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Q15942

- ZYX_HUMAN

UniProt

Q15942 - ZYX_HUMAN

Protein

Zyxin

Gene

ZYX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Adhesion plaque protein. Binds alpha-actinin and the CRP protein. Important for targeting TES and ENA/VASP family members to focal adhesions and for the formation of actin-rich structures. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression By similarity.By similarity

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: ProtInc
    2. cell-cell signaling Source: ProtInc
    3. regulation of inflammatory response Source: Ensembl
    4. signal transduction Source: ProtInc
    5. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion, Host-virus interaction

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Zyxin
    Alternative name(s):
    Zyxin-2
    Gene namesi
    Name:ZYX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:13200. ZYX.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton. Nucleus. Cell junctionfocal adhesion
    Note: Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of HESX1.

    GO - Cellular componenti

    1. cell-cell adherens junction Source: MGI
    2. cytoplasm Source: HPA
    3. focal adhesion Source: UniProtKB
    4. integral component of plasma membrane Source: ProtInc
    5. nucleus Source: UniProtKB-SubCell
    6. plasma membrane Source: ProtInc
    7. stress fiber Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi71 – 711F → A: Reduced interaction with ENAH and VASP. 1 Publication
    Mutagenesisi93 – 931F → A: Reduced interaction with ENAH and VASP. 1 Publication
    Mutagenesisi104 – 1041F → A: Greatly reduced interaction with ENAH and VASP; when associated with A-71 or with A-71 and A-93. 1 Publication
    Mutagenesisi114 – 1141F → A: No targeting to focal adhesions and reduced actin-rich structures; when associated with A-71; A-93 and A-104. 1 Publication

    Organism-specific databases

    PharmGKBiPA37765.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 572571ZyxinPRO_0000075913Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei143 – 1431PhosphoserineBy similarity
    Modified residuei169 – 1691Phosphoserine2 Publications
    Modified residuei179 – 1791Phosphothreonine1 Publication
    Modified residuei259 – 2591Phosphoserine3 Publications
    Modified residuei265 – 2651N6-acetyllysineBy similarity
    Modified residuei267 – 2671Phosphoserine3 Publications
    Modified residuei270 – 2701Phosphothreonine2 Publications
    Modified residuei272 – 2721N6-acetyllysineBy similarity
    Modified residuei274 – 2741Phosphothreonine2 Publications
    Modified residuei279 – 2791N6-acetyllysine1 Publication
    Modified residuei281 – 2811Phosphoserine5 Publications
    Modified residuei288 – 2881Phosphoserine1 Publication
    Modified residuei308 – 3081Phosphoserine2 Publications
    Modified residuei344 – 3441Phosphoserine5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15942.
    PaxDbiQ15942.
    PRIDEiQ15942.

    2D gel databases

    OGPiQ15942.

    PTM databases

    PhosphoSiteiQ15942.

    Miscellaneous databases

    PMAP-CutDBQ15942.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15942.
    BgeeiQ15942.
    CleanExiHS_ZYX.
    GenevestigatoriQ15942.

    Organism-specific databases

    HPAiCAB009321.
    HPA004835.

    Interactioni

    Subunit structurei

    Interacts with HPV type 6 protein E6. Does not interact significantly with E6 proteins from HPV types 11, 16, or 18. Interacts, via the Pro-rich regions, with the EVH1 domains of ENAH, EVL and VASP. Interacts with the first LIM domain of TES. Interacts with NEBL (isoform 2).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LASP1Q148475EBI-444225,EBI-742828
    LATS1O9583510EBI-444225,EBI-444209
    OPRM1P353722EBI-444225,EBI-2624570

    Protein-protein interaction databases

    BioGridi113569. 63 interactions.
    IntActiQ15942. 40 interactions.
    MINTiMINT-220515.
    STRINGi9606.ENSP00000324422.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15942.
    SMRiQ15942. Positions 383-564.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini384 – 44360LIM zinc-binding 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini444 – 50360LIM zinc-binding 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini504 – 57067LIM zinc-binding 3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi64 – 7714Pro-richAdd
    BLAST
    Compositional biasi94 – 10815Pro-richAdd
    BLAST
    Compositional biasi115 – 1217Pro-rich
    Compositional biasi127 – 13711Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the zyxin/ajuba family.Curated
    Contains 3 LIM zinc-binding domains.PROSITE-ProRule annotation

    Keywords - Domaini

    LIM domain, Repeat

    Phylogenomic databases

    eggNOGiNOG279196.
    HOGENOMiHOG000220910.
    HOVERGENiHBG093602.
    InParanoidiQ15942.
    KOiK06273.
    OMAiAPQKKFG.
    OrthoDBiEOG7992Q6.
    PhylomeDBiQ15942.
    TreeFamiTF320310.

