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Protein

Zyxin

Gene

Zyx

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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

GO - Biological processi

  • cell-matrix adhesion Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB
  • regulation of inflammatory response Source: Ensembl
  • stress fiber assembly Source: MGI
  • transforming growth factor beta receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Zyxin
Gene namesi
Name:Zyx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:103072. Zyx.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 564563ZyxinPRO_0000075914Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei117 – 1171PhosphoserineBy similarity
Modified residuei144 – 1441PhosphoserineCombined sources
Modified residuei170 – 1701PhosphoserineBy similarity
Modified residuei180 – 1801PhosphothreonineBy similarity
Modified residuei256 – 2561N6-acetyllysineCombined sources
Modified residuei263 – 2631N6-acetyllysineCombined sources
Modified residuei265 – 2651PhosphothreonineBy similarity
Modified residuei270 – 2701N6-acetyllysineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei300 – 3001PhosphoserineBy similarity
Modified residuei336 – 3361PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ62523.
MaxQBiQ62523.
PaxDbiQ62523.
PRIDEiQ62523.

PTM databases

iPTMnetiQ62523.
PhosphoSiteiQ62523.
SwissPalmiQ62523.

Expressioni

Gene expression databases

BgeeiQ62523.
CleanExiMM_ZYX.
ExpressionAtlasiQ62523. baseline and differential.
GenevisibleiQ62523. MM.

Interactioni

Subunit structurei

Interacts, via the Pro-rich regions, with the EVH1 domains of ENAH, EVL and VASP. Interacts with the first LIM domain of TES (By similarity).By similarity

Protein-protein interaction databases

BioGridi204712. 2 interactions.
STRINGi10090.ENSMUSP00000070427.

Structurei

3D structure databases

ProteinModelPortaliQ62523.
SMRiQ62523. Positions 376-534.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini376 – 43560LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini436 – 49560LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST
Domaini496 – 56267LIM zinc-binding 3PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi64 – 7714Pro-richAdd
BLAST
Compositional biasi94 – 10916Pro-richAdd
BLAST
Compositional biasi116 – 1216Pro-rich
Compositional biasi128 – 13811Pro-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

eggNOGiKOG1701. Eukaryota.
ENOG410Y3GP. LUCA.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000220910.
HOVERGENiHBG093602.
InParanoidiQ62523.
KOiK06273.
OMAiCLFHVEC.
OrthoDBiEOG7992Q6.
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.

Q62523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAPRPPPAI SVSVSAPAFY APQKKFAPVV APKPKVNPFR PGDSEPPVAA
60 70 80 90 100
GAQRAQMGRV GEIPPPPPED FPLPPPPLIG EGDDSEGALG GAFPPPPPPM
110 120 130 140 150
IEEPFPPAPL EEDIFPSPPP PLEEEGGPEA PTQLPPQPRE KVCSIDLEID
160 170 180 190 200
SLSSLLDDMT KNDPFKARVS SGYVPPPVAT PFVPKPSTKP APGGTAPLPP
210 220 230 240 250
WKTPSSSQPP PQPQAKPQVQ LHVQPQAKPH VQPQPVSSAN TQPRGPLSQA
260 270 280 290 300
PTPAPKFAPV APKFTPVVSK FSPGAPSGPG PQPNQKMVPP DAPSSVSTGS
310 320 330 340 350
PQPPSFTYAQ QKEKPLVQEK QHPQPPPAQN QNQVRSPGGP GPLTLKEVEE
360 370 380 390 400
LEQLTQQLMQ DMEHPQRQSV AVNESCGKCN QPLARAQPAV RALGQLFHIT
410 420 430 440 450
CFTCHQCQQQ LQGQQFYSLE GAPYCEGCYT DTLEKCNTCG QPITDRMLRA
460 470 480 490 500
TGKAYHPQCF TCVVCACPLE GTSFIVDQAN QPHCVPDYHK QYAPRCSVCS
510 520 530 540 550
EPIMPEPGRD ETVRVVALDK NFHMKCYKCE DCGKPLSIEA DDNGCFPLDG
560
HVLCRKCHSA RAQT
Length:564
Mass (Da):60,546
Last modified:July 27, 2011 - v2
Checksum:i98CF20E3E6B8BE9C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2151A → R in CAA67510 (PubMed:8940160).Curated
Sequence conflicti284 – 2929NQKMVPPDA → IKKWCLRMP in CAA67510 (PubMed:8940160).Curated
Sequence conflicti484 – 4841C → S in CAA67510 (PubMed:8940160).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07711 mRNA. Translation: CAA68984.1.
X99063 mRNA. Translation: CAA67510.1.
AK147812 mRNA. Translation: BAE28154.1.
CH466533 Genomic DNA. Translation: EDL13482.1.
CCDSiCCDS20066.1.
RefSeqiNP_001276546.1. NM_001289617.1.
NP_001276547.1. NM_001289618.1.
NP_001276548.1. NM_001289619.1.
NP_035907.1. NM_011777.3.
XP_006505999.1. XM_006505936.2.
UniGeneiMm.282303.

Genome annotation databases

EnsembliENSMUST00000164375; ENSMUSP00000126622; ENSMUSG00000029860.
ENSMUST00000203652; ENSMUSP00000145451; ENSMUSG00000029860.
GeneIDi22793.
KEGGimmu:22793.
UCSCiuc009bqz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07711 mRNA. Translation: CAA68984.1.
X99063 mRNA. Translation: CAA67510.1.
AK147812 mRNA. Translation: BAE28154.1.
CH466533 Genomic DNA. Translation: EDL13482.1.
CCDSiCCDS20066.1.
RefSeqiNP_001276546.1. NM_001289617.1.
NP_001276547.1. NM_001289618.1.
NP_001276548.1. NM_001289619.1.
NP_035907.1. NM_011777.3.
XP_006505999.1. XM_006505936.2.
UniGeneiMm.282303.

3D structure databases

ProteinModelPortaliQ62523.
SMRiQ62523. Positions 376-534.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204712. 2 interactions.
STRINGi10090.ENSMUSP00000070427.

PTM databases

iPTMnetiQ62523.
PhosphoSiteiQ62523.
SwissPalmiQ62523.

Proteomic databases

EPDiQ62523.
MaxQBiQ62523.
PaxDbiQ62523.
PRIDEiQ62523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000164375; ENSMUSP00000126622; ENSMUSG00000029860.
ENSMUST00000203652; ENSMUSP00000145451; ENSMUSG00000029860.
GeneIDi22793.
KEGGimmu:22793.
UCSCiuc009bqz.2. mouse.

Organism-specific databases

CTDi7791.
MGIiMGI:103072. Zyx.

Phylogenomic databases

eggNOGiKOG1701. Eukaryota.
ENOG410Y3GP. LUCA.
GeneTreeiENSGT00760000119039.
HOGENOMiHOG000220910.
HOVERGENiHBG093602.
InParanoidiQ62523.
KOiK06273.
OMAiCLFHVEC.
OrthoDBiEOG7992Q6.
TreeFamiTF320310.

Miscellaneous databases

PROiQ62523.
SOURCEiSearch...

Gene expression databases

BgeeiQ62523.
CleanExiMM_ZYX.
ExpressionAtlasiQ62523. baseline and differential.
GenevisibleiQ62523. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR X Swiss Webster.
  2. Otte J., Heischmann A., Breier G., Beckerle M.C., von der Ahe D.
    Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 AND SER-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Spleen and Testis.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-256 AND LYS-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiZYX_MOUSE
AccessioniPrimary (citable) accession number: Q62523
Secondary accession number(s): P70461, Q3UGQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.