Full text data of SCAMP2
SCAMP2
[Confidence: low (only semi-automatic identification from reviews)]
Secretory carrier-associated membrane protein 2; Secretory carrier membrane protein 2
Secretory carrier-associated membrane protein 2; Secretory carrier membrane protein 2
UniProt
O15127
ID SCAM2_HUMAN Reviewed; 329 AA.
AC O15127; B2RDF0; Q9BQE8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JUL-2001, sequence version 2.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Secretory carrier-associated membrane protein 2;
DE Short=Secretory carrier membrane protein 2;
GN Name=SCAMP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9378760;
RA Singleton D.R., Wu T.T., Castle J.D.;
RT "Three mammalian SCAMPs (secretory carrier membrane proteins) are
RT highly related products of distinct genes having similar subcellular
RT distributions.";
RL J. Cell Sci. 110:2099-2107(1997).
RN [2]
RP SEQUENCE REVISION.
RA Singleton D.R., Wu T.T., Castle J.D.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SLC9A7.
RX PubMed=15840657; DOI=10.1242/jcs.02315;
RA Lin P.J., Williams W.P., Luu Y., Molday R.S., Orlowski J., Numata M.;
RT "Secretory carrier membrane proteins interact and regulate trafficking
RT of the organellar (Na+,K+)/H+ exchanger NHE7.";
RL J. Cell Sci. 118:1885-1897(2005).
RN [7]
RP INTERACTION WITH SLC6A4.
RX PubMed=16870614; DOI=10.1074/jbc.M602848200;
RA Mueller H.K., Wiborg O., Haase J.;
RT "Subcellular redistribution of the serotonin transporter by secretory
RT carrier membrane protein 2.";
RL J. Biol. Chem. 281:28901-28909(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC recycling carrier to the cell surface.
CC -!- SUBUNIT: Interacts with SLC6A4 and SLC9A7.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC membrane; Multi-pass membrane protein. Recycling endosome
CC membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the SCAMP family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF005038; AAB62723.2; -; mRNA.
DR EMBL; AK315516; BAG37897.1; -; mRNA.
DR EMBL; CH471136; EAW99300.1; -; Genomic_DNA.
DR EMBL; BC001376; AAH01376.1; -; mRNA.
DR EMBL; BC004385; AAH04385.1; -; mRNA.
DR RefSeq; NP_005688.2; NM_005697.3.
DR UniGene; Hs.458917; -.
DR ProteinModelPortal; O15127; -.
DR IntAct; O15127; 4.
DR MINT; MINT-5003778; -.
DR STRING; 9606.ENSP00000268099; -.
DR PhosphoSite; O15127; -.
DR PaxDb; O15127; -.
DR PeptideAtlas; O15127; -.
DR PRIDE; O15127; -.
DR Ensembl; ENST00000268099; ENSP00000268099; ENSG00000140497.
DR GeneID; 10066; -.
DR KEGG; hsa:10066; -.
DR UCSC; uc002azb.1; human.
DR CTD; 10066; -.
DR GeneCards; GC15M075136; -.
DR HGNC; HGNC:10564; SCAMP2.
DR HPA; HPA014699; -.
DR HPA; HPA019194; -.
DR MIM; 606912; gene.
DR neXtProt; NX_O15127; -.
DR PharmGKB; PA34977; -.
DR eggNOG; NOG285953; -.
DR HOGENOM; HOG000294221; -.
DR HOVERGEN; HBG071938; -.
DR InParanoid; O15127; -.
DR OMA; SIIMMVV; -.
DR OrthoDB; EOG7FZ009; -.
DR PhylomeDB; O15127; -.
DR ChiTaRS; SCAMP2; human.
DR GeneWiki; SCAMP2; -.
DR GenomeRNAi; 10066; -.
DR NextBio; 38041; -.
DR PRO; PR:O15127; -.
DR ArrayExpress; O15127; -.
DR Bgee; O15127; -.
DR CleanEx; HS_SCAMP2; -.
DR Genevestigator; O15127; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral to membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endosome; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1 329 Secretory carrier-associated membrane
FT protein 2.
FT /FTId=PRO_0000191254.
FT TOPO_DOM 1 153 Cytoplasmic (Potential).
FT TRANSMEM 154 174 Helical; (Potential).
FT TOPO_DOM 175 181 Lumenal (Potential).
FT TRANSMEM 182 202 Helical; (Potential).
FT TOPO_DOM 203 218 Cytoplasmic (Potential).
FT TRANSMEM 219 239 Helical; (Potential).
FT TOPO_DOM 240 262 Lumenal (Potential).
FT TRANSMEM 263 283 Helical; (Potential).
FT TOPO_DOM 284 329 Cytoplasmic (Potential).
FT REGION 203 218 Interaction with SLC9A7.
FT MOD_RES 319 319 Phosphoserine.
FT MOD_RES 320 320 Phosphoserine.
