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Q70CQ2

- UBP34_HUMAN

UniProt

Q70CQ2 - UBP34_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 34

Gene

USP34

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    Ubiquitin hydrolase that can remove conjugated ubiquitin from AXIN1 and AXIN2, thereby acting as a regulator of Wnt signaling pathway. Acts as an activator of the Wnt signaling pathway downstream of the beta-catenin destruction complex by deubiquitinating and stabilizing AXIN1 and AXIN2, leading to promote nuclear accumulation of AXIN1 and AXIN2 and positively regulate beta-catenin (CTNBB1)-mediated transcription. Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.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).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1903 – 19031NucleophileCurated
    Active sitei2164 – 21641Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
    2. protein deubiquitination Source: FlyBase
    3. protein K48-linked deubiquitination Source: UniProtKB
    4. ubiquitin-dependent protein catabolic process Source: InterPro
    5. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway, Wnt signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_200777. TCF dependent signaling in response to WNT.

    Protein family/group databases

    MEROPSiC19.067.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 34 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 34
    Ubiquitin thioesterase 34
    Ubiquitin-specific-processing protease 34
    Gene namesi
    Name:USP34
    Synonyms:KIAA0570, KIAA0729
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:20066. USP34.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1903 – 19031C → S: Loss of function. 1 Publication

    Organism-specific databases

    PharmGKBiPA134897042.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 35463546Ubiquitin carboxyl-terminal hydrolase 34PRO_0000249519Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei352 – 3521Phosphoserine1 Publication
    Modified residuei649 – 6491Phosphoserine1 Publication
    Modified residuei2488 – 24881Phosphoserine1 Publication
    Modified residuei3358 – 33581Phosphoserine1 Publication
    Modified residuei3359 – 33591Phosphoserine1 Publication
    Modified residuei3406 – 34061Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ70CQ2.
    PaxDbiQ70CQ2.
    PRIDEiQ70CQ2.

    PTM databases

    PhosphoSiteiQ70CQ2.

    Expressioni

    Tissue specificityi

    Expressed in brain at low level.1 Publication

    Gene expression databases

    ArrayExpressiQ70CQ2.
    BgeeiQ70CQ2.
    CleanExiHS_USP34.
    GenevestigatoriQ70CQ2.

    Organism-specific databases

    HPAiHPA025815.

    Interactioni

    Subunit structurei

    Interacts with AXIN1 and AXIN2.1 Publication

    Protein-protein interaction databases

    BioGridi115085. 39 interactions.
    IntActiQ70CQ2. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ70CQ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1894 – 2239346USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiCOG5077.
    HOVERGENiHBG092616.
    InParanoidiQ70CQ2.
    KOiK11853.
    OMAiCLISKTE.
    PhylomeDBiQ70CQ2.
    TreeFamiTF323966.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 4 hits.
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q70CQ2-1) [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

