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P39447

- ZO1_MOUSE

UniProt

P39447 - ZO1_MOUSE

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Protein
Tight junction protein ZO-1
Gene
Tjp1, Zo1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells By similarity.

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein domain specific binding Source: MGI
Complete GO annotation...

GO - Biological processi

  1. blastocyst formation Source: MGI
  2. cellular response to glucose stimulus Source: Ensembl
  3. negative regulation of vascular permeability Source: Ensembl
  4. response to drug Source: Ensembl
  5. response to ethanol Source: Ensembl
  6. response to lipopolysaccharide Source: Ensembl
  7. response to magnetism Source: Ensembl
  8. sensory perception of sound Source: MGI
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_196537. Signaling by Hippo.
REACT_224600. c-src mediated regulation of Cx43 function and closure of gap junctions.

Names & Taxonomyi

Protein namesi
Recommended name:
Tight junction protein ZO-1
Alternative name(s):
Tight junction protein 1
Zona occludens protein 1
Zonula occludens protein 1
Gene namesi
Name:Tjp1
Synonyms:Zo1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:98759. Tjp1.

Subcellular locationi

Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junctiontight junction By similarity. Cell junctiongap junction. CytoplasmmyofibrilsarcomereI band
Note: Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact. Detected at the leading edge of migrating and wounded cells By similarity.1 Publication

GO - Cellular componenti

  1. I band Source: UniProtKB-SubCell
  2. adherens junction Source: MGI
  3. apical junction complex Source: MGI
  4. apical part of cell Source: MGI
  5. apical plasma membrane Source: MGI
  6. apicolateral plasma membrane Source: MGI
  7. basolateral plasma membrane Source: MGI
  8. cell junction Source: MGI
  9. cell surface Source: MGI
  10. cell-cell adherens junction Source: MGI
  11. cell-cell junction Source: MGI
  12. cytoplasm Source: MGI
  13. gap junction Source: UniProtKB-SubCell
  14. intercalated disc Source: MGI
  15. intercellular canaliculus Source: MGI
  16. membrane Source: MGI
  17. nucleus Source: MGI
  18. plasma membrane Source: MGI
  19. tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Gap junction, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17451745Tight junction protein ZO-1
PRO_0000094541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251Phosphoserine By similarity
Modified residuei175 – 1751Phosphoserine By similarity
Modified residuei178 – 1781Phosphoserine By similarity
Modified residuei179 – 1791Phosphoserine By similarity
Modified residuei185 – 1851Phosphothreonine By similarity
Modified residuei277 – 2771Phosphoserine By similarity
Modified residuei297 – 2971Phosphoserine By similarity
Modified residuei300 – 3001Phosphoserine By similarity
Modified residuei329 – 3291Phosphoserine By similarity
Modified residuei334 – 3341Phosphoserine By similarity
Modified residuei337 – 3371Phosphoserine By similarity
Modified residuei353 – 3531Phosphoserine By similarity
Modified residuei617 – 6171Phosphoserine By similarity
Modified residuei622 – 6221Phosphoserine By similarity
Modified residuei912 – 9121Phosphoserine2 Publications
Modified residuei1139 – 11391Phosphotyrosine1 Publication
Modified residuei1164 – 11641Phosphotyrosine1 Publication
Modified residuei1353 – 13531Phosphotyrosine1 Publication
Modified residuei1365 – 13651Phosphoserine By similarity
Modified residuei1542 – 15421Phosphoserine By similarity
Modified residuei1614 – 16141Phosphoserine By similarity

Post-translational modificationi

Phosphorylated. Dephosphorylated by PTPRJ By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39447.
PaxDbiP39447.
PRIDEiP39447.

PTM databases

PhosphoSiteiP39447.

Expressioni

Gene expression databases

ArrayExpressiP39447.
BgeeiP39447.
CleanExiMM_TJP1.
GenevestigatoriP39447.

