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Transport and Golgi organization protein 1 homolog (TANGO1) (C219-reactive peptide) (D320) (Melanoma inhibitory activity protein 3)

 TGO1_HUMAN              Reviewed;        1907 AA.
Q5JRA6; A8K2S0; A8MT05; A8MT13; B7Z430; Q14083; Q3S4X3; Q5JRA5;
Q5JRB0; Q5JRB1; Q5JRB2; Q6UVY8; Q86Y60; Q8N8M5; Q92580;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
05-DEC-2018, entry version 131.
RecName: Full=Transport and Golgi organization protein 1 homolog {ECO:0000305};
Short=TANGO1 {ECO:0000303|PubMed:19269366};
AltName: Full=C219-reactive peptide {ECO:0000303|PubMed:7758977};
AltName: Full=D320 {ECO:0000303|PubMed:7758977};
AltName: Full=Melanoma inhibitory activity protein 3 {ECO:0000312|HGNC:HGNC:24008};
Flags: Precursor;
Name=MIA3 {ECO:0000312|HGNC:HGNC:24008};
Synonyms=KIAA0268 {ECO:0000312|EMBL:BAA13448.1},
TANGO {ECO:0000303|PubMed:15183315}; ORFNames=UNQ6077/PRO20088;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
GLU-482.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 419-1492 (ISOFORM 2).
TISSUE=Brain, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[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 [MRNA] OF 1-125, AND TISSUE SPECIFICITY.
PubMed=15183315; DOI=10.1016/j.modgep.2003.12.002;
Bosserhoff A.K., Moser M., Buettner R.;
"Characterization and expression pattern of the novel MIA homolog
TANGO.";
Gene Expr. Patterns 4:473-479(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 715-1907 (ISOFORM 1), AND
VARIANT GLY-881.
TISSUE=Bone marrow;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1306-1441.
TISSUE=Leukemia;
PubMed=7758977; DOI=10.1016/0378-1119(94)00541-Y;
Norris M.D., Gilbert J., Madafiglio J., Haber M.;
"Analysis of a novel cDNA encoding a C219-reactive peptide isolated
from methotrexate-selected multidrug-resistant human leukemic cells.";
Gene 156:313-314(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1441-1907 (ISOFORM 1), AND
VARIANTS CYS-1659 AND GLU-1723.
TISSUE=Brain;
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).
[8]
TISSUE SPECIFICITY.
PubMed=17044017; DOI=10.1002/ijc.22242;
Arndt S., Bosserhoff A.K.;
"TANGO is a tumor suppressor of malignant melanoma.";
Int. J. Cancer 119:2812-2820(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1906, 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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[11]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COL7A1; SEC23A AND
SEC24C, TOPOLOGY, DOMAIN, AND REGION.
PubMed=19269366; DOI=10.1016/j.cell.2008.12.025;
Saito K., Chen M., Bard F., Chen S., Zhou H., Woodley D.,
Polischuk R., Schekman R., Malhotra V.;
"TANGO1 facilitates cargo loading at endoplasmic reticulum exit
sites.";
Cell 136:891-902(2009).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-589.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
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).
[14]
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).
[15]
INTERACTION WITH CTAGE5, SUBCELLULAR LOCATION, AND REGION.
PubMed=21525241; DOI=10.1091/mbc.E11-02-0143;
Saito K., Yamashiro K., Ichikawa Y., Erlmann P., Kontani K.,
Malhotra V., Katada T.;
"cTAGE5 mediates collagen secretion through interaction with TANGO1 at
endoplasmic reticulum exit sites.";
Mol. Biol. Cell 22:2301-2308(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1745, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1706, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727; SER-876; SER-1067;
SER-1706 AND SER-1906, 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).
[19]
PHOSPHORYLATION AT SER-226; SER-229 AND SER-1906.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[20]
FUNCTION, AND INTERACTION WITH APOB AND MIA2.
