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Q15942

- ZYX_HUMAN

UniProt

Q15942 - ZYX_HUMAN

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Protein

Zyxin

Gene

ZYX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell adhesion Source: ProtInc
  2. cell-cell signaling Source: ProtInc
  3. cell-matrix adhesion Source: UniProtKB
  4. integrin-mediated signaling pathway Source: UniProtKB
  5. regulation of inflammatory response Source: Ensembl
  6. signal transduction Source: ProtInc
  7. stress fiber assembly Source: UniProtKB
  8. transforming growth factor beta receptor signaling pathway Source: UniProtKB
  9. viral process Source: UniProtKB-KW
Complete GO annotation...

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
  6. plasma membrane Source: ProtInc
  7. stress fiber Source: UniProtKB
Complete GO annotation...

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

BgeeiQ15942.
CleanExiHS_ZYX.
ExpressionAtlasiQ15942. baseline and differential.
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. 65 interactions.
IntActiQ15942. 41 interactions.
MINTiMINT-220515.
STRINGi9606.ENSP00000324422.

Structurei

3D structure databases

ProteinModelPortaliQ15942.
SMRiQ15942. Positions 383-545.
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.
GeneTreeiENSGT00760000119039.
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

        10         20         30         40         50
MAAPRPSPAI SVSVSAPAFY APQKKFGPVV APKPKVNPFR PGDSEPPPAP
60 70 80 90 100
GAQRAQMGRV GEIPPPPPED FPLPPPPLAG DGDDAEGALG GAFPPPPPPI
110 120 130 140 150
EESFPPAPLE EEIFPSPPPP PEEEGGPEAP IPPPPQPREK VSSIDLEIDS
160 170 180 190 200
LSSLLDDMTK NDPFKARVSS GYVPPPVATP FSSKSSTKPA AGGTAPLPPW
210 220 230 240 250
KSPSSSQPLP QVPAPAQSQT QFHVQPQPQP KPQVQLHVQS QTQPVSLANT
260 270 280 290 300
QPRGPPASSP APAPKFSPVT PKFTPVASKF SPGAPGGSGS QPNQKLGHPE
310 320 330 340 350
ALSAGTGSPQ PPSFTYAQQR EKPRVQEKQH PVPPPAQNQN QVRSPGAPGP
360 370 380 390 400
LTLKEVEELE QLTQQLMQDM EHPQRQNVAV NELCGRCHQP LARAQPAVRA
410 420 430 440 450
LGQLFHIACF TCHQCAQQLQ GQQFYSLEGA PYCEGCYTDT LEKCNTCGEP
460 470 480 490 500
ITDRMLRATG KAYHPHCFTC VVCARPLEGT SFIVDQANRP HCVPDYHKQY
510 520 530 540 550
APRCSVCSEP IMPEPGRDET VRVVALDKNF HMKCYKCEDC GKPLSIEADD
560 570
NGCFPLDGHV LCRKCHTARA QT
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 383-545.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113569. 65 interactions.
IntActi Q15942. 41 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.
GeneTreei ENSGT00760000119039.
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

Bgeei Q15942.
CleanExi HS_ZYX.
ExpressionAtlasi Q15942. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 143 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