C9JWU8 (C9JWU8_HUMAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Gap junction protein RuleBase RU000630

Gene names

Name:

GJB1 Ensembl ENSP00000407223

Organism

Homo sapiens (Human) [Reference proteome] Ensembl ENSP00000407223

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	84 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell By similarity. RuleBase RU000630
Subunit structure	A connexon is composed of a hexamer of connexins By similarity. RuleBase RU000630
Subcellular location	Membrane; Multi-pass membrane protein By similarity RuleBase RU000630.
Sequence similarities	Belongs to the connexin family. RuleBase RU000630
Caution	The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSP00000407223

Ontologies

Keywords
Cellular component	Cell junction Cell membrane SAAS SAAS017990 Gap junction RuleBase RU000630 SAAS SAAS017990 Membrane
Domain	Transmembrane Transmembrane helix SAAS SAAS017990
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell communication Inferred from electronic annotation. Source: InterPro protein oligomerization Inferred from electronic annotation. Source: Compara purine ribonucleotide transport Inferred from electronic annotation. Source: Compara
Cellular_component	connexon complex Inferred from electronic annotation. Source: InterPro endoplasmic reticulum Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	gap junction channel activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Experimental info
	Non-terminal residue	84	1	Ensembl ENSP00000407223

Sequences

	Sequence		Length	Mass (Da)
	C9JWU8 [UniParc]. Last modified November 3, 2009. Version 1. Checksum: 74EDCFF878731D58	FASTA	84	9,549
	10 20 30 40 50 60 MNWTGLYTLL SGVNRHSTAI GRVWLSVIFI FRIMVLVVAA ESVWGDEKSS FICNTLQPGC 70 80 NSVCYDQFFP ISHVRLWSLQ LILV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	Ensembl Submitted (JUL-2011) to UniProtKB Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL590762 Genomic DNA. No translation available.
IPI	IPI00640484.
3D structure databases
ProteinModelPortal	C9JWU8.
SMR	C9JWU8. Positions 2-84.
ModBase	Search...
Protein-protein interaction databases
STRING	C9JWU8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000447581; ENSP00000407223; ENSG00000169562.
Organism-specific databases
HGNC	HGNC:4283. GJB1.
GenAtlas	Search...
Gene expression databases
ArrayExpress	C9JWU8.
Bgee	C9JWU8.
Family and domain databases
InterPro	IPR000500. Connexin. IPR017990. Connexin_CS. IPR013092. Connexin_N. [Graphical view]
PANTHER	PTHR11984. PTHR11984. 1 hit.
Pfam	PF00029. Connexin. 1 hit. [Graphical view]
PRINTS	PR00206. CONNEXIN.
SMART	SM00037. CNX. 1 hit. [Graphical view]
PROSITE	PS00407. CONNEXINS_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	35488124.

Entry information

Entry name

C9JWU8_HUMAN

Accession

Primary (citable) accession number: C9JWU8

Entry history

Integrated into UniProtKB/TrEMBL:	November 3, 2009
Last sequence update:	November 3, 2009
Last modified:	April 3, 2013
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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.