PubMed=27138255; DOI=10.1083/jcb.201603072;
Santos A.J., Nogueira C., Ortega-Bellido M., Malhotra V.;
"TANGO1 and Mia2/cTAGE5 (TALI) cooperate to export bulky pre-
chylomicrons/VLDLs from the endoplasmic reticulum.";
J. Cell Biol. 213:343-354(2016).
[21]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SEC16A AND SEC23A,
AND REGION SIR.
PubMed=28442536; DOI=10.1083/jcb.201703084;
Maeda M., Katada T., Saito K.;
"TANGO1 recruits Sec16 to coordinately organize ER exit sites for
efficient secretion.";
J. Cell Biol. 216:1731-1743(2017).
[22] {ECO:0000244|PDB:5KYN, ECO:0000244|PDB:5KYU, ECO:0000244|PDB:5KYW}
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1796-1808 IN COMPLEX WITH
SEC23A, INTERACTION WITH SEC23A AND SEC23B, DOMAIN, AND REGION.
PubMed=27551091; DOI=10.1073/pnas.1605916113;
Ma W., Goldberg J.;
"TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large
COPII coats.";
Proc. Natl. Acad. Sci. U.S.A. 113:10061-10066(2016).
-!- FUNCTION: Plays a role in the transport of cargos that are too
large to fit into COPII-coated vesicles and require specific
mechanisms to be incorporated into membrane-bound carriers and
exported from the endoplasmic reticulum. This protein is required
for collagen VII (COL7A1) secretion by loading COL7A1 into
transport carriers. It may participate in cargo loading of COL7A1
at endoplasmic reticulum exit sites by binding to COPII coat
subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing
carrier. Does not play a role in global protein secretion and is
apparently specific to COL7A1 cargo loading. However, it may
participate in secretion of other proteins in cells that do not
secrete COL7A1. It is also specifically required for the secretion
of lipoproteins by participating in their export from the
endoplasmic reticulum (PubMed:27138255, PubMed:19269366). Required
for correct assembly of COPII coat components at endoplasmic
reticulum exit sites (ERES) and for the localization of SEC16A and
membrane-bound ER-resident complexes consisting of CTAGE5 and
PREB/SEC12 to ERES (PubMed:28442536).
{ECO:0000269|PubMed:19269366, ECO:0000269|PubMed:27138255,
ECO:0000269|PubMed:28442536}.
-!- SUBUNIT: Interacts with CTAGE5 (PubMed:21525241). Interacts (via
SH3 domain) with COL7A1 (PubMed:19269366). Interacts with the
COPII coat subunits SEC23A, SEC23B and maybe SEC24C
(PubMed:19269366, PubMed:27551091, PubMed:28442536). May interact
with APOB and MIA2 (PubMed:27138255). Isoform 1 and isoform 4
interact with SEC16A (PubMed:28442536).
{ECO:0000269|PubMed:19269366, ECO:0000269|PubMed:21525241,
ECO:0000269|PubMed:27138255, ECO:0000269|PubMed:27551091,
ECO:0000269|PubMed:28442536}.
-!- INTERACTION:
Q53EZ4:CEP55; NbExp=4; IntAct=EBI-10244342, EBI-747776;
Q02388:COL7A1; NbExp=2; IntAct=EBI-2291868, EBI-724237;
P51116:FXR2; NbExp=3; IntAct=EBI-10244342, EBI-740459;
Q9GZV8:PRDM14; NbExp=3; IntAct=EBI-10244342, EBI-3957793;
P14373:TRIM27; NbExp=3; IntAct=EBI-10244342, EBI-719493;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:19269366, ECO:0000269|PubMed:21525241};
Single-pass membrane protein {ECO:0000269|PubMed:19269366}.
Note=Localizes at endoplasmic reticulum exit sites (ERES), also
known as transitional endoplasmic reticulum (tER). SEC16A is
required for its proper localization to ERES. After loading of
COL7A1 into transport carriers, it is not incorporated into COPII
carriers and remains in the endoplasmic reticulum membrane.