SQ SEQUENCE 329 AA; 36649 MW; 046ACB926FD951DD CRC64;
MSAFDTNPFA DPVDVNPFQD PSVTQLTNAP QGGLAEFNPF SETNAATTVP VTQLPGSSQP
AVLQPSVEPT QPTPQAVVSA AQAGLLRQQE ELDRKAAELE RKERELQNTV ANLHVRQNNW
PPLPSWCPVK PCFYQDFSTE IPADYQRICK MLYYLWMLHS VTLFLNLLAC LAWFSGNSSK
GVDFGLSILW FLIFTPCAFL CWYRPIYKAF RSDNSFSFFV FFFVFFCQIG IYIIQLVGIP
GLGDSGWIAA LSTLDNHSLA ISVIMMVVAG FFTLCAVLSV FLLQRVHSLY RRTGASFQQA
QEEFSQGIFS SRTFHRAASS AAQGAFQGN
//
ID SCAM2_HUMAN Reviewed; 329 AA.
AC O15127; B2RDF0; Q9BQE8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JUL-2001, sequence version 2.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=Secretory carrier-associated membrane protein 2;
DE Short=Secretory carrier membrane protein 2;
GN Name=SCAMP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9378760;
RA Singleton D.R., Wu T.T., Castle J.D.;
RT "Three mammalian SCAMPs (secretory carrier membrane proteins) are
RT highly related products of distinct genes having similar subcellular
RT distributions.";
RL J. Cell Sci. 110:2099-2107(1997).
RN [2]
RP SEQUENCE REVISION.
RA Singleton D.R., Wu T.T., Castle J.D.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SLC9A7.
RX PubMed=15840657; DOI=10.1242/jcs.02315;
RA Lin P.J., Williams W.P., Luu Y., Molday R.S., Orlowski J., Numata M.;
RT "Secretory carrier membrane proteins interact and regulate trafficking
RT of the organellar (Na+,K+)/H+ exchanger NHE7.";
RL J. Cell Sci. 118:1885-1897(2005).
RN [7]
RP INTERACTION WITH SLC6A4.
RX PubMed=16870614; DOI=10.1074/jbc.M602848200;
RA Mueller H.K., Wiborg O., Haase J.;
RT "Subcellular redistribution of the serotonin transporter by secretory
RT carrier membrane protein 2.";
RL J. Biol. Chem. 281:28901-28909(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC recycling carrier to the cell surface.
CC -!- SUBUNIT: Interacts with SLC6A4 and SLC9A7.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC membrane; Multi-pass membrane protein. Recycling endosome
CC membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the SCAMP family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF005038; AAB62723.2; -; mRNA.
DR EMBL; AK315516; BAG37897.1; -; mRNA.
DR EMBL; CH471136; EAW99300.1; -; Genomic_DNA.
DR EMBL; BC001376; AAH01376.1; -; mRNA.
DR EMBL; BC004385; AAH04385.1; -; mRNA.
DR RefSeq; NP_005688.2; NM_005697.3.
DR UniGene; Hs.458917; -.
DR ProteinModelPortal; O15127; -.
DR IntAct; O15127; 4.
DR MINT; MINT-5003778; -.
DR STRING; 9606.ENSP00000268099; -.
DR PhosphoSite; O15127; -.
DR PaxDb; O15127; -.
DR PeptideAtlas; O15127; -.
DR PRIDE; O15127; -.
DR Ensembl; ENST00000268099; ENSP00000268099; ENSG00000140497.
DR GeneID; 10066; -.
DR KEGG; hsa:10066; -.
DR UCSC; uc002azb.1; human.
DR CTD; 10066; -.
DR GeneCards; GC15M075136; -.
DR HGNC; HGNC:10564; SCAMP2.
DR HPA; HPA014699; -.
DR HPA; HPA019194; -.
DR MIM; 606912; gene.
DR neXtProt; NX_O15127; -.
DR PharmGKB; PA34977; -.
DR eggNOG; NOG285953; -.
DR HOGENOM; HOG000294221; -.
DR HOVERGEN; HBG071938; -.
DR InParanoid; O15127; -.
DR OMA; SIIMMVV; -.
DR OrthoDB; EOG7FZ009; -.
DR PhylomeDB; O15127; -.
DR ChiTaRS; SCAMP2; human.
DR GeneWiki; SCAMP2; -.
DR GenomeRNAi; 10066; -.
DR NextBio; 38041; -.
DR PRO; PR:O15127; -.
DR ArrayExpress; O15127; -.
DR Bgee; O15127; -.
DR CleanEx; HS_SCAMP2; -.
DR Genevestigator; O15127; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral to membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endosome; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1 329 Secretory carrier-associated membrane
FT protein 2.
FT /FTId=PRO_0000191254.
FT TOPO_DOM 1 153 Cytoplasmic (Potential).
FT TRANSMEM 154 174 Helical; (Potential).
FT TOPO_DOM 175 181 Lumenal (Potential).
FT TRANSMEM 182 202 Helical; (Potential).
FT TOPO_DOM 203 218 Cytoplasmic (Potential).
FT TRANSMEM 219 239 Helical; (Potential).