Interactioni

Subunit structurei

Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3. Interacts with CGN/cingulin, CALM, CXADR, GJD3, HSPA4 and UBN1. Interacts (via ZU5 domain) with CDC42BPB. Interacts (via PDZ domain) with GJA1 By similarity. Interacts with OCLN, claudins, GJA12 and KIRREL1. Interacts with BVES (via the C-terminus cytoplasmic tail). Interacts (via ZU5 domain) with MYZAP. Interacts (via PDZ domains) with ANKRD2 By similarity.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Actn4P577806EBI-79508,EBI-445071
Gjb6P706893EBI-79508,EBI-2615416

Protein-protein interaction databases

BioGridi204209. 7 interactions.
DIPiDIP-30946N.
IntActiP39447. 15 interactions.
MINTiMINT-113090.
STRINGi10090.ENSMUSP00000032729.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 267
Beta strandi36 – 394
Beta strandi44 – 463
Turni49 – 513
Beta strandi55 – 595
Beta strandi61 – 633
Turni64 – 685
Beta strandi73 – 786
Beta strandi84 – 863
Helixi88 – 969
Beta strandi102 – 1087

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RRMNMR-A18-110[»]
ProteinModelPortaliP39447.
SMRiP39447. Positions 18-110, 185-264, 420-802, 1626-1745.

Miscellaneous databases

EvolutionaryTraceiP39447.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 11088PDZ 1
Add
BLAST
Domaini186 – 26479PDZ 2
Add
BLAST
Domaini421 – 50282PDZ 3
Add
BLAST
Domaini516 – 58469SH3
Add
BLAST
Domaini610 – 791182Guanylate kinase-like
Add
BLAST
Domaini1629 – 172193ZU5
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1242 – 12476Poly-Pro
Compositional biasi1424 – 14307Poly-Pro

Domaini

The second PDZ domain mediates interaction with GJA12.1 Publication

Sequence similaritiesi

Belongs to the MAGUK family.
Contains 3 PDZ (DHR) domains.
Contains 1 SH3 domain.
Contains 1 ZU5 domain.

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG239704.
GeneTreeiENSGT00640000091263.
HOGENOMiHOG000230923.
HOVERGENiHBG007849.
KOiK05701.
OMAiQANSIER.
OrthoDBiEOG7T1RB4.
TreeFamiTF315957.

Family and domain databases

Gene3Di2.30.42.10. 3 hits.
3.40.50.300. 1 hit.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZonOcculdens.
IPR005418. ZonOcculS1.
IPR000906. ZU5.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSiPR01597. ZONOCCLUDNS.
PR01598. ZONOCCLUDNS1.
SMARTiSM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39447-1 [UniParc]FASTAAdd to Basket