{ECO:0000269|PubMed:19269366, ECO:0000269|PubMed:21525241,
ECO:0000269|PubMed:28442536}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=TANGO1L {ECO:0000303|PubMed:28442536};
IsoId=Q5JRA6-1; Sequence=Displayed;
Name=2;
IsoId=Q5JRA6-2; Sequence=VSP_025864;
Name=3;
IsoId=Q5JRA6-3; Sequence=VSP_025861, VSP_025862;
Name=4; Synonyms=TANGO1S {ECO:0000303|PubMed:28442536};
IsoId=Q5JRA6-4; Sequence=VSP_025860, VSP_025863;
-!- TISSUE SPECIFICITY: Broadly expressed, except in bone marrow and
peripheral blood mononuclear cells. Down-regulated in melanoma
tissue. {ECO:0000269|PubMed:15183315,
ECO:0000269|PubMed:17044017}.
-!- DOMAIN: The proline-rich domain (PRD) contains repeated PPP
motifs. A single PPP motif is necessary and sufficient to mediate
interaction with the COPII coat subunits SEC23A and SEC23B.
{ECO:0000269|PubMed:19269366, ECO:0000269|PubMed:27551091}.
-!- DOMAIN: Although 2 transmembrane domains are predicted,
PubMed:19269366 showed that it only contains one transmembrane
domain. The other predicted transmembrane region is probably a
hairpin-type region embedded into the membrane, which does not
cross the membrane. It is unclear which of the 2 predicted
transmembrane regions is the transmembrane or the hairpin-type
region. {ECO:0000269|PubMed:19269366}.
-!- SIMILARITY: Belongs to the MIA/OTOR family. Tango1 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC04810.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAF83024.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY359091; AAQ89449.1; -; mRNA.
EMBL; AK096526; BAC04810.1; ALT_INIT; mRNA.
EMBL; AK290335; BAF83024.1; ALT_INIT; mRNA.
EMBL; AK296712; BAH12416.1; -; mRNA.
EMBL; AL592148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D87742; BAA13448.1; -; mRNA.
EMBL; L34688; AAB00324.1; -; mRNA.
EMBL; DQ166034; AAZ95512.1; -; mRNA.
EMBL; BC047116; AAH47116.2; -; mRNA.
CCDS; CCDS41470.1; -. [Q5JRA6-1]
CCDS; CCDS73035.1; -. [Q5JRA6-4]
RefSeq; NP_001287796.1; NM_001300867.1. [Q5JRA6-4]
RefSeq; NP_001310992.1; NM_001324063.1. [Q5JRA6-2]
RefSeq; NP_940953.2; NM_198551.3. [Q5JRA6-1]
UniGene; Hs.118474; -.
PDB; 5KYN; X-ray; 2.55 A; C=1796-1803.
PDB; 5KYU; X-ray; 3.51 A; C=1796-1803.
PDB; 5KYW; X-ray; 3.20 A; C=1800-1808.
PDBsum; 5KYN; -.
PDBsum; 5KYU; -.
PDBsum; 5KYW; -.
ProteinModelPortal; Q5JRA6; -.
SMR; Q5JRA6; -.
BioGrid; 131952; 51.
CORUM; Q5JRA6; -.
IntAct; Q5JRA6; 27.
STRING; 9606.ENSP00000340900; -.
TCDB; 9.B.113.1.2; the collagen secretory protein, mia3 (mia3) family.
GlyConnect; 1498; -.
iPTMnet; Q5JRA6; -.
PhosphoSitePlus; Q5JRA6; -.
BioMuta; MIA3; -.
DMDM; 74741823; -.
EPD; Q5JRA6; -.
MaxQB; Q5JRA6; -.
PaxDb; Q5JRA6; -.
PeptideAtlas; Q5JRA6; -.
