Q16625 (OCLN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Occludin

Gene names

Name:

OCLN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions. Ref.11
Subunit structure	Interacts with TJP1/ZO1 and with VAPA. Ref.9
Subcellular location	Membrane; Multi-pass membrane protein. Cell junction › tight junction Ref.9 Ref.10 Ref.11.
Tissue specificity	Localized at tight junctions of both epithelial and endothelial cells. Highly expressed in kidney. Not detected in testis.
Domain	The C-terminal is cytoplasmic and is important for interaction with ZO-1. Sufficient for the tight junction localization. Involved in the regulation of the permeability barrier function of the tight junction By similarity. The first extracellular loop participates in an adhesive interaction. Ref.2
Post-translational modification	Dephosphorylated by PTPRJ. The tyrosine phosphorylation on Tyr-398 and Tyr-402 reduces its ability to interact with TJP1. Phosphorylation at Ser-490 also attenuates the interaction with TJP1. Ref.9 Ref.10 Ref.11 Ref.12
Involvement in disease	Band-like calcification with simplified gyration and polymicrogyria (BLCPMG) [MIM:251290]: A neurologic disorder with characteristic clinical and neuroradiologic features that mimic intrauterine TORCH infection in the absence of evidence of infection. Affected individuals have congenital microcephaly, intracranial calcifications, and severe developmental delay. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13
Sequence similarities	Belongs to the ELL/occludin family. Contains 1 MARVEL domain.

Ontologies

Keywords
Cellular component	Cell junction Membrane Tight junction
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Coiled coil Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell-cell junction organization Inferred from mutant phenotype PubMed 20164257. Source: MGI cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome protein complex assembly Traceable author statement PubMed 10749869. Source: ProtInc
Cellular_component	apical plasma membrane Inferred from electronic annotation. Source: Compara apicolateral plasma membrane Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay. Source: HPA tight junction Inferred from direct assay PubMed 20028514. Source: BHF-UCL
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16625-1)

Also known as: WT-OCLN; TM4(+);

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.

Isoform 2 (identifier: Q16625-2)

Also known as: OCLN-ex4del; TM4(-);

The sequence of this isoform differs from the canonical sequence as follows:
     244-297: Missing.

Isoform 3 (identifier: Q16625-3)

Also known as: OCLN-ex7ext;

The sequence of this isoform differs from the canonical sequence as follows:
     476-522: AAADEYNRLKQVKGSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQKT → VNST

Isoform 4 (identifier: Q16625-4)

Also known as: OCLN-ex3del; OCLN-ex3pdel;

The sequence of this isoform differs from the canonical sequence as follows:
     1-251: Missing.

Isoform 5 (identifier: Q16625-5)

Also known as: OCLN-ex3-4del;

The sequence of this isoform differs from the canonical sequence as follows:
     1-251: Missing.
     252-322: Missing.

Isoform 6 (identifier: Q16625-6)

Also known as: OCLN-ex3p-9pdel;

The sequence of this isoform differs from the canonical sequence as follows:
     50-69: DEILHFYKWTSPPGVIRILS → ESLQAVKEQIVTHQEDGWRL
     70-70: Missing.
     71-522: Missing.

Isoform 7 (identifier: Q16625-7)

Also known as: OCLN-ex3p-7pdel;

The sequence of this isoform differs from the canonical sequence as follows:
     52-70: ILHFYKWTSPPGVIRILSM → MTIEKKVKSTWLLLMNTID
     71-522: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 522

522

Occludin

PRO_0000146739

Regions

Topological domain

1 – 66

66

Cytoplasmic Potential

Transmembrane

67 – 89

23

Helical; Potential

Topological domain

90 – 135

46

Extracellular Ref.2

Transmembrane

136 – 160

25

Helical; Potential

Topological domain

161 – 170

10

Cytoplasmic Potential

Transmembrane

171 – 195

25

Helical; Potential

Topological domain

196 – 243

48

Extracellular Potential

Transmembrane

244 – 265

22

Helical; Potential

Topological domain

266 – 522

257

Cytoplasmic Potential

Domain

60 – 269

210

MARVEL

Coiled coil

426 – 489

64

Potential

Compositional bias

92 – 131

40

Gly/Tyr-rich

Amino acid modifications

Modified residue

340

1

Phosphoserine By similarity

Modified residue

398

1

Phosphotyrosine Ref.9

Modified residue

402

1

Phosphotyrosine Ref.9

Modified residue

403

1

Phosphothreonine; by PKC/PRKCH Ref.11

Modified residue

404

1

Phosphothreonine; by PKC/PRKCH Ref.11

Modified residue

490

1

Phosphoserine Ref.12

Natural variations

Alternative sequence

1 – 251

251

Missing in isoform 4 and isoform 5.