    MCENCADLVE VLNEISDVEG GDGLQLRKEH TLKIFTYINS WTQRQCLCCF     50
    KEYKHLEIFN QVVCALINLV IAQVQVLRDQ LCKHCTTINI DSTWQDESNQ 100
    AEEPLNIDRE CNEGSTERQK SIEKKSNSTR ICNLTEEESS KSSDPFSLWS 150
    TDEKEKLLLC VAKIFQIQFP LYTAYKHNTH PTIEDISTQE SNILGAFCDM 200
    NDVEVPLHLL RYVCLFCGKN GLSLMKDCFE YGTPETLPFL IAHAFITVVS 250
    NIRIWLHIPA VMQHIIPFRT YVIRYLCKLS DQELRQSAAR NMADLMWSTV 300
    KEPLDTTLCF DKESLDLAFK YFMSPTLTMR LAGLSQITNQ LHTFNDVCNN 350
    ESLVSDTETS IAKELADWLI SNNVVEHIFG PNLHIEIIKQ CQVILNFLAA 400
    EGRLSTQHID CIWAAAQLKH CSRYIHDLFP SLIKNLDPVP LRHLLNLVSA 450
    LEPSVHTEQT LYLASMLIKA LWNNALAAKA QLSKQSSFAS LLNTNIPIGN 500
    KKEEEELRRT APSPWSPAAS PQSSDNSDTH QSGGSDIEMD EQLINRTKHV 550
    QQRLSDTEES MQGSSDETAN SGEDGSSGPG SSSGHSDGSS NEVNSSHASQ 600
    SAGSPGSEVQ SEDIADIEAL KEEDEDDDHG HNPPKSSCGT DLRNRKLESQ 650
    AGICLGDSQG MSERNGTSSG TGKDLVFNTE SLPSVDNRMR MLDACSHSED 700
    PEHDISGEMN ATHIAQGSQE SCITRTGDFL GETIGNELFN CRQFIGPQHH 750
    HHHHHHHHHH DGHMVDDMLS ADDVSCSSSQ VSAKSEKNMA DFDGEESGCE 800
    EELVQINSHA ELTSHLQQHL PNLASIYHEH LSQGPVVHKH QFNSNAVTDI 850
    NLDNVCKKGN TLLWDIVQDE DAVNLSEGLI NEAEKLLCSL VCWFTDRQIR 900
    MRFIEGCLEN LGNNRSVVIS LRLLPKLFGT FQQFGSSYDT HWITMWAEKE 950
    LNMMKLFFDN LVYYIQTVRE GRQKHALYSH SAEVQVRLQF LTCVFSTLGS 1000
    PDHFRLSLEQ VDILWHCLVE DSECYDDALH WFLNQVRSKD QHAMGMETYK 1050
    HLFLEKMPQL KPETISMTGL NLFQHLCNLA RLATSAYDGC SNSELCGMDQ 1100
    FWGIALRAQS GDVSRAAIQY INSYYINGKT GLEKEQEFIS KCMESLMIAS 1150
    SSLEQESHSS LMVIERGLLM LKTHLEAFRR RFAYHLRQWQ IEGTGISSHL 1200
    KALSDKQSLP LRVVCQPAGL PDKMTIEMYP SDQVADLRAE VTHWYENLQK 1250
    EQINQQAQLQ EFGQSNRKGE FPGGLMGPVR MISSGHELTT DYDEKALHEL 1300
    GFKDMQMVFV SLGAPRRERK GEGVQLPASC LPPPQKDNIP MLLLLQEPHL 1350
    TTLFDLLEML ASFKPPSGKV AVDDSESLRC EELHLHAENL SRRVWELLML 1400
    LPTCPNMLMA FQNISDEQSN DGFNWKELLK IKSAHKLLYA LEIIEALGKP 1450
    NRRIRRESTG SYSDLYPDSD DSSEDQVENS KNSWSCKFVA AGGLQQLLEI 1500
    FNSGILEPKE QESWTVWQLD CLACLLKLIC QFAVDPSDLD LAYHDVFAWS 1550
    GIAESHRKRT WPGKSRKAAG DHAKGLHIPR LTEVFLVLVQ GTSLIQRLMS 1600
    VAYTYDNLAP RVLKAQSDHR SRHEVSHYSM WLLVSWAHCC SLVKSSLADS 1650
    DHLQDWLKKL TLLIPETAVR HESCSGLYKL SLSGLDGGDS INRSFLLLAA 1700
    STLLKFLPDA QALKPIRIDD YEEEPILKPG CKEYFWLLCK LVDNIHIKDA 1750
    SQTTLLDLDA LARHLADCIR SREILDHQDG NVEDDGLTGL LRLATSVVKH 1800
    KPPFKFSREG QEFLRDIFNL LFLLPSLKDR QQPKCKSHSS RAAAYDLLVE 1850
    MVKGSVENYR LIHNWVMAQH MQSHAPYKWD YWPHEDVRAE CRFVGLTNLG 1900
    ATCYLASTIQ QLYMIPEARQ AVFTAKYSED MKHKTTLLEL QKMFTYLMES 1950
    ECKAYNPRPF CKTYTMDKQP LNTGEQKDMT EFFTDLITKI EEMSPELKNT 2000
    VKSLFGGVIT NNVVSLDCEH VSQTAEEFYT VRCQVADMKN IYESLDEVTI 2050
    KDTLEGDNMY TCSHCGKKVR AEKRACFKKL PRILSFNTMR YTFNMVTMMK 2100
    EKVNTHFSFP LRLDMTPYTE DFLMGKSERK EGFKEVSDHS KDSESYEYDL 2150
    IGVTVHTGTA DGGHYYSFIR DIVNPHAYKN NKWYLFNDAE VKPFDSAQLA 2200
    SECFGGEMTT KTYDSVTDKF MDFSFEKTHS AYMLFYKRME PEEENGREYK 2250
    FDVSSELLEW IWHDNMQFLQ DKNIFEHTYF GFMWQLCSCI PSTLPDPKAV 2300
    SLMTAKLSTS FVLETFIHSK EKPTMLQWIE LLTKQFNNSQ AACEWFLDRM 2350
    ADDDWWPMQI LIKCPNQIVR QMFQRLCIHV IQRLRPVHAH LYLQPGMEDG 2400
    SDDMDTSVED IGGRSCVTRF VRTLLLIMEH GVKPHSKHLT EYFAFLYEFA 2450
    KMGEEESQFL LSLQAISTMV HFYMGTKGPE NPQVEVLSEE EGEEEEEEED 2500
    ILSLAEEKYR PAALEKMIAL VALLVEQSRS ERHLTLSQTD MAALTGGKGF 2550
    PFLFQHIRDG INIRQTCNLI FSLCRYNNRL AEHIVSMLFT SIAKLTPEAA 2600
    NPFFKLLTML MEFAGGPPGM PPFASYILQR IWEVIEYNPS QCLDWLAVQT 2650
    PRNKLAHSWV LQNMENWVER FLLAHNYPRV RTSAAYLLVS LIPSNSFRQM 2700
    FRSTRSLHIP TRDLPLSPDT TVVLHQVYNV LLGLLSRAKL YVDAAVHGTT 2750
    KLVPYFSFMT YCLISKTEKL MFSTYFMDLW NLFQPKLSEP AIATNHNKQA 2800
    LLSFWYNVCA DCPENIRLIV QNPVVTKNIA FNYILADHDD QDVVLFNRGM 2850
    LPAYYGILRL CCEQSPAFTR QLASHQNIQW AFKNLTPHAS QYPGAVEELF 2900
    NLMQLFIAQR PDMREEELED IKQFKKTTIS CYLRCLDGRS CWTTLISAFR 2950
    ILLESDEDRL LVVFNRGLIL MTESFNTLHM MYHEATACHV TGDLVELLSI 3000
    FLSVLKSTRP YLQRKDVKQA LIQWQERIEF AHKLLTLLNS YSPPELRNAC 3050
    IDVLKELVLL SPHDFLHTLV PFLQHNHCTY HHSNIPMSLG PYFPCRENIK 3100
    LIGGKSNIRP PRPELNMCLL PTMVETSKGK DDVYDRMLLD YFFSYHQFIH 3150
    LLCRVAINCE KFTETLVKLS VLVAYEGLPL HLALFPKLWT ELCQTQSAMS 3200
    KNCIKLLCED PVFAEYIKCI LMDERTFLNN NIVYTFMTHF LLKVQSQVFS 3250
    EANCANLIST LITNLISQYQ NLQSDFSNRV EISKASASLN GDLRALALLL 3300
    SVHTPKQLNP ALIPTLQELL SKCRTCLQQR NSLQEQEAKE RKTKDDEGAT 3350
    PIKRRRVSSD EEHTVDSCIS DMKTETREVL TPTSTSDNET RDSSIIDPGT 3400
    EQDLPSPENS SVKEYRMEVP SSFSEDMSNI RSQHAEEQSN NGRYDDCKEF 3450
    KDLHCSKDST LAEEESEFPS TSISAVLSDL ADLRSCDGQA LPSQDPEVAL 3500
    SLSCGHSRGL FSHMQQHDIL DTLCRTIEST IHVVTRISGK GNQAAS 3546
    Length:3,546
    Mass (Da):404,233
    Last modified:November 4, 2008 - v2
    Checksum:iA31851911D990044
    GO
    Isoform 2 (identifier: Q70CQ2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-139: Missing.
         140-162: SKSSDPFSLWSTDEKEKLLLCVA → MRRKNSYYVWQ