PRIDE; Q5JRA6; -.
ProteomicsDB; 63078; -.
ProteomicsDB; 63079; -. [Q5JRA6-2]
ProteomicsDB; 63080; -. [Q5JRA6-3]
ProteomicsDB; 63081; -. [Q5JRA6-4]
Ensembl; ENST00000340535; ENSP00000345866; ENSG00000154305. [Q5JRA6-4]
Ensembl; ENST00000344507; ENSP00000341348; ENSG00000154305. [Q5JRA6-3]
Ensembl; ENST00000344922; ENSP00000340900; ENSG00000154305. [Q5JRA6-1]
GeneID; 375056; -.
KEGG; hsa:375056; -.
UCSC; uc001hnl.4; human. [Q5JRA6-1]
CTD; 375056; -.
DisGeNET; 375056; -.
EuPathDB; HostDB:ENSG00000154305.16; -.
GeneCards; MIA3; -.
H-InvDB; HIX0001613; -.
HGNC; HGNC:24008; MIA3.
HPA; HPA055922; -.
HPA; HPA056816; -.
MIM; 613455; gene.
neXtProt; NX_Q5JRA6; -.
OpenTargets; ENSG00000154305; -.
PharmGKB; PA143485536; -.
eggNOG; ENOG410IFUG; Eukaryota.
eggNOG; ENOG410YVAS; LUCA.
GeneTree; ENSGT00940000154238; -.
HOVERGEN; HBG108133; -.
InParanoid; Q5JRA6; -.
OMA; FGPGMRP; -.
OrthoDB; EOG091G0PEA; -.
PhylomeDB; Q5JRA6; -.
TreeFam; TF333137; -.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
ChiTaRS; MIA3; human.
GenomeRNAi; 375056; -.
PMAP-CutDB; Q5JRA6; -.
PRO; PR:Q5JRA6; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000154305; Expressed in 217 organ(s), highest expression level in stomach.
CleanEx; HS_MIA3; -.
ExpressionAtlas; Q5JRA6; baseline and differential.
Genevisible; Q5JRA6; HS.
GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0042954; F:lipoprotein transporter activity; IMP:UniProtKB.
GO; GO:0090110; P:cargo loading into COPII-coated vesicle; IMP:UniProtKB.
GO; GO:0035459; P:cargo loading into vesicle; IBA:GO_Central.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; IMP:BHF-UCL.
GO; GO:0007029; P:endoplasmic reticulum organization; IMP:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:UniProtKB.
GO; GO:0006887; P:exocytosis; IMP:UniProtKB.
GO; GO:0042953; P:lipoprotein transport; IMP:UniProtKB.
GO; GO:0007162; P:negative regulation of cell adhesion; IDA:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; IDA:BHF-UCL.
GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; IMP:BHF-UCL.
GO; GO:2000402; P:negative regulation of lymphocyte migration; IMP:BHF-UCL.
GO; GO:0002687; P:positive regulation of leukocyte migration; IDA:BHF-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IMP:UniProtKB.
GO; GO:0009306; P:protein secretion; IBA:GO_Central.
GO; GO:0015031; P:protein transport; IMP:UniProtKB.
GO; GO:0042060; P:wound healing; IDA:BHF-UCL.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF07653; SH3_2; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Endoplasmic reticulum; ER-Golgi transport; Exocytosis; Glycoprotein;
Membrane; Methylation; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; SH3 domain; Signal;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 1907 Transport and Golgi organization protein
1 homolog.
/FTId=PRO_0000288998.
TOPO_DOM 23 1144 Lumenal. {ECO:0000255}.
INTRAMEM 1145 1165 {ECO:0000255}.
TOPO_DOM 1166 1176 Lumenal. {ECO:0000255}.
TRANSMEM 1177 1197 Helical. {ECO:0000255}.
TOPO_DOM 1198 1907 Cytoplasmic. {ECO:0000255}.