VSP_043872

Alternative sequence

50 – 69

20

DEILH…IRILS → ESLQAVKEQIVTHQEDGWRL in isoform 6.

VSP_043873

Alternative sequence

52 – 70

19

ILHFY…RILSM → MTIEKKVKSTWLLLMNTID in isoform 7.

VSP_043874

Alternative sequence

70

1

Missing in isoform 6.

VSP_043875

Alternative sequence

71 – 522

452

Missing in isoform 6 and isoform 7.

VSP_043876

Alternative sequence

244 – 297

54

Missing in isoform 2.

VSP_043877

Alternative sequence

252 – 322

71

Missing in isoform 5.

VSP_043878

Alternative sequence

476 – 522

47

AAADE…DRQKT → VNST in isoform 3.

VSP_043879

Natural variant

219

1

F → S in BLCPMG. Ref.13

VAR_064910

Experimental info

Mutagenesis

398

1

Y → A: Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with A-402. Ref.9

Mutagenesis

398

1

Y → D: Loss of phosphorylation, almost complete loss of binding to TJP1, loss of regulation of TJP1 binding and loss of localization to plasma membrane and sites of cell-cell contact; when associated with D-402. Ref.9

Mutagenesis

398

1

Y → F: Loss of phosphorylation, decrease in binding to TJP1 and significant loss of regulation of TJP1 binding; when associated with F-402. Ref.9

Mutagenesis

402

1

Y → A: Loss of phosphorylation and loss of regulation of TJP1 binding; when associated with A-398. Ref.9

Mutagenesis

402

1

Y → D: Loss of phosphorylation, almost complete loss of binding to TJP1, loss of regulation of TJP1 binding and loss of localization to plasma membrane and sites of cell-cell contact; when associated with D-398. Ref.9

Mutagenesis

402

1

Y → F: Loss of phosphorylation, decrease in binding to TJP1 and significant loss of regulation of TJP1 binding; when associated with F-398. Ref.9

Mutagenesis

404

1

T → A: Loss of localization to the tight junctions. Ref.11

Sequence conflict

233

1

L → S in AAH29886. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

522

Helix Strand Turn

Details...

