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Secretory carrier-associated membrane protein 3 (Secretory carrier membrane protein 3)

 SCAM3_HUMAN             Reviewed;         347 AA.
O14828; A9Z1W6; B1AVS6; O15128; Q96FR8; Q9BPY0;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 3.
20-JUN-2018, entry version 173.
RecName: Full=Secretory carrier-associated membrane protein 3;
Short=Secretory carrier membrane protein 3;
Name=SCAMP3; Synonyms=C1orf3, PROPIN1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ARG-38;
ALA-235; ASN-239 AND ASP-242.
TISSUE=Brain;
PubMed=9331372;
Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.;
"Identification of three additional genes contiguous to the
glucocerebrosidase locus on chromosome 1q21: implications for Gaucher
disease.";
Genome Res. 7:1020-1026(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9378760;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Cervix, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-76, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
UBIQUITINATION, INTERACTION WITH NEDD4; NEDD4L AND TSG101, AND
MUTAGENESIS OF PRO-67.
PubMed=19158374; DOI=10.1091/mbc.E08-09-0894;
Aoh Q.L., Castle A.M., Hubbard C.H., Katsumata O., Castle J.D.;
"SCAMP3 negatively regulates epidermal growth factor receptor
degradation and promotes receptor recycling.";
Mol. Biol. Cell 20:1816-1832(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
INTERACTION WITH RNF126.
PubMed=23418353; DOI=10.1242/jcs.116129;
Smith C.J., Berry D.M., McGlade C.J.;
"The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal
sorting of the epidermal growth factor receptor.";
J. Cell Sci. 126:1366-1380(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; THR-37; SER-72 AND
SER-85, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-76, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-313, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
recycling carrier to the cell surface.
-!- SUBUNIT: Interacts with NEDD4, NEDD4L and TSG101. Interacts with
RNF126. {ECO:0000269|PubMed:19158374,
ECO:0000269|PubMed:23418353}.
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O14828-1; Sequence=Displayed;
Name=2;
IsoId=O14828-2; Sequence=VSP_004381;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
heart and skeletal muscle.
-!- PTM: Monoubiquitinated.
-!- SIMILARITY: Belongs to the SCAMP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF023268; AAC51821.1; -; Genomic_DNA.
EMBL; AF005039; AAB62724.1; -; mRNA.
EMBL; AL713999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53090.1; -; Genomic_DNA.
EMBL; CH471121; EAW53092.1; -; Genomic_DNA.
EMBL; BC000161; AAH00161.1; -; mRNA.
EMBL; BC005135; AAH05135.1; -; mRNA.
EMBL; BC010505; AAH10505.1; -; mRNA.
CCDS; CCDS1105.1; -. [O14828-1]
CCDS; CCDS1106.1; -. [O14828-2]
PIR; T08826; T08826.
RefSeq; NP_005689.2; NM_005698.3. [O14828-1]
RefSeq; NP_443069.1; NM_052837.2. [O14828-2]
UniGene; Hs.200600; -.
ProteinModelPortal; O14828; -.
SMR; O14828; -.
BioGrid; 115378; 64.
CORUM; O14828; -.
ELM; O14828; -.
IntAct; O14828; 46.
MINT; O14828; -.
STRING; 9606.ENSP00000307275; -.
TCDB; 8.A.103.1.3; the secretory carrier-associated membrane protein (scamp) family.
iPTMnet; O14828; -.
PhosphoSitePlus; O14828; -.
SwissPalm; O14828; -.
BioMuta; SCAMP3; -.
EPD; O14828; -.
MaxQB; O14828; -.
PaxDb; O14828; -.
PeptideAtlas; O14828; -.
PRIDE; O14828; -.
ProteomicsDB; 48259; -.
ProteomicsDB; 48260; -. [O14828-2]
DNASU; 10067; -.
Ensembl; ENST00000302631; ENSP00000307275; ENSG00000116521. [O14828-1]
Ensembl; ENST00000355379; ENSP00000347540; ENSG00000116521. [O14828-2]
Ensembl; ENST00000570831; ENSP00000461521; ENSG00000263290. [O14828-1]
Ensembl; ENST00000573013; ENSP00000458542; ENSG00000263290. [O14828-2]
GeneID; 10067; -.
KEGG; hsa:10067; -.