FT TOPO_DOM 240 262 Lumenal (Potential).
FT TRANSMEM 263 283 Helical; (Potential).
FT TOPO_DOM 284 329 Cytoplasmic (Potential).
FT REGION 203 218 Interaction with SLC9A7.
FT MOD_RES 319 319 Phosphoserine.
FT MOD_RES 320 320 Phosphoserine.
SQ SEQUENCE 329 AA; 36649 MW; 046ACB926FD951DD CRC64;
MSAFDTNPFA DPVDVNPFQD PSVTQLTNAP QGGLAEFNPF SETNAATTVP VTQLPGSSQP
AVLQPSVEPT QPTPQAVVSA AQAGLLRQQE ELDRKAAELE RKERELQNTV ANLHVRQNNW
PPLPSWCPVK PCFYQDFSTE IPADYQRICK MLYYLWMLHS VTLFLNLLAC LAWFSGNSSK
GVDFGLSILW FLIFTPCAFL CWYRPIYKAF RSDNSFSFFV FFFVFFCQIG IYIIQLVGIP
GLGDSGWIAA LSTLDNHSLA ISVIMMVVAG FFTLCAVLSV FLLQRVHSLY RRTGASFQQA
QEEFSQGIFS SRTFHRAASS AAQGAFQGN
//
MIM
606912
*RECORD*
*FIELD* NO
606912
*FIELD* TI
*606912 SECRETORY CARRIER MEMBRANE PROTEIN 2; SCAMP2
*FIELD* TX
CLONING
Singleton et al. (1997) amplified SCAMP2 by PCR using primers designed
read morefrom SCAMP1 (606911). They cloned the full-length SCAMP2 cDNA from a
HeLa cell cDNA library. They also identified SCAMP3 (606913) as another
paralog in the HeLa cell library. SCAMP2 encodes a deduced 329-amino
acid protein with a calculated molecular mass of 36.6 kD. The protein
shares structural features with SCAMP1 and SCAMP3, including a leucine
zipper-like segment, a proline-rich element, an extended central core
that includes 4 putative transmembrane domains, a polar segment, and an
alanine-rich C terminus. SCAMP2 shares 54% and 56% overall sequence
identity with SCAMP1 and SCAMP3, respectively, and 94% identity with the
mouse homolog. The most divergent regions are in the N terminus.
Northern blot analysis detected a 1.3-kb SCAMP2 transcript, with highest
expression in heart, placenta, and skeletal muscle, intermediate
expression in lung, pancreas, and liver, and low expression in brain and
kidney. Immunofluorescent localization in HeLa cells showed punctate
staining with some perinuclear and peripheral enrichment, and partial
colocalization with SCAMP1 and SCAMP3.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SCAMP2
gene to chromosome 15 (TMAP sts-W74766).
*FIELD* RF
1. Singleton, D. R.; Wu, T. T.; Castle, J. D.: Three mammalian SCAMPs
(secretory carrier membrane proteins) are highly related products
of distinct genes having similar subcellular distributions. J. Cell
Sci. 110: 2099-2107, 1997.
*FIELD* CD
Patricia A. Hartz: 5/7/2002
*FIELD* ED
carol: 05/08/2002
*RECORD*
*FIELD* NO
606912
*FIELD* TI
*606912 SECRETORY CARRIER MEMBRANE PROTEIN 2; SCAMP2
*FIELD* TX
CLONING
Singleton et al. (1997) amplified SCAMP2 by PCR using primers designed
read morefrom SCAMP1 (606911). They cloned the full-length SCAMP2 cDNA from a
HeLa cell cDNA library. They also identified SCAMP3 (606913) as another
paralog in the HeLa cell library. SCAMP2 encodes a deduced 329-amino
acid protein with a calculated molecular mass of 36.6 kD. The protein
shares structural features with SCAMP1 and SCAMP3, including a leucine
zipper-like segment, a proline-rich element, an extended central core
that includes 4 putative transmembrane domains, a polar segment, and an
alanine-rich C terminus. SCAMP2 shares 54% and 56% overall sequence
identity with SCAMP1 and SCAMP3, respectively, and 94% identity with the
mouse homolog. The most divergent regions are in the N terminus.
Northern blot analysis detected a 1.3-kb SCAMP2 transcript, with highest
expression in heart, placenta, and skeletal muscle, intermediate
expression in lung, pancreas, and liver, and low expression in brain and
kidney. Immunofluorescent localization in HeLa cells showed punctate
staining with some perinuclear and peripheral enrichment, and partial
colocalization with SCAMP1 and SCAMP3.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the SCAMP2
gene to chromosome 15 (TMAP sts-W74766).
*FIELD* RF
1. Singleton, D. R.; Wu, T. T.; Castle, J. D.: Three mammalian SCAMPs
(secretory carrier membrane proteins) are highly related products
of distinct genes having similar subcellular distributions. J. Cell
Sci. 110: 2099-2107, 1997.
*FIELD* CD
Patricia A. Hartz: 5/7/2002
*FIELD* ED
carol: 05/08/2002