Turn

417 – 419

3

Helix

426 – 466

41

Helix

472 – 488

17

Helix

491 – 520

30

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (WT-OCLN) (TM4(+)) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A0CF9574BCF6E974	FASTA	522	59,144
	10 20 30 40 50 60 MSSRPLESPP PYRPDEFKPN HYAPSNDIYG GEMHVRPMLS QPAYSFYPED EILHFYKWTS 70 80 90 100 110 120 PPGVIRILSM LIIVMCIAIF ACVASTLAWD RGYGTSLLGG SVGYPYGGSG FGSYGSGYGY 130 140 150 160 170 180 GYGYGYGYGG YTDPRAAKGF MLAMAAFCFI AALVIFVTSV IRSEMSRTRR YYLSVIIVSA 190 200 210 220 230 240 ILGIMVFIAT IVYIMGVNPT AQSSGSLYGS QIYALCNQFY TPAATGLYVD QYLYHYCVVD 250 260 270 280 290 300 PQEAIAIVLG FMIIVAFALI IFFAVKTRRK MDRYDKSNIL WDKEHIYDEQ PPNVEEWVKN 310 320 330 340 350 360 VSAGTQDVPS PPSDYVERVD SPMAYSSNGK VNDKRFYPES SYKSTPVPEV VQELPLTSPV 370 380 390 400 410 420 DDFRQPRYSS GGNFETPSKR APAKGRAGRS KRTEQDHYET DYTTGGESCD ELEEDWIREY 430 440 450 460 470 480 PPITSDQQRQ LYKRNFDTGL QEYKSLQSEL DEINKELSRL DKELDDYREE SEEYMAAADE 490 500 510 520 YNRLKQVKGS ADYKSKKNHC KQLKSKLSHI KKMVGDYDRQ KT
	Isoform 2 (OCLN-ex4del) (TM4(-)) [UniParc]. Checksum: 570C03F39D5B9F09	FASTA	468	52,706
	10 20 30 40 50 60 MSSRPLESPP PYRPDEFKPN HYAPSNDIYG GEMHVRPMLS QPAYSFYPED EILHFYKWTS 70 80 90 100 110 120 PPGVIRILSM LIIVMCIAIF ACVASTLAWD RGYGTSLLGG SVGYPYGGSG FGSYGSGYGY 130 140 150 160 170 180 GYGYGYGYGG YTDPRAAKGF MLAMAAFCFI AALVIFVTSV IRSEMSRTRR YYLSVIIVSA 190 200 210 220 230 240 ILGIMVFIAT IVYIMGVNPT AQSSGSLYGS QIYALCNQFY TPAATGLYVD QYLYHYCVVD 250 260 270 280 290 300 PQEVKNVSAG TQDVPSPPSD YVERVDSPMA YSSNGKVNDK RFYPESSYKS TPVPEVVQEL 310 320 330 340 350 360 PLTSPVDDFR QPRYSSGGNF ETPSKRAPAK GRAGRSKRTE QDHYETDYTT GGESCDELEE 370 380 390 400 410 420 DWIREYPPIT SDQQRQLYKR NFDTGLQEYK SLQSELDEIN KELSRLDKEL DDYREESEEY 430 440 450 460 MAAADEYNRL KQVKGSADYK SKKNHCKQLK SKLSHIKKMV GDYDRQKT
	Isoform 3 (OCLN-ex7ext) [UniParc]. Checksum: BAC5CDCFD4AB3FE9	FASTA	479	54,124
	10 20 30 40 50 60 MSSRPLESPP PYRPDEFKPN HYAPSNDIYG GEMHVRPMLS QPAYSFYPED EILHFYKWTS 70 80 90 100 110 120 PPGVIRILSM LIIVMCIAIF ACVASTLAWD RGYGTSLLGG SVGYPYGGSG FGSYGSGYGY 130 140 150 160 170 180 GYGYGYGYGG YTDPRAAKGF MLAMAAFCFI AALVIFVTSV IRSEMSRTRR YYLSVIIVSA 190 200 210 220 230 240 ILGIMVFIAT IVYIMGVNPT AQSSGSLYGS QIYALCNQFY TPAATGLYVD QYLYHYCVVD 250 260 270 280 290 300 PQEAIAIVLG FMIIVAFALI IFFAVKTRRK MDRYDKSNIL WDKEHIYDEQ PPNVEEWVKN 310 320 330 340 350 360 VSAGTQDVPS PPSDYVERVD SPMAYSSNGK VNDKRFYPES SYKSTPVPEV VQELPLTSPV 370 380 390 400 410 420 DDFRQPRYSS GGNFETPSKR APAKGRAGRS KRTEQDHYET DYTTGGESCD ELEEDWIREY 430 440 450 460 470 PPITSDQQRQ LYKRNFDTGL QEYKSLQSEL DEINKELSRL DKELDDYREE SEEYMVNST
	Isoform 4 (OCLN-ex3del) (OCLN-ex3pdel) [UniParc]. Checksum: 17110B0747658560	FASTA	271	31,602
	10 20 30 40 50 60 MIIVAFALII FFAVKTRRKM DRYDKSNILW DKEHIYDEQP PNVEEWVKNV SAGTQDVPSP 70 80 90 100 110 120 PSDYVERVDS PMAYSSNGKV NDKRFYPESS YKSTPVPEVV QELPLTSPVD DFRQPRYSSG 130 140 150 160 170 180 GNFETPSKRA PAKGRAGRSK RTEQDHYETD YTTGGESCDE LEEDWIREYP PITSDQQRQL 190 200 210 220 230 240 YKRNFDTGLQ EYKSLQSELD EINKELSRLD KELDDYREES EEYMAAADEY NRLKQVKGSA 250 260 270 DYKSKKNHCK QLKSKLSHIK KMVGDYDRQK T
	Isoform 5 (OCLN-ex3-4del) [UniParc]. Checksum: CA521768CF62815F	FASTA	200	23,324
	10 20 30 40 50 60 MAYSSNGKVN DKRFYPESSY KSTPVPEVVQ ELPLTSPVDD FRQPRYSSGG NFETPSKRAP 70 80 90 100 110 120 AKGRAGRSKR TEQDHYETDY TTGGESCDEL EEDWIREYPP ITSDQQRQLY KRNFDTGLQE 130 140 150 160 170 180 YKSLQSELDE INKELSRLDK ELDDYREESE EYMAAADEYN RLKQVKGSAD YKSKKNHCKQ 190 200 LKSKLSHIKK MVGDYDRQKT
	Isoform 6 (OCLN-ex3p-9pdel) [UniParc]. Checksum: 44E322DFFA119B8E	FASTA	69	8,033
	10 20 30 40 50 60 MSSRPLESPP PYRPDEFKPN HYAPSNDIYG GEMHVRPMLS QPAYSFYPEE SLQAVKEQIV THQEDGWRL
	Isoform 7 (OCLN-ex3p-7pdel) [UniParc]. Checksum: FF4DA5B4703A5BAD	FASTA	70	8,175
	10 20 30 40 50 60 MSSRPLESPP PYRPDEFKPN HYAPSNDIYG GEMHVRPMLS QPAYSFYPED EMTIEKKVKS 70 TWLLLMNTID

