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Q9H9J4

- UBP42_HUMAN

UniProt

Q9H9J4 - UBP42_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 42

Gene

USP42

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (08 Feb 2011)
      Previous versions | rss
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    Functioni

    Deubiquitinating enzyme which may play an important role during spermatogenesis.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).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei120 – 1201NucleophilePROSITE-ProRule annotation
    Active sitei371 – 3711Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ubiquitin-specific protease activity Source: FlyBase

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. protein deubiquitination Source: UniProtKB
    3. spermatogenesis Source: UniProtKB-KW
    4. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Differentiation, Spermatogenesis, Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC19.048.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 42 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 42
    Ubiquitin thioesterase 42
    Ubiquitin-specific-processing protease 42
    Gene namesi
    Name:USP42
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:20068. USP42.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134902515.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13241324Ubiquitin carboxyl-terminal hydrolase 42PRO_0000080672Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei856 – 8561Phosphoserine4 Publications
    Modified residuei1226 – 12261Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H9J4.
    PaxDbiQ9H9J4.
    PRIDEiQ9H9J4.

    PTM databases

    PhosphoSiteiQ9H9J4.

    Miscellaneous databases

    PMAP-CutDBQ9H9J4.

    Expressioni

    Tissue specificityi

    Broadly expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9H9J4.
    BgeeiQ9H9J4.
    CleanExiHS_USP42.
    GenevestigatoriQ9H9J4.

    Organism-specific databases

    HPAiHPA006752.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TP53P046372EBI-2513638,EBI-366083

    Protein-protein interaction databases

    BioGridi123904. 30 interactions.
    IntActiQ9H9J4. 27 interactions.
    MINTiMINT-7899498.
    STRINGi9606.ENSP00000301962.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H9J4.
    SMRiQ9H9J4. Positions 111-409.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 412302USPAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi742 – 937196Pro-richAdd
    BLAST
    Compositional biasi946 – 1118173Arg-richAdd
    BLAST
    Compositional biasi1176 – 124671Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5533.
    HOGENOMiHOG000236355.
    HOVERGENiHBG080724.
    InParanoidiQ9H9J4.
    KOiK11855.
    OMAiGKLMPAP.
    OrthoDBiEOG72VH5K.
    PhylomeDBiQ9H9J4.
    TreeFamiTF315281.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    [Graphical view]
    PROSITEiPS00972. 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: Q9H9J4-1) [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

    MTIVDKASES SDPSAYQNQP GSSEAVSPGD MDAGSASWGA VSSLNDVSNH     50
    TLSLGPVPGA VVYSSSSVPD KSKPSPQKDQ ALGDGIAPPQ KVLFPSEKIC 100
    LKWQQTHRVG AGLQNLGNTC FANAALQCLT YTPPLANYML SHEHSKTCHA 150
    EGFCMMCTMQ AHITQALSNP GDVIKPMFVI NEMRRIARHF RFGNQEDAHE 200
    FLQYTVDAMQ KACLNGSNKL DRHTQATTLV CQIFGGYLRS RVKCLNCKGV 250
    SDTFDPYLDI TLEIKAAQSV NKALEQFVKP EQLDGENSYK CSKCKKMVPA 300
    SKRFTIHRSS NVLTLSLKRF ANFTGGKIAK DVKYPEYLDI RPYMSQPNGE 350
    PIVYVLYAVL VHTGFNCHAG HYFCYIKASN GLWYQMNDSI VSTSDIRSVL 400
    SQQAYVLFYI RSHDVKNGGE LTHPTHSPGQ SSPRPVISQR VVTNKQAAPG 450
    FIGPQLPSHM IKNPPHLNGT GPLKDTPSSS MSSPNGNSSV NRASPVNASA 500
    SVQNWSVNRS SVIPEHPKKQ KITISIHNKL PVRQCQSQPN LHSNSLENPT 550
    KPVPSSTITN SAVQSTSNAS TMSVSSKVTK PIPRSESCSQ PVMNGKSKLN 600
    SSVLVPYGAE SSEDSDEESK GLGKENGIGT IVSSHSPGQD AEDEEATPHE 650
    LQEPMTLNGA NSADSDSDPK ENGLAPDGAS CQGQPALHSE NPFAKANGLP 700
    GKLMPAPLLS LPEDKILETF RLSNKLKGST DEMSAPGAER GPPEDRDAEP 750
    QPGSPAAESL EEPDAAAGLS STKKAPPPRD PGTPATKEGA WEAMAVAPEE 800
    PPPSAGEDIV GDTAPPDLCD PGSLTGDASP LSQDAKGMIA EGPRDSALAE 850
    APEGLSPAPP ARSEEPCEQP LLVHPSGDHA RDAQDPSQSL GAPEAAERPP 900
    APVLDMAPAG HPEGDAEPSP GERVEDAAAP KAPGPSPAKE KIGSLRKVDR 950
    GHYRSRRERS SSGEPARESR SKTEGHRHRR RRTCPRERDR QDRHAPEHHP 1000
    GHGDRLSPGE RRSLGRCSHH HSRHRSGVEL DWVRHHYTEG ERGWGREKFY 1050
    PDRPRWDRCR YYHDRYALYA ARDWKPFHGG REHERAGLHE RPHKDHNRGR 1100
    RGCEPARERE RHRPSSPRAG APHALAPHPD RFSHDRTALV AGDNCNLSDR 1150
    FHEHENGKSR KRRHDSVENS DSHVEKKARR SEQKDPLEEP KAKKHKKSKK 1200
    KKKSKDKHRD RDSRHQQDSD LSAACSDADL HRHKKKKKKK KRHSRKSEDF 1250
    VKDSELHLPR VTSLETVAQF RRAQGGFPLS GGPPLEGVGP FREKTKHLRM 1300
    ESRDDRCRLF EYGQGKRRYL ELGR 1324
    Length:1,324
    Mass (Da):145,392
    Last modified:February 8, 2011 - v3
    Checksum:i6EB4975521ABF516
    GO
    Isoform 2 (identifier: Q9H9J4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1316-1324: KRRYLELGR → D