    Family and domain databases

    Gene3Di2.10.110.10. 3 hits.
    InterProiIPR001781. Znf_LIM.
    [Graphical view]
    PfamiPF00412. LIM. 3 hits.
    [Graphical view]
    SMARTiSM00132. LIM. 3 hits.
    [Graphical view]
    PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q15942-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAPRPSPAI SVSVSAPAFY APQKKFGPVV APKPKVNPFR PGDSEPPPAP    50
    GAQRAQMGRV GEIPPPPPED FPLPPPPLAG DGDDAEGALG GAFPPPPPPI 100
    EESFPPAPLE EEIFPSPPPP PEEEGGPEAP IPPPPQPREK VSSIDLEIDS 150
    LSSLLDDMTK NDPFKARVSS GYVPPPVATP FSSKSSTKPA AGGTAPLPPW 200
    KSPSSSQPLP QVPAPAQSQT QFHVQPQPQP KPQVQLHVQS QTQPVSLANT 250
    QPRGPPASSP APAPKFSPVT PKFTPVASKF SPGAPGGSGS QPNQKLGHPE 300
    ALSAGTGSPQ PPSFTYAQQR EKPRVQEKQH PVPPPAQNQN QVRSPGAPGP 350
    LTLKEVEELE QLTQQLMQDM EHPQRQNVAV NELCGRCHQP LARAQPAVRA 400
    LGQLFHIACF TCHQCAQQLQ GQQFYSLEGA PYCEGCYTDT LEKCNTCGEP 450
    ITDRMLRATG KAYHPHCFTC VVCARPLEGT SFIVDQANRP HCVPDYHKQY 500
    APRCSVCSEP IMPEPGRDET VRVVALDKNF HMKCYKCEDC GKPLSIEADD 550
    NGCFPLDGHV LCRKCHTARA QT 572
    Length:572
    Mass (Da):61,277
    Last modified:November 1, 1997 - v1
    Checksum:i2833B1EFA260B762
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti223 – 2231H → L.
    Corresponds to variant rs11978404 [ dbSNP | Ensembl ].
    VAR_034081

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94991 mRNA. Translation: CAA64447.1.
    X95735 mRNA. Translation: CAA65050.1.
    CR457431 mRNA. Translation: CAG33712.1.
    AC092214 Genomic DNA. Translation: AAS07459.1.
    CH236959 Genomic DNA. Translation: EAL23788.1.
    BC008743 mRNA. Translation: AAH08743.1.
    BC009360 mRNA. Translation: AAH09360.1.
    BC010031 mRNA. Translation: AAH10031.1.
    CCDSiCCDS5883.1.
    PIRiG02845.
    RefSeqiNP_001010972.1. NM_001010972.1.
    NP_003452.1. NM_003461.4.
    UniGeneiHs.490415.

    Genome annotation databases

    EnsembliENST00000322764; ENSP00000324422; ENSG00000159840.
    GeneIDi7791.
    KEGGihsa:7791.
    UCSCiuc003wcw.3. human.

    Polymorphism databases

    DMDMi2497677.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94991 mRNA. Translation: CAA64447.1 .
    X95735 mRNA. Translation: CAA65050.1 .
    CR457431 mRNA. Translation: CAG33712.1 .
    AC092214 Genomic DNA. Translation: AAS07459.1 .
    CH236959 Genomic DNA. Translation: EAL23788.1 .
    BC008743 mRNA. Translation: AAH08743.1 .
    BC009360 mRNA. Translation: AAH09360.1 .
    BC010031 mRNA. Translation: AAH10031.1 .
    CCDSi CCDS5883.1.
    PIRi G02845.
    RefSeqi NP_001010972.1. NM_001010972.1.
    NP_003452.1. NM_003461.4.
    UniGenei Hs.490415.