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Interspecies diversity of the occludin sequence: cDNA cloning of human, mouse, dog, and rat-kangaroo homologues." Ando-Akatsuka Y., Saitou M., Hirase T., Kishi M., Sakakibara A., Itoh M., Yonemura S., Furuse M., Tsukita S. J. Cell Biol. 133:43-47(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Colon carcinoma.
[2]	"Occludin confers adhesiveness when expressed in fibroblasts." Van Itallie C.M., Anderson J.M. J. Cell Sci. 110:1113-1121(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DOMAIN, TOPOLOGY. Tissue: Liver.
[3]	"Splicing diversity of the human OCLN gene and its biological significance for hepatitis C virus entry." Kohaar I., Ploss A., Korol E., Mu K., Schoggins J.W., O'Brien T.R., Rice C.M., Prokunina-Olsson L. J. Virol. 84:6987-6994(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), ALTERNATIVE SPLICING. Tissue: Liver.
[4]	"Genomic structure of occludin gene." Fukasawa M., Toyota T., Yoshitsugu K., Yoshikawa T. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORM 1). Tissue: Brain and Lung.
[8]	"Occludin TM4(-): an isoform of the tight junction protein present in primates lacking the fourth transmembrane domain." Ghassemifar M.R., Sheth B., Papenbrock T., Leese H.J., Houghton F.D., Fleming T.P. J. Cell Sci. 115:3171-3180(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
[9]	"Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions." Elias B.C., Suzuki T., Seth A., Giorgianni F., Kale G., Shen L., Turner J.R., Naren A., Desiderio D.M., Rao R. J. Biol. Chem. 284:1559-1569(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TJP1, PHOSPHORYLATION AT TYR-398 AND TYR-402, MUTAGENESIS OF TYR-398 AND TYR-402, SUBCELLULAR LOCATION.
[10]	"Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells." Sallee J.L., Burridge K. J. Biol. Chem. 284:14997-15006(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION.
[11]	"PKC eta regulates occludin phosphorylation and epithelial tight junction integrity." Suzuki T., Elias B.C., Seth A., Shen L., Turner J.R., Giorgianni F., Desiderio D., Guntaka R., Rao R. Proc. Natl. Acad. Sci. U.S.A. 106:61-66(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-403 AND THR-404, MUTAGENESIS OF THR-404.
[12]	"Identification and analysis of occludin phosphosites: a combined mass spectrometry and bioinformatics approach." Sundstrom J.M., Tash B.R., Murakami T., Flanagan J.M., Bewley M.C., Stanley B.A., Gonsar K.B., Antonetti D.A. J. Proteome Res. 8:808-817(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 416-522, PHOSPHORYLATION AT SER-490.
[13]	"Recessive mutations in the gene encoding the tight junction protein occludin cause band-like calcification with simplified gyration and polymicrogyria." O'Driscoll M.C., Daly S.B., Urquhart J.E., Black G.C., Pilz D.T., Brockmann K., McEntagart M., Abdel-Salam G., Zaki M., Wolf N.I., Ladda R.L., Sell S., D'Arrigo S., Squier W., Dobyns W.B., Livingston J.H., Crow Y.J. Am. J. Hum. Genet. 87:354-364(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BLCPMG SER-219.
+	Additional computationally mapped references.

