAi HPA026723.
    HPA028428.
    MIMi 610569. gene.
    neXtProti NX_Q9UPU5.
    PharmGKBi PA37248.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5077.
    HOGENOMi HOG000068011.
    HOVERGENi HBG105784.
    InParanoidi Q9UPU5.
    KOi K11840.
    OMAi CMEYFDL.
    OrthoDBi EOG712TV9.
    PhylomeDBi Q9UPU5.
    TreeFami TF323966.

    Miscellaneous databases

    ChiTaRSi USP24. human.
    GeneWikii USP24.
    GenomeRNAii 23358.
    NextBioi 45380.
    PROi Q9UPU5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UPU5.
    Bgeei Q9UPU5.
    CleanExi HS_USP24.
    Genevestigatori Q9UPU5.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR029071. Ubiquitin-rel_dom.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    SSF48371. SSF48371. 2 hits.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50030. UBA. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] OF 751-2082 AND 2256-2620, VARIANT ALA-2468.
    3. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2233-2620, VARIANT ALA-2468.
      Tissue: Brain.
    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] OF 1483-2620.
      Tissue: Placenta.
    5. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-1141; SER-2047; THR-2565 AND SER-2604, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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].
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2047, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-2561, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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-2047 AND THR-2565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-2047 AND THR-2565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "The deubiquitinating protein USP24 interacts with DDB2 and regulates DDB2 stability."
      Zhang L., Lubin A., Chen H., Sun Z., Gong F.
      Cell Cycle 11:4378-4384(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBP24_HUMAN
    AccessioniPrimary (citable) accession number: Q9UPU5
    Secondary accession number(s): Q6ZSY2, Q8N2Y4, Q9NXD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 130 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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