    3D structure databases

    ProteinModelPortali Q15942.
    SMRi Q15942. Positions 383-564.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113569. 63 interactions.
    IntActi Q15942. 40 interactions.
    MINTi MINT-220515.
    STRINGi 9606.ENSP00000324422.

    PTM databases

    PhosphoSitei Q15942.

    Polymorphism databases

    DMDMi 2497677.

    2D gel databases

    OGPi Q15942.

    Proteomic databases

    MaxQBi Q15942.
    PaxDbi Q15942.
    PRIDEi Q15942.

    Protocols and materials databases

    DNASUi 7791.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322764 ; ENSP00000324422 ; ENSG00000159840 .
    GeneIDi 7791.
    KEGGi hsa:7791.
    UCSCi uc003wcw.3. human.

    Organism-specific databases

    CTDi 7791.
    GeneCardsi GC07P143078.
    HGNCi HGNC:13200. ZYX.
    HPAi CAB009321.
    HPA004835.
    MIMi 602002. gene.
    neXtProti NX_Q15942.
    PharmGKBi PA37765.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG279196.
    HOGENOMi HOG000220910.
    HOVERGENi HBG093602.
    InParanoidi Q15942.
    KOi K06273.
    OMAi APQKKFG.
    OrthoDBi EOG7992Q6.
    PhylomeDBi Q15942.
    TreeFami TF320310.

    Miscellaneous databases

    ChiTaRSi ZYX. human.
    GeneWikii Zyxin.
    GenomeRNAii 7791.
    NextBioi 30155.
    PMAP-CutDB Q15942.
    PROi Q15942.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15942.
    Bgeei Q15942.
    CleanExi HS_ZYX.
    Genevestigatori Q15942.

    Family and domain databases

    Gene3Di 2.10.110.10. 3 hits.
    InterProi IPR001781. Znf_LIM.
    [Graphical view ]
    Pfami PF00412. LIM. 3 hits.
    [Graphical view ]
    SMARTi SM00132. LIM. 3 hits.
    [Graphical view ]
    PROSITEi PS00478. LIM_DOMAIN_1. 2 hits.
    PS50023. LIM_DOMAIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Umbilical vein.
    2. "A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts."
      Zumbrunn J., Trueb B.
      Eur. J. Biochem. 241:657-663(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "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].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Kidney, Skin and Uterus.
    7. Bienvenut W.V., Calvo F.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-25; 36-54; 168-184; 280-320 AND 325-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    8. "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins."
      Drees B., Friederich E., Fradelizi J., Louvard D., Beckerle M.C., Golsteyn R.M.
      J. Biol. Chem. 275:22503-22511(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ENAH AND VASP, MUTAGENESIS OF PHE-71; PHE-93; PHE-104 AND PHE-114.
    9. "Interaction of zyxin, a focal adhesion protein, with the E6 protein from human papillomavirus type 6 results in its nuclear translocation."
      Degenhardt Y.Y., Silverstein S.
      J. Virol. 75:11791-11802(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HPV6 E6.
    10. "The conformational state of Tes regulates its zyxin-dependent recruitment to focal adhesions."
      Garvalov B.K., Higgins T.E., Sutherland J.D., Zettl M., Scaplehorn N., Koecher T., Piddini E., Griffiths G., Way M.
      J. Cell Biol. 161:33-39(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TES.
    11. "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-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding."
      Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J., McDonald N.Q., Way M.
      Mol. Cell 28:1071-1082(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EVL; VASP AND ENAH.
    15. "The LIM-domain protein zyxin binds the homeodomain factor Xanf1/Hesx1 and modulates its activity in the anterior neural plate of Xenopus laevis embryo."
      Martynova N.Y., Eroshkin F.M., Ermolina L.V., Ermakova G.V., Korotaeva A.L., Smurova K.M., Gyoeva F.K., Zaraisky A.G.
      Dev. Dyn. 237:736-749(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; SER-281 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-259; SER-267; THR-270; THR-274; SER-281; SER-288; SER-308 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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-169; THR-179; SER-259; THR-274; SER-281; SER-308 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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-267; THR-270; SER-281 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiZYX_HUMAN
    AccessioniPrimary (citable) accession number: Q15942
    Secondary accession number(s): A4D2G6, Q6I9S4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 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, Direct protein sequencing, 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3