« Hide

MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG     50
ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK 100
NAKITIRRKK KVQIPVSHPD PEPVSDNEDD SYDEEVHDPR AGRGALANRR 150
SEKSWARDRS ASRERSLSPR SDRRSVASSQ PAKPTKVTLV KSRKNEEYGL 200
RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM SLTDAKTLIE 250
RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 300
GRSHDRPPRR SQSRSPDQRS EPSDHSTQSP QQPSNGSLRS REEERMSKPG 350
AISTPVKHVD DHPPKAVEEV TVEKNEKQTP TLPEPKPVYA QVGQPDVDLP 400
VSPSDGALPN SAHEDGILRP SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV 450
LEDSPAAKEG LEEGDQILRV NNVDFTNIIR EEAVLFLLDL PKGEEVTILA 500
QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG EVFRVVDTLY 550
NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 600
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF 650
GPIADVAREK LAREEPDIYQ IAKSEPRDAG TDHRSSGIIR LHTIKQIIDQ 700
DKHALLDVTP NAVDRLNYAQ WYPIVVFLNP DSKQGVKTMR MRLCPESRKS 750
ARKLYERSHK LRKNNHHLFT TTINLNSMND GWYGALKEAI QQQQNQLVWV 800
SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT SDYEDTDTEG 850
GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 900
QAQPQAIHRI DSPGLKPASQ QKAEASSPVP YLSPETTPAS SASAVNHNVS 950
VTNVSLEEPA PAPPTSHASQ PGCLGAPSAE AAHVVLRGEG PPLPPHADPA 1000
KVYRKEPYSE EMMRQNHILK QPALGHPGQR PDKEPNLAYE PQLPYIEKQA 1050
SRDLEQPSYR YEVSSYTDQF SRNYDHRLRF EDRIPTYEDQ WSYYDDKQPY 1100
QPRPFENQHP RDLDSRQHPE EASERGYFQR FEEPAPLSYD SRTRYEQLPR 1150
TSTLRHEEQP APAYEVHNRY RPEAQPYSST GPKSSEPKQY FDQYPRSYEQ 1200
VPPPGFTSKT GHYEPLHGAA VVPPLIPSSQ QKPEVLPSAT KPQPPPPTLT 1250
EEEEDPAMKP QSVLTRVKMF ENKRSASLEN KKDVNDTASF KPPEVASKPP 1300
GASLAGPKPV PQSQFSEHDK TLYRLPEPQK PQVKPPEDIV RSNHYDPEED 1350
EEYYRKQLSY FDRRSFESKP SAHLPAGHHS EPAKPVHSQS QPNFSSYSSK 1400
GKPETDAVDR SFSEKRYDPA QATPPPPPLP SQYSQPAPPL SSSSLHIHSK 1450
GAQGEGNSVS LDFQNSYMSK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS 1500
FPDKAPVNGA EQTQKTITPV YNRFTPKPYT SSARPFERKF ESPKFNHNLL 1550
PSETVHKPEL SSKTPTSPKT LMKAHSSTQP PEFDSGVETF SVHTDKPKYQ 1600
MNNISTMPKA VPVSPSAVEE DEDEDGHTVV ATARGIFNSN GGVLSSIETG 1650
VSIIIPQGAI PEGIEQEIYF KVCRDNSILP PLDKEKGETL LSPLVMCGPH 1700
GLKFLKPVEL RLPHCDPKTW QNKCLPGDPN YLVGANCVSV LIDHF 1745
Length:1,745
Mass (Da):194,742
Last modified:July 27, 2011 - v2
Checksum:i002B96F5A998B5CD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021L → P in BAA03274. 1 Publication
Sequence conflicti222 – 2221N → D in BAA03274. 1 Publication
Sequence conflicti676 – 6761P → L in BAA03274. 1 Publication
Sequence conflicti985 – 9851V → G in BAA03274. 1 Publication
Sequence conflicti1237 – 12371P → R in BAA03274. 1 Publication
Sequence conflicti1395 – 13951S → P in BAA03274. 1 Publication
Sequence conflicti1584 – 15841D → G in BAA03274. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14340 mRNA. Translation: BAA03274.1.
AC122222 Genomic DNA. No translation available.
AC131741 Genomic DNA. No translation available.
CCDSiCCDS21338.1.
PIRiA46431.
RefSeqiNP_033412.2. NM_009386.2.
UniGeneiMm.4342.

Genome annotation databases

EnsembliENSMUST00000102592; ENSMUSP00000099652; ENSMUSG00000030516.
GeneIDi21872.
KEGGimmu:21872.
UCSCiuc009hgp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14340 mRNA. Translation: BAA03274.1 .
AC122222 Genomic DNA. No translation available.
AC131741 Genomic DNA. No translation available.
CCDSi CCDS21338.1.
PIRi A46431.
RefSeqi NP_033412.2. NM_009386.2.
UniGenei Mm.4342.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2RRM NMR - A 18-110 [» ]
ProteinModelPortali P39447.
SMRi P39447. Positions 18-110, 185-264, 420-802, 1626-1745.
ModBasei Search...

Protein-protein interaction databases

BioGridi 204209. 7 interactions.
DIPi DIP-30946N.
IntActi P39447. 15 interactions.
MINTi MINT-113090.
STRINGi 10090.ENSMUSP00000032729.