    Show »
    Length:3,395
    Mass (Da):387,154
    Checksum:i6171809F72C5EE8E
    GO
    Isoform 3 (identifier: Q70CQ2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-139: Missing.
         140-162: SKSSDPFSLWSTDEKEKLLLCVA → MRRKNSYYVWQ
         2936-3018: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:3,312
    Mass (Da):377,599
    Checksum:i4815E0ED77EC1C03
    GO

    Sequence cautioni

    The sequence AAI07762.1 differs from that shown. Reason: Frameshift at position 3200.
    The sequence BAA25496.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAG54261.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti661 – 6611M → T.3 Publications
    Corresponds to variant rs6722430 [ dbSNP | Ensembl ].
    VAR_047106
    Natural varianti1663 – 16631L → R.
    Corresponds to variant rs6723818 [ dbSNP | Ensembl ].
    VAR_047107
    Natural varianti2348 – 23481D → N.
    Corresponds to variant rs4386306 [ dbSNP | Ensembl ].
    VAR_047108

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 139139Missing in isoform 2 and isoform 3. 4 PublicationsVSP_035639Add
    BLAST
    Alternative sequencei140 – 16223SKSSD…LLCVA → MRRKNSYYVWQ in isoform 2 and isoform 3. 4 PublicationsVSP_035640Add
    BLAST
    Alternative sequencei2936 – 301883Missing in isoform 3. 1 PublicationVSP_020463Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ586138 mRNA. Translation: CAE51938.1.
    AB011142 mRNA. Translation: BAA25496.2. Different initiation.
    AC016747 Genomic DNA. No translation available.
    AL050092 mRNA. Translation: CAB43264.1.
    AL831918 mRNA. Translation: CAD38579.1.
    AK125898 mRNA. Translation: BAG54261.1. Different initiation.
    AB018272 mRNA. Translation: BAA34449.1.
    BC022783 mRNA. Translation: AAH22783.1.
    BC062325 mRNA. Translation: AAH62325.1.
    BC107761 mRNA. Translation: AAI07762.1. Frameshift.
    CCDSiCCDS42686.1. [Q70CQ2-1]
    PIRiT00338.
    T13057.
    RefSeqiNP_055524.3. NM_014709.3. [Q70CQ2-1]
    UniGeneiHs.644708.