UCSC; uc001fjs.4; human. [O14828-1]
CTD; 10067; -.
DisGeNET; 10067; -.
EuPathDB; HostDB:ENSG00000116521.10; -.
GeneCards; SCAMP3; -.
HGNC; HGNC:10565; SCAMP3.
HPA; HPA071167; -.
MIM; 606913; gene.
neXtProt; NX_O14828; -.
OpenTargets; ENSG00000116521; -.
PharmGKB; PA34978; -.
eggNOG; KOG3088; Eukaryota.
eggNOG; ENOG410XSJN; LUCA.
GeneTree; ENSGT00390000014393; -.
HOGENOM; HOG000294221; -.
HOVERGEN; HBG071938; -.
InParanoid; O14828; -.
KO; K19995; -.
OMA; WILLFTP; -.
OrthoDB; EOG091G0ID2; -.
PhylomeDB; O14828; -.
TreeFam; TF313797; -.
SIGNOR; O14828; -.
ChiTaRS; SCAMP3; human.
GeneWiki; SCAMP3; -.
GenomeRNAi; 10067; -.
PMAP-CutDB; O14828; -.
PRO; PR:O14828; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116521; -.
CleanEx; HS_SCAMP3; -.
Genevisible; O14828; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR007273; SCAMP.
PANTHER; PTHR10687; PTHR10687; 1.
Pfam; PF04144; SCAMP; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Isopeptide bond; Membrane;
Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 347 Secretory carrier-associated membrane
protein 3.
/FTId=PRO_0000191257.
TOPO_DOM 1 170 Cytoplasmic. {ECO:0000255}.
TRANSMEM 171 191 Helical. {ECO:0000255}.
TRANSMEM 197 217 Helical. {ECO:0000255}.
TRANSMEM 247 267 Helical. {ECO:0000255}.
TRANSMEM 277 297 Helical. {ECO:0000255}.
TOPO_DOM 298 347 Cytoplasmic. {ECO:0000255}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 37 37 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 41 41 Phosphotyrosine.
{ECO:0000244|PubMed:15144186}.
MOD_RES 53 53 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 83 83 Phosphotyrosine.
{ECO:0000250|UniProtKB:O35609}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
CROSSLNK 313 313 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
VAR_SEQ 23 48 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_004381.
VARIANT 38 38 L -> R (in dbSNP:rs760073).
{ECO:0000269|PubMed:9331372}.
/FTId=VAR_011885.
VARIANT 235 235 V -> A (in dbSNP:rs1318328).
{ECO:0000269|PubMed:9331372}.
/FTId=VAR_011886.
VARIANT 239 239 I -> N (in dbSNP:rs909106).
{ECO:0000269|PubMed:9331372}.
/FTId=VAR_011887.
VARIANT 242 242 V -> D (in dbSNP:rs909107).
{ECO:0000269|PubMed:9331372}.
/FTId=VAR_011888.
MUTAGEN 67 67 P->L: Abolishes interaction with TSG101.
{ECO:0000269|PubMed:19158374}.
CONFLICT 3 3 Q -> R (in Ref. 2; AAB62724).
{ECO:0000305}.
CONFLICT 74 74 K -> M (in Ref. 2; AAB62724).
{ECO:0000305}.
CONFLICT 331 331 A -> R (in Ref. 1; AAC51821).
{ECO:0000305}.
SEQUENCE 347 AA; 38287 MW; D5B0870C66B84F9F CRC64;
MAQSRDGGNP FAEPSELDNP FQDPAVIQHR PSRQYATLDV YNPFETREPP PAYEPPAPAP
LPPPSAPSLQ PSRKLSPTEP KNYGSYSTQA SAAAATAELL KKQEELNRKA EELDRREREL
QHAALGGTAT RQNNWPPLPS FCPVQPCFFQ DISMEIPQEF QKTVSTMYYL WMCSTLALLL
NFLACLASFC VETNNGAGFG LSILWVLLFT PCSFVCWYRP MYKAFRSDSS FNFFVFFFIF
FVQDVLFVLQ AIGIPGWGFS GWISALVVPK GNTAVSVLML LVALLFTGIA VLGIVMLKRI
HSLYRRTGAS FQKAQQEFAA GVFSNPAVRT AAANAAAGAA ENAFRAP


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