    Show »
    Length:1,316
    Mass (Da):144,335
    Checksum:i28998E673C8EFE3B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti655 – 6551M → T in CAE53097. (PubMed:14715245)Curated
    Sequence conflicti655 – 6551M → T in BAB14232. (PubMed:14702039)Curated
    Sequence conflicti1214 – 12141R → RR in CAE53097. (PubMed:14715245)Curated
    Sequence conflicti1217 – 12171Q → R in AAT67238. (PubMed:15489334)Curated
    Sequence conflicti1294 – 12941K → E in AAT67238. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1030 – 10301L → P.
    Corresponds to variant rs6463529 [ dbSNP | Ensembl ].
    VAR_059754

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1316 – 13249KRRYLELGR → D in isoform 2. 1 PublicationVSP_040529

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ601395 mRNA. Translation: CAE53097.1.
    AY618868 mRNA. Translation: AAT67238.1.
    AC004895 Genomic DNA. No translation available.
    BC060846 mRNA. Translation: AAH60846.2.
    BC132862 mRNA. Translation: AAI32863.1.
    AK022759 mRNA. Translation: BAB14232.1.
    CCDSiCCDS47535.1. [Q9H9J4-2]
    RefSeqiNP_115548.1. NM_032172.2. [Q9H9J4-2]
    XP_005249939.1. XM_005249882.2. [Q9H9J4-1]
    UniGeneiHs.31856.

    Genome annotation databases

    EnsembliENST00000306177; ENSP00000301962; ENSG00000106346. [Q9H9J4-2]
    GeneIDi84132.
    KEGGihsa:84132.
    UCSCiuc011jwo.1. human. [Q9H9J4-1]
    uc011jwp.2. human. [Q9H9J4-2]

    Polymorphism databases

    DMDMi322510098.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ601395 mRNA. Translation: CAE53097.1 .
    AY618868 mRNA. Translation: AAT67238.1 .
    AC004895 Genomic DNA. No translation available.
    BC060846 mRNA. Translation: AAH60846.2 .
    BC132862 mRNA. Translation: AAI32863.1 .
    AK022759 mRNA. Translation: BAB14232.1 .
    CCDSi CCDS47535.1. [Q9H9J4-2 ]
    RefSeqi NP_115548.1. NM_032172.2. [Q9H9J4-2 ]
    XP_005249939.1. XM_005249882.2. [Q9H9J4-1 ]
    UniGenei Hs.31856.

    3D structure databases

    ProteinModelPortali Q9H9J4.
    SMRi Q9H9J4. Positions 111-409.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123904. 30 interactions.
    IntActi Q9H9J4. 27 interactions.
    MINTi MINT-7899498.
    STRINGi 9606.ENSP00000301962.

    Protein family/group databases

    MEROPSi C19.048.

    PTM databases

    PhosphoSitei Q9H9J4.

    Polymorphism databases

    DMDMi 322510098.

    Proteomic databases

    MaxQBi Q9H9J4.
    PaxDbi Q9H9J4.
    PRIDEi Q9H9J4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306177 ; ENSP00000301962 ; ENSG00000106346 . [Q9H9J4-2 ]
    GeneIDi 84132.
    KEGGi hsa:84132.
    UCSCi uc011jwo.1. human. [Q9H9J4-1 ]
    uc011jwp.2. human. [Q9H9J4-2 ]

    Organism-specific databases

    CTDi 84132.
    GeneCardsi GC07P006144.
    H-InvDB HIX0006462.
    HGNCi HGNC:20068. USP42.
    HPAi HPA006752.
    neXtProti NX_Q9H9J4.
    PharmGKBi PA134902515.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5533.
    HOGENOMi HOG000236355.
    HOVERGENi HBG080724.
    InParanoidi Q9H9J4.
    KOi K11855.
    OMAi GKLMPAP.
    OrthoDBi EOG72VH5K.
    PhylomeDBi Q9H9J4.
    TreeFami TF315281.

    Miscellaneous databases

    GeneWikii USP42.
    GenomeRNAii 84132.
    NextBioi 73425.
    PMAP-CutDB Q9H9J4.
    PROi Q9H9J4.

    Gene expression databases

    ArrayExpressi Q9H9J4.
    Bgeei Q9H9J4.
    CleanExi HS_USP42.
    Genevestigatori Q9H9J4.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    [Graphical view ]
    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 1), TISSUE SPECIFICITY, ENZYME ACTIVITY.
    2. "A discovery of a novel deubiquitinating enzyme human USP42."
      Baek K.-H., Yoo K.-J.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1202 (ISOFORM 1).
      Tissue: Placenta.
    5. "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 1-1198.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, 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. "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-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "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-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-856, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBP42_HUMAN
    AccessioniPrimary (citable) accession number: Q9H9J4
    Secondary accession number(s): A2RUE3
    , B5MDA5, Q0VIN8, Q3C166, Q6P9B4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 118 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 7
      Human chromosome 7: 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. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3