    Genome annotation databases

    EnsembliENST00000398571; ENSP00000381577; ENSG00000115464. [Q70CQ2-1]
    ENST00000453734; ENSP00000410559; ENSG00000115464.
    GeneIDi9736.
    KEGGihsa:9736.
    UCSCiuc002sbe.3. human. [Q70CQ2-1]

    Polymorphism databases

    DMDMi212276488.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ586138 mRNA. Translation: CAE51938.1 .
    AB011142 mRNA. Translation: BAA25496.2 . Different initiation.
    AC016747 Genomic DNA. No translation available.
    AL050092 mRNA. Translation: CAB43264.1 .
    AL831918 mRNA. Translation: CAD38579.1 .
    AK125898 mRNA. Translation: BAG54261.1 . Different initiation.
    AB018272 mRNA. Translation: BAA34449.1 .
    BC022783 mRNA. Translation: AAH22783.1 .
    BC062325 mRNA. Translation: AAH62325.1 .
    BC107761 mRNA. Translation: AAI07762.1 . Frameshift.
    CCDSi CCDS42686.1. [Q70CQ2-1 ]
    PIRi T00338.
    T13057.
    RefSeqi NP_055524.3. NM_014709.3. [Q70CQ2-1 ]
    UniGenei Hs.644708.

    3D structure databases

    ProteinModelPortali Q70CQ2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115085. 39 interactions.
    IntActi Q70CQ2. 2 interactions.

    Protein family/group databases

    MEROPSi C19.067.

    PTM databases

    PhosphoSitei Q70CQ2.

    Polymorphism databases

    DMDMi 212276488.

    Proteomic databases

    MaxQBi Q70CQ2.
    PaxDbi Q70CQ2.
    PRIDEi Q70CQ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398571 ; ENSP00000381577 ; ENSG00000115464 . [Q70CQ2-1 ]
    ENST00000453734 ; ENSP00000410559 ; ENSG00000115464 .
    GeneIDi 9736.
    KEGGi hsa:9736.
    UCSCi uc002sbe.3. human. [Q70CQ2-1 ]

    Organism-specific databases

    CTDi 9736.
    GeneCardsi GC02M061414.
    H-InvDB HIX0002082.
    HIX0161884.
    HGNCi HGNC:20066. USP34.
    HPAi HPA025815.
    MIMi 615295. gene.
    neXtProti NX_Q70CQ2.
    PharmGKBi PA134897042.
    HUGEi Search...
    Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5077.
    HOVERGENi HBG092616.
    InParanoidi Q70CQ2.
    KOi K11853.
    OMAi CLISKTE.
    PhylomeDBi Q70CQ2.
    TreeFami TF323966.

    Enzyme and pathway databases

    Reactomei REACT_200777. TCF dependent signaling in response to WNT.

    Miscellaneous databases

    ChiTaRSi USP34. human.
    GeneWikii USP34.
    GenomeRNAii 9736.
    NextBioi 36636.
    PROi Q70CQ2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q70CQ2.
    Bgeei Q70CQ2.
    CleanExi HS_USP34.
    Genevestigatori Q70CQ2.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 4 hits.
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, ENZYME ACTIVITY, VARIANT THR-661.
    2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-661.
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1723-2532 AND 2629-3546 (ISOFORM 1).
      Tissue: Amygdala and Uterus.
    6. "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 1821-3338.
      Tissue: Testis.
    7. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2351-3546 (ISOFORM 2).
      Tissue: Brain.
    8. "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 2561-3546 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3024-3546 (ISOFORM 3).
      Tissue: Brain, Colon and Kidney.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, VARIANT [LARGE SCALE ANALYSIS] THR-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352; SER-3358; SER-3359 AND SER-3406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-2488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The Ubiquitin specific protease USP34 regulates Axin stability and Wnt/beta-catenin signaling."
      Lui T.T., Lacroix C., Ahmed S.M., Goldenberg S.J., Leach C.A., Daulat A.M., Angers S.
      Mol. Cell. Biol. 31:2053-2065(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH AXIN1 AND AXIN2, MUTAGENESIS OF CYS-1903.

    Entry informationi

    Entry nameiUBP34_HUMAN
    AccessioniPrimary (citable) accession number: Q70CQ2
    Secondary accession number(s): A8MWD0
    , B3KWU9, O60316, O94834, Q3B777, Q6P6C9, Q7L8P6, Q8N3T9, Q8TBW2, Q9UGA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 94 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 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. 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