Web resources

Wikipedia

Occludin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U49184 mRNA. Translation: AAC50451.1.
U53823 mRNA. Translation: AAB00195.1.
FJ786083 mRNA. Translation: ACT53743.1.
FJ786084 mRNA. Translation: ACT53744.1.
AF400630 , AF400623, AF400624, AF400625, AF400626, AF400627, AF400628, AF400629 Genomic DNA. Translation: AAL47094.1.
GQ225096 mRNA. Translation: ACT83431.1.
GQ225097 mRNA. Translation: ACT83432.1.
GQ225098 mRNA. Translation: ACT83433.1.
GQ402517 mRNA. Translation: ACZ80515.1.
AB451306 mRNA. Translation: BAG70120.1.
AB451437 mRNA. Translation: BAG70251.1.
AC145146 Genomic DNA. No translation available.
AC147575 Genomic DNA. No translation available.
BC029886 mRNA. Translation: AAH29886.1.
BK001650 mRNA. Translation: DAA01837.1.

IPI

IPI00003373.
IPI00479078.
IPI00954898.
IPI00954920.
IPI00965141.
IPI00978567.

PIR

G02533.

RefSeq

NP_001192183.1. NM_001205254.1.
NP_001192184.1. NM_001205255.1.
NP_002529.1. NM_002538.3.

UniGene

Hs.592605.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WPA	X-ray	1.50	A	413-522	[»]
1XAW	X-ray	1.45	A	383-522	[»]
3G7C	X-ray	2.00	A	416-522	[»]

ProteinModelPortal

Q16625.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42791N.

IntAct

Q16625. 1 interaction.

MINT

MINT-5006137.

STRING

9606.ENSP00000347379.

PTM databases

PhosphoSite

Q16625.

Polymorphism databases

DMDM

3914196.

Proteomic databases

PaxDb

Q16625.

PRIDE

Q16625.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355237; ENSP00000347379; ENSG00000197822.
ENST00000380766; ENSP00000370143; ENSG00000197822.
ENST00000396442; ENSP00000379719; ENSG00000197822.
ENST00000538151; ENSP00000445940; ENSG00000197822.
ENST00000542132; ENSP00000440000; ENSG00000197822.

GeneID

100506658.

KEGG

hsa:100506658.

UCSC

uc003jwu.3. human.

Organism-specific databases

CTD

100506658.

GeneCards

GC05P068788.

HGNC

HGNC:8104. OCLN.

HPA

CAB013075.
HPA005933.

MIM

251290. phenotype.
602876. gene.

neXtProt

NX_Q16625.

Orphanet

1229. Congenital intrauterine infection-like syndrome.

PharmGKB

PA31893.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG71745.

HOGENOM

HOG000233490.

HOVERGEN

HBG004523.

InParanoid

Q16625.

KO

K06088.

OMA

MMFIATI.

OrthoDB

EOG4J9N09.

PhylomeDB

Q16625.

Enzyme and pathway databases

Pathway_Interaction_DB

tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_578. Apoptosis.

Gene expression databases

Bgee

Q16625.

CleanEx

HS_OCLN.

Genevestigator

Q16625.

GermOnline

ENSG00000197822. Homo sapiens.

Family and domain databases

InterPro

IPR008253. Marvel.
IPR021128. MARVEL-like_dom.
IPR002958. Occludin.
IPR010844. Occludin_RNApol2_elong_fac_ELL.
[Graphical view]

PANTHER

PTHR23288:SF4. PTHR23288:SF4. 1 hit.

Pfam

PF01284. MARVEL. 1 hit.
PF07303. Occludin_ELL. 1 hit.
[Graphical view]

PIRSF

PIRSF005993. Occludin. 1 hit.

PRINTS

PR01258. OCCLUDIN.

PROSITE

PS51225. MARVEL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q16625.

GenomeRNAi

100506658.

NextBio

34054345.

PMAP-CutDB

Q16625.

SOURCE

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Entry information

Entry name

OCLN_HUMAN

Accession

Primary (citable) accession number: Q16625
Secondary accession number(s): B5BU70 , D2DU64, D2DU65, D2IGC0, D2IGC1, E2CYV9, Q5U1V4, Q8N6K1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.