O60635 (TSN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tetraspanin-1
Short name=Tspan-1

Alternative name(s):
Tetraspan NET-1
Tetraspanin TM4-C

Gene names

Name:

TSPAN1

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	241 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subcellular location	Lysosome membrane; Multi-pass membrane protein Ref.8.
Sequence similarities	Belongs to the tetraspanin (TM4SF) family.

Ontologies

Keywords
Cellular component	Lysosome Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	integral to membrane Traceable author statement Ref.1. Source: ProtInc lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 241	241	Tetraspanin-1		PRO_0000219234
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 32	21	Helical; Potential
	Topological domain	33 – 52	20	Extracellular Potential
	Transmembrane	53 – 73	21	Helical; Potential
	Topological domain	74 – 88	15	Cytoplasmic Potential
	Transmembrane	89 – 109	21	Helical; Potential
	Topological domain	110 – 211	102	Extracellular Potential
	Transmembrane	212 – 232	21	Helical; Potential
	Topological domain	233 – 241	9	Cytoplasmic Potential
Amino acid modifications
	Glycosylation	141	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	154	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	178	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	184	1	N-linked (GlcNAc...) Ref.8
Natural variations
	Natural variant	38	1	S → F. Corresponds to variant rs2234267 [ dbSNP | Ensembl ].		VAR_052327
	Natural variant	87	1	V → M. Corresponds to variant rs2234268 [ dbSNP | Ensembl ].		VAR_034573
Experimental info
	Mutagenesis	141	1	N → A: Loss of glycosylation. Ref.8
	Mutagenesis	154	1	N → A: Loss of glycosylation. Ref.8
	Mutagenesis	178	1	N → A: Loss of glycosylation. Ref.8
	Mutagenesis	184	1	N → A: Loss of glycosylation. Ref.8
	Sequence conflict	189	1	K → E in AAC69714. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O60635 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: AF938AD7147CB884	FASTA	241	26,301
	10 20 30 40 50 60 MQCFSFIKTM MILFNLLIFL CGAALLAVGI WVSIDGASFL KIFGPLSSSA MQFVNVGYFL 70 80 90 100 110 120 IAAGVVVFAL GFLGCYGAKT ESKCALVTFF FILLLIFIAE VAAAVVALVY TTMAEHFLTL 130 140 150 160 170 180 LVVPAIKKDY GSQEDFTQVW NTTMKGLKCC GFTNYTDFED SPYFKENSAF PPFCCNDNVT 190 200 210 220 230 240 NTANETCTKQ KAHDQKVEGC FNQLLYDIRT NAVTVGGVAA GIGGLELAAM IVSMYLYCNL Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequences and expression of six new members of the tetraspanin/TM4SF family." Todd S.C., Doctor V.S., Levy S. Biochim. Biophys. Acta 1399:101-104(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"New tetraspans identified in the EST database." Rubinstein E., Serru V., Boucheix C. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The molecular characterization of four tetraspanins." Puls K.L., Ni J., Liu D., Morahan G., Wright M.D. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]. Tissue: Colon.
[8]	"Glycosylation of tetraspanin Tspan-1 at four distinct sites promotes its transition through the endoplasmic reticulum." Scholz C.-J., Sauer G., Deissler H. Protein Pept. Lett. 16:1244-1248(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-141; ASN-154; ASN-178 AND ASN-184, MUTAGENESIS OF ASN-141; ASN-154; ASN-178 AND ASN-184.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF054838 mRNA. Translation: AAC69714.1. AF065388 mRNA. Translation: AAC17119.1. AF133425 mRNA. Translation: AAF08364.1. AK313774 mRNA. Translation: BAG36512.1. AL672043 Genomic DNA. Translation: CAH72468.1. CH471059 Genomic DNA. Translation: EAX06938.1. CH471059 Genomic DNA. Translation: EAX06939.1. CH471059 Genomic DNA. Translation: EAX06940.1. BC007290 mRNA. Translation: AAH07290.1. BC013404 mRNA. Translation: AAH13404.1.
IPI	IPI00030936.
PIR	A59262.
RefSeq	NP_005718.2. NM_005727.3.
UniGene	Hs.38972.
3D structure databases
ProteinModelPortal	O60635.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60635. 1 interaction.
STRING	9606.ENSP00000236130.
Proteomic databases
PaxDb	O60635.
PeptideAtlas	O60635.
PRIDE	O60635.
Protocols and materials databases
DNASU	10103.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000372003; ENSP00000361072; ENSG00000117472.
GeneID	10103.
KEGG	hsa:10103.
UCSC	uc001cpd.3. human.
Organism-specific databases
CTD	10103.
GeneCards	GC01P046640.
HGNC	HGNC:20657. TSPAN1.
MIM	613170. gene.
neXtProt	NX_O60635.
PharmGKB	PA134938100.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG281528.
HOGENOM	HOG000230651.
HOVERGEN	HBG107159.
InParanoid	O60635.
OMA	GLKCCGF.
OrthoDB	EOG4T4CWZ.
PhylomeDB	O60635.
Gene expression databases
Bgee	O60635.
CleanEx	HS_TSPAN1.
Genevestigator	O60635.
GermOnline	ENSG00000117472. Homo sapiens.
Family and domain databases
InterPro	IPR000301. Tetraspanin. IPR018499. Tetraspanin/Peripherin. IPR018503. Tetraspanin_CS. IPR008952. Tetraspanin_EC2. [Graphical view]
Pfam	PF00335. Tetraspannin. 1 hit. [Graphical view]
PIRSF	PIRSF002419. Tetraspanin. 1 hit.
PRINTS	PR00259. TMFOUR.
SUPFAM	SSF48652. Tetraspanin. 1 hit.
PROSITE	PS00421. TM4_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10103.
NextBio	38217.
SOURCE	Search...

Entry information

Entry name

TSN1_HUMAN

Accession

Primary (citable) accession number: O60635
Secondary accession number(s): D3DQ14, O60745, Q5VST0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	April 3, 2013
This is version 103 of the entry and version 2 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.