位置:首页 > 蛋白库 > TSN1_HUMAN
TSN1_HUMAN
ID   TSN1_HUMAN              Reviewed;         241 AA.
AC   O60635; D3DQ14; O60745; Q5VST0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Tetraspanin-1;
DE            Short=Tspan-1;
DE   AltName: Full=Tetraspan NET-1;
DE   AltName: Full=Tetraspanin TM4-C;
GN   Name=TSPAN1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9714763; DOI=10.1016/s0167-4781(98)00087-6;
RA   Todd S.C., Doctor V.S., Levy S.;
RT   "Sequences and expression of six new members of the tetraspanin/TM4SF
RT   family.";
RL   Biochim. Biophys. Acta 1399:101-104(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Rubinstein E., Serru V., Boucheix C.;
RT   "New tetraspans identified in the EST database.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Puls K.L., Ni J., Liu D., Morahan G., Wright M.D.;
RT   "The molecular characterization of four tetraspanins.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-141; ASN-154; ASN-178 AND
RP   ASN-184, AND MUTAGENESIS OF ASN-141; ASN-154; ASN-178 AND ASN-184.
RX   PubMed=19508227; DOI=10.2174/092986609789071234;
RA   Scholz C.-J., Sauer G., Deissler H.;
RT   "Glycosylation of tetraspanin Tspan-1 at four distinct sites promotes its
RT   transition through the endoplasmic reticulum.";
RL   Protein Pept. Lett. 16:1244-1248(2009).
CC   -!- INTERACTION:
CC       O60635; O60779: SLC19A2; NbExp=5; IntAct=EBI-3914312, EBI-3941998;
CC       O60635; Q00059: TFAM; NbExp=3; IntAct=EBI-3914312, EBI-1049924;
CC       O60635; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-3914312, EBI-11742770;
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:19508227};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:19508227}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/TSPAN1ID44178ch1p34.html";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF054838; AAC69714.1; -; mRNA.
DR   EMBL; AF065388; AAC17119.1; -; mRNA.
DR   EMBL; AF133425; AAF08364.1; -; mRNA.
DR   EMBL; AK313774; BAG36512.1; -; mRNA.
DR   EMBL; AL672043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX06938.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06939.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06940.1; -; Genomic_DNA.
DR   EMBL; BC007290; AAH07290.1; -; mRNA.
DR   EMBL; BC013404; AAH13404.1; -; mRNA.
DR   CCDS; CCDS530.1; -.
DR   PIR; A59262; A59262.
DR   RefSeq; NP_005718.2; NM_005727.3.
DR   AlphaFoldDB; O60635; -.
DR   SMR; O60635; -.
DR   BioGRID; 115410; 40.
DR   IntAct; O60635; 4.
DR   STRING; 9606.ENSP00000361072; -.
DR   GlyConnect; 1797; 9 N-Linked glycans (2 sites).
DR   GlyGen; O60635; 4 sites, 10 N-linked glycans (2 sites).
DR   iPTMnet; O60635; -.
DR   PhosphoSitePlus; O60635; -.
DR   BioMuta; TSPAN1; -.
DR   EPD; O60635; -.
DR   jPOST; O60635; -.
DR   MassIVE; O60635; -.
DR   MaxQB; O60635; -.
DR   PaxDb; O60635; -.
DR   PeptideAtlas; O60635; -.
DR   PRIDE; O60635; -.
DR   ProteomicsDB; 49488; -.
DR   Antibodypedia; 32752; 278 antibodies from 31 providers.
DR   DNASU; 10103; -.
DR   Ensembl; ENST00000372003.6; ENSP00000361072.1; ENSG00000117472.10.
DR   GeneID; 10103; -.
DR   KEGG; hsa:10103; -.
DR   MANE-Select; ENST00000372003.6; ENSP00000361072.1; NM_005727.4; NP_005718.2.
DR   UCSC; uc001cpd.4; human.
DR   CTD; 10103; -.
DR   DisGeNET; 10103; -.
DR   GeneCards; TSPAN1; -.
DR   HGNC; HGNC:20657; TSPAN1.
DR   HPA; ENSG00000117472; Tissue enhanced (intestine).
DR   MalaCards; TSPAN1; -.
DR   MIM; 613170; gene.
DR   neXtProt; NX_O60635; -.
DR   OpenTargets; ENSG00000117472; -.
DR   PharmGKB; PA134938100; -.
DR   VEuPathDB; HostDB:ENSG00000117472; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   GeneTree; ENSGT00940000158851; -.
DR   HOGENOM; CLU_055524_4_1_1; -.
DR   InParanoid; O60635; -.
DR   OMA; HKESKCL; -.
DR   PhylomeDB; O60635; -.
DR   TreeFam; TF352892; -.
DR   PathwayCommons; O60635; -.
DR   SignaLink; O60635; -.
DR   BioGRID-ORCS; 10103; 10 hits in 1066 CRISPR screens.
DR   ChiTaRS; TSPAN1; human.
DR   GenomeRNAi; 10103; -.
DR   Pharos; O60635; Tbio.
DR   PRO; PR:O60635; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O60635; protein.
DR   Bgee; ENSG00000117472; Expressed in bronchial epithelial cell and 128 other tissues.
DR   Genevisible; O60635; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR   Gene3D; 1.10.1450.10; -; 1.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   InterPro; IPR000301; Tetraspanin_animals.
DR   InterPro; IPR018503; Tetraspanin_CS.
DR   InterPro; IPR008952; Tetraspanin_EC2_sf.
DR   PANTHER; PTHR19282; PTHR19282; 1.
DR   Pfam; PF00335; Tetraspanin; 1.
DR   PIRSF; PIRSF002419; Tetraspanin; 1.
DR   SUPFAM; SSF48652; SSF48652; 1.
DR   PROSITE; PS00421; TM4_1; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Lysosome; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..241
FT                   /note="Tetraspanin-1"
FT                   /id="PRO_0000219234"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..52
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19508227"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19508227"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19508227"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19508227"
FT   VARIANT         38
FT                   /note="S -> F (in dbSNP:rs2234267)"
FT                   /id="VAR_052327"
FT   VARIANT         87
FT                   /note="V -> M (in dbSNP:rs2234268)"
FT                   /id="VAR_034573"
FT   MUTAGEN         141
FT                   /note="N->A: Loss of glycosylation."
FT                   /evidence="ECO:0000269|PubMed:19508227"
FT   MUTAGEN         154
FT                   /note="N->A: Loss of glycosylation."
FT                   /evidence="ECO:0000269|PubMed:19508227"
FT   MUTAGEN         178
FT                   /note="N->A: Loss of glycosylation."
FT                   /evidence="ECO:0000269|PubMed:19508227"
FT   MUTAGEN         184
FT                   /note="N->A: Loss of glycosylation."
FT                   /evidence="ECO:0000269|PubMed:19508227"
FT   CONFLICT        189
FT                   /note="K -> E (in Ref. 1; AAC69714)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   241 AA;  26301 MW;  AF938AD7147CB884 CRC64;
     MQCFSFIKTM MILFNLLIFL CGAALLAVGI WVSIDGASFL KIFGPLSSSA MQFVNVGYFL
     IAAGVVVFAL GFLGCYGAKT ESKCALVTFF FILLLIFIAE VAAAVVALVY TTMAEHFLTL
     LVVPAIKKDY GSQEDFTQVW NTTMKGLKCC GFTNYTDFED SPYFKENSAF PPFCCNDNVT
     NTANETCTKQ KAHDQKVEGC FNQLLYDIRT NAVTVGGVAA GIGGLELAAM IVSMYLYCNL
     Q
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024