PTM databases

PhosphoSitei P39447.

Proteomic databases

MaxQBi P39447.
PaxDbi P39447.
PRIDEi P39447.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102592 ; ENSMUSP00000099652 ; ENSMUSG00000030516 .
GeneIDi 21872.
KEGGi mmu:21872.
UCSCi uc009hgp.2. mouse.

Organism-specific databases

CTDi 7082.
MGIi MGI:98759. Tjp1.

Phylogenomic databases

eggNOGi NOG239704.
GeneTreei ENSGT00640000091263.
HOGENOMi HOG000230923.
HOVERGENi HBG007849.
KOi K05701.
OMAi QANSIER.
OrthoDBi EOG7T1RB4.
TreeFami TF315957.

Enzyme and pathway databases

Reactomei REACT_196537. Signaling by Hippo.
REACT_224600. c-src mediated regulation of Cx43 function and closure of gap junctions.

Miscellaneous databases

EvolutionaryTracei P39447.
NextBioi 301376.
PROi P39447.
SOURCEi Search...

Gene expression databases

ArrayExpressi P39447.
Bgeei P39447.
CleanExi MM_TJP1.
Genevestigatori P39447.

Family and domain databases

Gene3Di 2.30.42.10. 3 hits.
3.40.50.300. 1 hit.
InterProi IPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR005417. ZonOcculdens.
IPR005418. ZonOcculS1.
IPR000906. ZU5.
[Graphical view ]
Pfami PF00625. Guanylate_kin. 1 hit.
PF00595. PDZ. 3 hits.
PF07653. SH3_2. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view ]
PRINTSi PR01597. ZONOCCLUDNS.
PR01598. ZONOCCLUDNS1.
SMARTi SM00072. GuKc. 1 hit.
SM00228. PDZ. 3 hits.
SM00326. SH3. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF50156. SSF50156. 3 hits.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50052. GUANYLATE_KINASE_2. 1 hit.
PS50106. PDZ. 3 hits.
PS50002. SH3. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy."
    Itoh M., Nagafuchi A., Yonemura S., Yasuda-Kitani T., Tsukita S., Tsukita S.
    J. Cell Biol. 121:491-502(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "NEPH1 defines a novel family of podocin interacting proteins."
    Sellin L., Huber T.B., Gerke P., Quack I., Pavenstaedt H., Walz G.
    FASEB J. 17:115-117(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIRREL1.
    Strain: Swiss Webster.
    Tissue: Brain.
  4. "Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain."
    Li X., Ionescu A.V., Lynn B.D., Lu S., Kamasawa N., Morita M., Davidson K.G.V., Yasumura T., Rash J.E., Nagy J.I.
    Neuroscience 126:611-630(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GJA12, DOMAIN.
  5. "Bves modulates epithelial integrity through an interaction at the tight junction."
    Osler M.E., Chang M.S., Bader D.M.
    J. Cell Sci. 118:4667-4678(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BVES.
  6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1139 AND TYR-1353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. "Myozap, a novel intercalated disc protein, activates serum response factor-dependent signaling and is required to maintain cardiac function in vivo."
    Seeger T.S., Frank D., Rohr C., Will R., Just S., Grund C., Lyon R., Luedde M., Koegl M., Sheikh F., Rottbauer W., Franke W.W., Katus H.A., Olson E.N., Frey N.
    Circ. Res. 106:880-890(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYZAP, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  13. "(1)H, (13)C, and (15)N resonance assignment of the first PDZ domain of mouse ZO-1."
    Umetsu Y., Goda N., Taniguchi R., Satomura K., Ikegami T., Furuse M., Hiroaki H.
    Biomol. NMR. Assign. 5:207-210(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 18-110.

Entry informationi

Entry nameiZO1_MOUSE
AccessioniPrimary (citable) accession number: P39447
Secondary accession number(s): E9QK00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 145 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

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi