UniProtKB - Q07157 (ZO1_HUMAN)

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History
Entry version 205 (18 Jul 2018)
Sequence version 3 (24 Jan 2006)
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Protein

Tight junction protein ZO-1

Gene

TJP1

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates to the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity).By similarity2 Publications

GO - Molecular functionⁱ

cadherin binding
Source: BHF-UCL
Inferred from high throughput direct assayⁱ
- 25468996
calmodulin binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell-cell junction assembly
Source: ProtInc
Traceable author statementⁱ
- 8486731
cell-cell signaling involved in cell-cell junction organization
Source: UniProtKB
Non-traceable author statementⁱ
- 8395056
establishment of endothelial intestinal barrier
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23885123
hippo signaling Source: Reactome
regulation of bicellular tight junction assembly Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Calmodulin-binding

Molecular function

Calmodulin-binding

Enzyme and pathway databases

Reactomeⁱ	R-HSA-191647 c-src mediated regulation of Cx43 function and closure of gap junctions R-HSA-2028269 Signaling by Hippo R-HSA-351906 Apoptotic cleavage of cell adhesion proteins R-HSA-8935964 RUNX1 regulates expression of components of tight junctions
SIGNORⁱ	Q07157

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 15

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000104067.16
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11827 TJP1
MIMⁱ	601009 gene
neXtProtⁱ	NX_Q07157

Keywords - Cellular componentⁱ

Cell junction, Cell membrane, Cell projection, Gap junction, Membrane, Tight junction

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	201	R → A: Strongly reduced interaction with GJA1. 1 Publication	1
Mutagenesisⁱ	209	K → A: Abolishes interaction with GJA1. 1 Publication	1
Mutagenesisⁱ	1699 – 1700	MC → AA: Abolishes interaction with CDC42BPB. 1 Publication	2
Mutagenesisⁱ	1748	Missing : Abolishes interaction with CDC42BPB and MYZAP. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	7082
Open Targets More...OpenTargetsⁱ	ENSG00000104067
PharmGKBⁱ	PA36532

Polymorphism and mutation databases

BioMutaⁱ	TJP1
DMDMⁱ	85700443

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000094540	1 – 1748	Tight junction protein ZO-1Add BLAST		1748

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	125	PhosphoserineCombined sources	1
Modified residueⁱ	132	PhosphotyrosineBy similarity	1
Modified residueⁱ	175	PhosphoserineCombined sources	1
Modified residueⁱ	178	PhosphoserineCombined sources	1
Modified residueⁱ	179	PhosphoserineCombined sources	1
Modified residueⁱ	185	PhosphothreonineCombined sources	1
Modified residueⁱ	212	PhosphoserineCombined sources	1
Modified residueⁱ	241	PhosphoserineBy similarity	1
Modified residueⁱ	267	PhosphothreonineCombined sources	1
Modified residueⁱ	275	PhosphoserineCombined sources	1
Modified residueⁱ	277	PhosphoserineCombined sources	1
Modified residueⁱ	280	PhosphoserineCombined sources	1
Modified residueⁱ	284	PhosphoserineCombined sources	1
Modified residueⁱ	290	PhosphoserineCombined sources	1
Modified residueⁱ	294	PhosphoserineCombined sources	1
Modified residueⁱ	297	PhosphoserineCombined sources	1
Modified residueⁱ	300	PhosphoserineCombined sources	1
Modified residueⁱ	323	PhosphoserineBy similarity	1
Modified residueⁱ	329	PhosphoserineCombined sources	1
Modified residueⁱ	334	PhosphoserineCombined sources	1
Modified residueⁱ	337	PhosphoserineCombined sources	1
Modified residueⁱ	353	PhosphoserineCombined sources	1
Modified residueⁱ	354	PhosphothreonineCombined sources	1
Modified residueⁱ	617	PhosphoserineCombined sources	1
Modified residueⁱ	622	PhosphoserineCombined sources	1
Modified residueⁱ	809	PhosphothreonineCombined sources	1
Modified residueⁱ	810	PhosphoserineBy similarity	1
Modified residueⁱ	821	PhosphoserineCombined sources	1
Modified residueⁱ	822	PhosphotyrosineBy similarity	1
Modified residueⁱ	824	PhosphoserineBy similarity	1
Modified residueⁱ	828	PhosphoserineBy similarity	1
Modified residueⁱ	837	PhosphoserineCombined sources	1
Modified residueⁱ	846	PhosphothreonineBy similarity	1
Modified residueⁱ	848	PhosphothreonineBy similarity	1
Modified residueⁱ	854	PhosphothreonineCombined sources	1
Modified residueⁱ	861	PhosphothreonineCombined sources	1
Modified residueⁱ	868	PhosphothreonineCombined sources	1
Modified residueⁱ	912	PhosphoserineCombined sources	1
Modified residueⁱ	968	PhosphoserineCombined sources	1
Modified residueⁱ	1071	PhosphoserineBy similarity	1
Modified residueⁱ	1111	PhosphoserineCombined sources	1
Modified residueⁱ	1139	PhosphoserineBy similarity	1
Modified residueⁱ	1140	PhosphotyrosineBy similarity	1
Modified residueⁱ	1165	PhosphotyrosineBy similarity	1
Modified residueⁱ	1354	PhosphotyrosineBy similarity	1
Modified residueⁱ	1366	PhosphoserineCombined sources	1
Modified residueⁱ	1413	PhosphoserineCombined sources	1
Modified residueⁱ	1545	PhosphoserineCombined sources	1
Modified residueⁱ	1617	PhosphoserineCombined sources	1
Isoform Short (identifier: Q07157-2)
Modified residueⁱ	912	PhosphoserineCombined sources	1

Post-translational modificationⁱ

Phosphorylated at tyrosine redidues in response to epidermal growth factor (EGF) (PubMed:19332538, PubMed:7542259). This response is dependent on an intact actin microfilament system (PubMed:7542259). Dephosphorylated by PTPRJ (PubMed:19332538).2 Publications

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	Q07157
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q07157
PaxDbⁱ	Q07157
PeptideAtlas More...PeptideAtlasⁱ	Q07157
PRIDEⁱ	Q07157
ProteomicsDBⁱ	58506 58507 [Q07157-2]

PTM databases

iPTMnetⁱ	Q07157
PhosphoSitePlusⁱ	Q07157

Expressionⁱ

Tissue specificityⁱ

The alpha-containing isoform is found in most epithelial cell junctions. The short isoform is found both in endothelial cells and the highly specialized epithelial junctions of renal glomeruli and Sertoli cells of the seminiferous tubules.

Gene expression databases

Bgeeⁱ	ENSG00000104067
CleanExⁱ	HS_TJP1
ExpressionAtlasⁱ	Q07157 baseline and differential
Genevisibleⁱ	Q07157 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB010822 HPA001636 HPA001637

HPAⁱ

CAB010822
HPA001636
HPA001637

Interactionⁱ

Subunit structureⁱ

Homodimer (PubMed:17928286). Forms heterodimers (via the PDZ2 domain) with TJP2 and TJP3 (PubMed:9792688, PubMed:17928286, PubMed:16737969). Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJA12, GJD3 and UBN1 (PubMed:7798316, PubMed:11734628, PubMed:12023291, PubMed:12154091, PubMed:15183511, PubMed:18823282, PubMed:20200156). Interacts (via ZU5 domain) with CDC42BPB and MYZAP (PubMed:20093627, PubMed:21240187). Interacts (via PDZ domain) with GJA1 (PubMed:18636092). Interacts (via PDZ domains) with ANKRD2 (PubMed:22016770). Interacts with BVES (via the C-terminus cytoplasmic tail) (By similarity). Interacts with HSPA4 and KIRREL1 (By similarity). Interacts with DLL1 (By similarity). Interacts with USP53 (via the C-terminal region) (By similarity). Interacts (via ABR region) with F-actin (PubMed:9792688, PubMed:12354695, PubMed:20930113).By similarity15 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
ACTN4	O43707	4	EBI-79553,EBI-351526
GJA1	P17302	3	EBI-79553,EBI-1103439
Gjc1	P28229	3	EBI-79553,EBI-1767271	From Mus musculus.
GJD3	Q8N144	2	EBI-79553,EBI-2629520
KIRREL1	Q96J84	7	EBI-79553,EBI-3988456
Wwtr1	Q9EPK5	4	EBI-79553,EBI-1211920	From Mus musculus.

Show more details

GO - Molecular functionⁱ

cadherin binding
Source: BHF-UCL
Inferred from high throughput direct assayⁱ
- 25468996
calmodulin binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	112937, 113 interactors
CORUMⁱ	Q07157
ELMⁱ	Q07157
IntActⁱ	Q07157, 60 interactors
Molecular INTeraction database More...MINTⁱ	Q07157
STRINGⁱ	9606.ENSP00000281537

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	19 – 27	Combined sources	9
Turnⁱ	30 – 32	Combined sources	3
Beta strandⁱ	36 – 40	Combined sources	5
Turnⁱ	47 – 49	Combined sources	3
Beta strandⁱ	54 – 59	Combined sources	6
Turnⁱ	64 – 68	Combined sources	5
Beta strandⁱ	74 – 78	Combined sources	5
Helixⁱ	88 – 96	Combined sources	9
Beta strandⁱ	100 – 110	Combined sources	11
Beta strandⁱ	186 – 190	Combined sources	5
Turnⁱ	191 – 193	Combined sources	3
Beta strandⁱ	194 – 196	Combined sources	3
Beta strandⁱ	200 – 211	Combined sources	12
Helixⁱ	216 – 220	Combined sources	5
Beta strandⁱ	228 – 232	Combined sources	5
Helixⁱ	242 – 250	Combined sources	9
Turnⁱ	251 – 254	Combined sources	4
Beta strandⁱ	255 – 261	Combined sources	7
Beta strandⁱ	422 – 428	Combined sources	7
Beta strandⁱ	435 – 439	Combined sources	5
Beta strandⁱ	441 – 443	Combined sources	3
Beta strandⁱ	445 – 450	Combined sources	6
Beta strandⁱ	452 – 454	Combined sources	3
Helixⁱ	455 – 458	Combined sources	4
Beta strandⁱ	466 – 470	Combined sources	5
Helixⁱ	480 – 489	Combined sources	10
Beta strandⁱ	495 – 501	Combined sources	7
Helixⁱ	504 – 510	Combined sources	7
Beta strandⁱ	519 – 523	Combined sources	5
Beta strandⁱ	542 – 549	Combined sources	8
Helixⁱ	550 – 552	Combined sources	3
Beta strandⁱ	553 – 562	Combined sources	10
Helixⁱ	564 – 566	Combined sources	3
Beta strandⁱ	568 – 575	Combined sources	8
Helixⁱ	577 – 584	Combined sources	8
Beta strandⁱ	632 – 640	Combined sources	9
Beta strandⁱ	647 – 651	Combined sources	5
Helixⁱ	654 – 664	Combined sources	11
Turnⁱ	666 – 668	Combined sources	3
Beta strandⁱ	669 – 671	Combined sources	3
Beta strandⁱ	679 – 681	Combined sources	3
Helixⁱ	691 – 698	Combined sources	8
Turnⁱ	699 – 701	Combined sources	3
Beta strandⁱ	703 – 706	Combined sources	4
Helixⁱ	710 – 718	Combined sources	9
Beta strandⁱ	724 – 729	Combined sources	6
Helixⁱ	733 – 743	Combined sources	11
Helixⁱ	751 – 765	Combined sources	15
Helixⁱ	766 – 768	Combined sources	3
Beta strandⁱ	770 – 774	Combined sources	5
Helixⁱ	781 – 795	Combined sources	15
Beta strandⁱ	796 – 801	Combined sources	6
Beta strandⁱ	1633 – 1640	Combined sources	8
Beta strandⁱ	1645 – 1648	Combined sources	4
Turnⁱ	1650 – 1652	Combined sources	3
Beta strandⁱ	1655 – 1658	Combined sources	4
Beta strandⁱ	1669 – 1677	Combined sources	9
Beta strandⁱ	1679 – 1681	Combined sources	3
Turnⁱ	1687 – 1689	Combined sources	3
Beta strandⁱ	1701 – 1703	Combined sources	3
Beta strandⁱ	1706 – 1715	Combined sources	10
Helixⁱ	1720 – 1723	Combined sources	4
Helixⁱ	1732 – 1734	Combined sources	3
Turnⁱ	1735 – 1737	Combined sources	3
Beta strandⁱ	1738 – 1747	Combined sources	10

3D structure databases

ProteinModelPortalⁱ	Q07157
SMRⁱ	Q07157
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q07157

EvolutionaryTraceⁱ

Q07157

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	23 – 110	PDZ 1PROSITE-ProRule annotationAdd BLAST	88
Domainⁱ	186 – 264	PDZ 2PROSITE-ProRule annotationAdd BLAST	79
Domainⁱ	421 – 502	PDZ 3PROSITE-ProRule annotationAdd BLAST	82
Domainⁱ	516 – 584	SH3PROSITE-ProRule annotationAdd BLAST	69
Domainⁱ	598 – 779	Guanylate kinase-likePROSITE-ProRule annotationAdd BLAST	182
Domainⁱ	1634 – 1748	ZU5PROSITE-ProRule annotationAdd BLAST	115

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	633 – 876	Occludin (OCLN)-binding region1 PublicationAdd BLAST		244
Regionⁱ	1151 – 1371	Actin-binding region (ABR)1 PublicationAdd BLAST		221

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	1243 – 1248	Poly-Pro		6
Compositional biasⁱ	1426 – 1432	Poly-Pro		7

Domainⁱ

The 244-aa domain between residues 633 and 876 is the primary occludin (OCLN)-binding site and is required for stable association with the tight junction (PubMed:9792688).1 Publication

The C-terminal region (residues 1151-1372) is an actin-binding region (ABR) that interacts directly with F-actin and plays an important role in the localization of TJP1 at junctions (PubMed:9792688, PubMed:12354695, PubMed:20930113). The ABR is also required for the localization to puncta at the free edge of cells before initiation of cell-cell contact (PubMed:12354695). The ABR is also necessary for TJP1 recruitment to podosomes (PubMed:20930113).3 Publications

The second PDZ domain (PDZ2) mediates homodimerization and heterodimerization with TJP2 and TJP3 (PubMed:9792688, PubMed:17928286).2 Publications

Sequence similaritiesⁱ

Belongs to the MAGUK family.Curated

Keywords - Domainⁱ

Repeat, SH3 domain

Phylogenomic databases

eggNOGⁱ	KOG3580 Eukaryota ENOG410XQP3 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000118866
HOVERGENⁱ	HBG007849
InParanoidⁱ	Q07157
KEGG Orthology (KO) More...KOⁱ	K05701
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0AJZ
PhylomeDBⁱ	Q07157
TreeFamⁱ	TF315957

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd12026 SH3_ZO-1, 1 hit
InterProⁱ	View protein in InterPro IPR008145 GK/Ca_channel_bsu IPR008144 Guanylate_kin-like_dom IPR027417 P-loop_NTPase IPR001478 PDZ IPR036034 PDZ_sf IPR036028 SH3-like_dom_sf IPR001452 SH3_domain IPR005417 ZO IPR005418 ZO-1 IPR035597 ZO-1_SH3 IPR000906 ZU5_dom
PANTHERⁱ	PTHR13865:SF25 PTHR13865:SF25, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00625 Guanylate_kin, 1 hit PF00595 PDZ, 3 hits PF07653 SH3_2, 1 hit PF00791 ZU5, 1 hit
PRINTSⁱ	PR01597 ZONOCCLUDNS PR01598 ZONOCCLUDNS1
SMARTⁱ	View protein in SMART SM00072 GuKc, 1 hit SM00228 PDZ, 3 hits SM00218 ZU5, 1 hit
SUPFAMⁱ	SSF50044 SSF50044, 1 hit SSF50156 SSF50156, 3 hits SSF52540 SSF52540, 1 hit
PROSITEⁱ	View protein in PROSITE PS50052 GUANYLATE_KINASE_2, 1 hit PS50106 PDZ, 3 hits PS50002 SH3, 1 hit PS51145 ZU5, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform Long (identifier: Q07157-1) [UniParc]FASTA Add 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

        10         20         30         40         50
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG 
        60         70         80         90        100
ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK 
       110        120        130        140        150
NAKITIRRKK KVQIPVSRPD PEPVSDNEED SYDEEIHDPR SGRSGVVNRR 
       160        170        180        190        200
SEKIWPRDRS ASRERSLSPR SDRRSVASSQ PAKPTKVTLV KSRKNEEYGL 
       210        220        230        240        250
RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM SLTDAKTLIE 
       260        270        280        290        300
RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 
       310        320        330        340        350
GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG 
       360        370        380        390        400
AVSTPVKHAD DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP 
       410        420        430        440        450
VSPSDGVLPN STHEDGILRP SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV 
       460        470        480        490        500
LEDSPAAKEG LEEGDQILRV NNVDFTNIIR EEAVLFLLDL PKGEEVTILA 
       510        520        530        540        550
QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG EVFRVVDTLY 
       560        570        580        590        600
NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 
       610        620        630        640        650
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF 
       660        670        680        690        700
GPIADVAREK LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ 
       710        720        730        740        750
DKHALLDVTP NAVDRLNYAQ WYPIVVFLNP DSKQGVKTMR MRLCPESRKS 
       760        770        780        790        800
ARKLYERSHK LRKNNHHLFT TTINLNSMND GWYGALKEAI QQQQNQLVWV 
       810        820        830        840        850
SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT SDYEDTDTEG 
       860        870        880        890        900
GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 
       910        920        930        940        950
QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN 
       960        970        980        990       1000
LTNVRLEEPT PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT 
      1010       1020       1030       1040       1050
KVYRKDPYPE EMMRQNHVLK QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA 
      1060       1070       1080       1090       1100
SRDLEQPTYR YESSSYTDQF SRNYEHRLRY EDRVPMYEEQ WSYYDDKQPY 
      1110       1120       1130       1140       1150
PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY DSRPRYEQAP 
      1160       1170       1180       1190       1200
RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE 
      1210       1220       1230       1240       1250
QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ 
      1260       1270       1280       1290       1300
TEEEEDPAMK PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP 
      1310       1320       1330       1340       1350
SGAPIIGPKP TSQNQFSEHD KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE 
      1360       1370       1380       1390       1400
DEEYYRKQLS YFDRRSFENK PPAHIAASHL SEPAKPAHSQ NQSNFSSYSS 
      1410       1420       1430       1440       1450
KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ PVTSASLHIH 
      1460       1470       1480       1490       1500
SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP 
      1510       1520       1530       1540       1550
QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH 
      1560       1570       1580       1590       1600
NLLPSETAHK PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP 
      1610       1620       1630       1640       1650
KYQINNISTV PKAIPVSPSA VEEDEDEDGH TVVATARGIF NSNGGVLSSI 
      1660       1670       1680       1690       1700
ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS ILPPLDKEKG ETLLSPLVMC 
      1710       1720       1730       1740 
GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC VSVLIDHF

Length:1,748

Mass (Da):195,459

Last modified:January 24, 2006 - v3

Checksum:ⁱ189E31617084C0CC

Isoform Short (identifier: Q07157-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
922-1001: Missing.

« Hide

        10         20         30         40         50
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG 
        60         70         80         90        100
ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK 
       110        120        130        140        150
NAKITIRRKK KVQIPVSRPD PEPVSDNEED SYDEEIHDPR SGRSGVVNRR 
       160        170        180        190        200
SEKIWPRDRS ASRERSLSPR SDRRSVASSQ PAKPTKVTLV KSRKNEEYGL 
       210        220        230        240        250
RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM SLTDAKTLIE 
       260        270        280        290        300
RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 
       310        320        330        340        350
GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG 
       360        370        380        390        400
AVSTPVKHAD DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP 
       410        420        430        440        450
VSPSDGVLPN STHEDGILRP SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV 
       460        470        480        490        500
LEDSPAAKEG LEEGDQILRV NNVDFTNIIR EEAVLFLLDL PKGEEVTILA 
       510        520        530        540        550
QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG EVFRVVDTLY 
       560        570        580        590        600
NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 
       610        620        630        640        650
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF 
       660        670        680        690        700
GPIADVAREK LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ 
       710        720        730        740        750
DKHALLDVTP NAVDRLNYAQ WYPIVVFLNP DSKQGVKTMR MRLCPESRKS 
       760        770        780        790        800
ARKLYERSHK LRKNNHHLFT TTINLNSMND GWYGALKEAI QQQQNQLVWV 
       810        820        830        840        850
SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT SDYEDTDTEG 
       860        870        880        890        900
GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 
       910        920        930        940        950
QAQPQPIHRI DSPGFKPASQ QVYRKDPYPE EMMRQNHVLK QPAVSHPGHR 
       960        970        980        990       1000
PDKEPNLTYE PQLPYVEKQA SRDLEQPTYR YESSSYTDQF SRNYEHRLRY 
      1010       1020       1030       1040       1050
EDRVPMYEEQ WSYYDDKQPY PSRPPFDNQH SQDLDSRQHP EESSERGYFP 
      1060       1070       1080       1090       1100
RFEEPAPLSY DSRPRYEQAP RASALRHEEQ PAPGYDTHGR LRPEAQPHPS 
      1110       1120       1130       1140       1150
AGPKPAESKQ YFEQYSRSYE QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS 
      1160       1170       1180       1190       1200
QHKPEALPSN TKPLPPPPTQ TEEEEDPAMK PQSVLTRVKM FENKRSASLE 
      1210       1220       1230       1240       1250
TKKDVNDTGS FKPPEVASKP SGAPIIGPKP TSQNQFSEHD KTLYRIPEPQ 
      1260       1270       1280       1290       1300
KPQLKPPEDI VRSNHYDPEE DEEYYRKQLS YFDRRSFENK PPAHIAASHL 
      1310       1320       1330       1340       1350
SEPAKPAHSQ NQSNFSSYSS KGKPPEADGV DRSFGEKRYE PIQATPPPPP 
      1360       1370       1380       1390       1400
LPSQYAQPSQ PVTSASLHIH SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN 
      1410       1420       1430       1440       1450
KPATFRPPNR EDTAQAAFYP QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK 
      1460       1470       1480       1490       1500
PYTSSARPFE RKFESPKFNH NLLPSETAHK PDLSSKTPTS PKTLVKSHSL 
      1510       1520       1530       1540       1550
AQPPEFDSGV ETFSIHAEKP KYQINNISTV PKAIPVSPSA VEEDEDEDGH 
      1560       1570       1580       1590       1600
TVVATARGIF NSNGGVLSSI ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS 
      1610       1620       1630       1640       1650
ILPPLDKEKG ETLLSPLVMC GPHGLKFLKP VELRLPHCDP KTWQNKCLPG 
      1660 
DPNYLVGANC VSVLIDHF

Show »

Length:1,668

Mass (Da):186,966

Checksum:ⁱ5AD0570EC32FD9C3

Sequence cautionⁱ

The sequence AAA02891 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	394 – 417	QPDVD…HEDGI → NQMWIYLSVHLMVSYLIQLM KMGF in AAA02891 (PubMed:8395056).CuratedAdd BLAST	24
Sequence conflictⁱ	545	V → A in AAA02891 (PubMed:8395056).Curated	1
Sequence conflictⁱ	688	I → Y in AAA02891 (PubMed:8395056).Curated	1
Sequence conflictⁱ	762	R → A in AAA02891 (PubMed:8395056).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_025153	471	N → S1 PublicationCorresponds to variant dbSNP:rs2229517Ensembl.	1
Natural variantⁱVAR_025154	790	I → V3 PublicationsCorresponds to variant dbSNP:rs2229515Ensembl.	1
Natural variantⁱVAR_025155	930	P → L1 PublicationCorresponds to variant dbSNP:rs45529137Ensembl.	1
Natural variantⁱVAR_025156	1110	H → R1 PublicationCorresponds to variant dbSNP:rs45567033Ensembl.	1
Natural variantⁱVAR_025157	1347	D → A1 PublicationCorresponds to variant dbSNP:rs2291166Ensembl.	1
Natural variantⁱVAR_025158	1605	N → S1 PublicationCorresponds to variant dbSNP:rs45578638Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_003148	922 – 1001	Missing in isoform Short. CuratedAdd BLAST		80

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L14837 mRNA Translation: AAA02891.1 Different initiation. AK304758 mRNA Translation: BAG65513.1 DQ015919 Genomic DNA Translation: AAY22179.1 AC022613 Genomic DNA No translation available. BC111712 mRNA Translation: AAI11713.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS42007.1 [Q07157-1] CCDS45199.1 [Q07157-2]
PIRⁱ	A47747
NCBI Reference Sequences More...RefSeqⁱ	NP_003248.3, NM_003257.4 [Q07157-1] NP_783297.2, NM_175610.3 [Q07157-2]
UniGeneⁱ	Hs.743990

Genome annotation databases

Ensemblⁱ	ENST00000346128; ENSP00000281537; ENSG00000104067 [Q07157-1] ENST00000545208; ENSP00000441202; ENSG00000104067 [Q07157-2] ENST00000621049; ENSP00000484535; ENSG00000277401
GeneIDⁱ	7082
KEGGⁱ	hsa:7082
UCSC genome browser More...UCSCⁱ	uc001zcr.4 human [Q07157-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
Q07157	UPI000905269C		PANPR		1973
UPI0009486186		FELCA		1943
UPI00072E2B1F		ACIJB		1920
UPI000C9E5E65		HORSE		1863
UPI0004BD93C3		EQUPR		1758
+109
Q07157-2	UPI0007DC580B		HUMAN		1798
UPI000C9DC0ED		HORSE		1783
UPI000155D959		EQUPR		1678
Uncharacterized protein		PIG		1782
UPI00080A76C9		Cebus capucinus imitator		1772
+32

Protein	Similar proteins		Species	Score	Length
Q07157	UPI000905269C		PANPR		1973
UPI0009486186		FELCA		1943
UPI00072E2B1F		ACIJB		1920
UPI000C9E5E65		HORSE		1863
UPI0004BD93C3		EQUPR		1758
+302
Q07157-2	UPI0007DC580B		HUMAN		1798
UPI000C9DC0ED		HORSE		1783
UPI000155D959		EQUPR		1678
Uncharacterized protein		PIG		1782
UPI00080A76C9		Cebus capucinus imitator		1772
+1039

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2H2B	X-ray	1.60	A	18-110	[»]
2H2C	X-ray	2.00	A	18-110	[»]
2H3M	X-ray	2.90	A	18-110	[»]
2JWE	NMR	-	A/B	185-264	[»]
2KXR	NMR	-	A	1631-1748	[»]
2KXS	NMR	-	A	1631-1748	[»]
2RCZ	X-ray	1.70	A/B	186-264	[»]
3CYY	X-ray	2.40	A/B	182-273	[»]
3LH5	X-ray	2.60	A	516-803	[»]
3SHU	X-ray	2.75	A/B	421-512	[»]
3SHW	X-ray	2.90	A	421-888	[»]
3TSV	X-ray	1.99	A	417-516	[»]
3TSW	X-ray	2.85	A/B/C/D	417-803	[»]
3TSZ	X-ray	2.50	A	417-803	[»]
4OEO	X-ray	1.90	A/B/C	18-110	[»]
4OEP	X-ray	2.35	A/B	18-110	[»]
4Q2Q	X-ray	1.45	A	419-504	[»]
4YYX	X-ray	1.79	A/B	18-110	[»]
ProteinModelPortalⁱ	Q07157
SMRⁱ	Q07157
ModBaseⁱ	Search...
MobiDBⁱ	Search...

The DNASU plasmid repository More...DNASUⁱ	7082
Structural Biology Knowledgebase	Search...

CTDⁱ	7082
DisGeNET More...DisGeNETⁱ	7082
EuPathDBⁱ	HostDB:ENSG00000104067.16
GeneCardsⁱ	TJP1
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11827 TJP1
Human Protein Atlas More...HPAⁱ	CAB010822 HPA001636 HPA001637
MIMⁱ	601009 gene
neXtProtⁱ	NX_Q07157
Open Targets More...OpenTargetsⁱ	ENSG00000104067
PharmGKBⁱ	PA36532
GenAtlas: human gene database More...GenAtlasⁱ	Search...

ChiTaRSⁱ	TJP1 human
EvolutionaryTraceⁱ	Q07157
GeneWikiⁱ	Tight_junction_protein_1
GenomeRNAiⁱ	7082
Protein Ontology More...PROⁱ	PR:Q07157
SOURCEⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ZO1_HUMAN
Accessionⁱ	Q07157Primary (citable) accession number: Q07157 Secondary accession number(s): B4E3K1, Q2NKP3, Q4ZGJ6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
	Last sequence update:	January 24, 2006
	Last modified:	July 18, 2018
	This is version 205 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

3D-structure, Complete proteome, Reference proteome

Documents

Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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Tight junction protein ZO-1

TJP1

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