DOMAIN 45 107 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 1211 1650 Mediates interaction with CTAGE5.
{ECO:0000269|PubMed:21525241}.
REGION 1751 1907 Proline-rich domain (PRD); mediates
interaction with the COPII coat subunits
SEC23A and SEC23B.
{ECO:0000269|PubMed:19269366,
ECO:0000269|PubMed:27551091,
ECO:0000269|PubMed:28442536}.
REGION 1788 1847 SEC16A-interacting region (SIR); required
for its localization to endoplasmic
reticulum exit sites and for its
interaction with SEC16A.
{ECO:0000269|PubMed:28442536}.
COILED 471 531 {ECO:0000255}.
COILED 1214 1396 {ECO:0000255}.
COILED 1487 1639 {ECO:0000255}.
COMPBIAS 1640 1890 Pro-rich.
MOD_RES 226 226 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 229 229 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 876 876 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1067 1067 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1431 1431 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BI84}.
MOD_RES 1666 1666 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BI84}.
MOD_RES 1678 1678 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BI84}.
MOD_RES 1706 1706 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1727 1727 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BI84}.
MOD_RES 1741 1741 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BI84}.
MOD_RES 1745 1745 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1784 1784 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8BI84}.
MOD_RES 1892 1892 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BI84}.
MOD_RES 1906 1906 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 589 589 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VAR_SEQ 1 1122 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_025860.
VAR_SEQ 493 500 MTVHSSVH -> FKTEPIKL (in isoform 3).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_025861.
VAR_SEQ 501 1907 Missing (in isoform 3).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_025862.
VAR_SEQ 1123 1159 IDANKQPETAAEEPASVTPLENAILLIYSFMFYLTKS ->
MDSVPATVPSIAATPGDPELVGPLSVLYAAFIAKLLE (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_025863.
VAR_SEQ 1304 1362 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_025864.
VARIANT 482 482 K -> E (in dbSNP:rs2936053).
{ECO:0000269|PubMed:12975309}.
/FTId=VAR_032546.
VARIANT 605 605 K -> R (in dbSNP:rs2936052).
/FTId=VAR_032547.
VARIANT 881 881 E -> G (in dbSNP:rs2936051).
{ECO:0000269|PubMed:9039502}.
/FTId=VAR_032548.
VARIANT 1659 1659 G -> C (in dbSNP:rs17857325).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_032549.
VARIANT 1723 1723 K -> E (in dbSNP:rs17854428).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_032550.
CONFLICT 46 46 Missing (in Ref. 1; AAQ89449).
{ECO:0000305}.
CONFLICT 1032 1032 H -> R (in Ref. 2; BAC04810).
{ECO:0000305}.
CONFLICT 1443 1443 R -> Q (in Ref. 7; AAH47116).
{ECO:0000305}.
CONFLICT 1754 1754 K -> R (in Ref. 2; BAH12416).
{ECO:0000305}.
SEQUENCE 1907 AA; 213702 MW; D19C9AF1656F4B1C CRC64;
MAAAPGLLVW LLVLRLPWRV PGQLDPSTGR RFSEHKLCAD DECSMLMYRG EALEDFTGPD
CRFVNFKKGD PVYVYYKLAR GWPEVWAGSV GRTFGYFPKD LIQVVHEYTK EELQVPTDET
DFVCFDGGRD DFHNYNVEEL LGFLELYNSA ATDSEKAVEK TLQDMEKNPE LSKEREPEPE
PVEANSEESD SVFSENTEDL QEQFTTQKHH SHANSQANHA QGEQASFESF EEMLQDKLKV
PESENNKTSN SSQVSNEQDK IDAYKLLKKE MTLDLKTKFG STADALVSDD ETTRLVTSLE
DDFDEELDTE YYAVGKEDEE NQEDFDELPL LTFTDGEDMK TPAKSGVEKY PTDKEQNSNE
EDKVQLTVPP GIKNDDKNIL TTWGDTIFSI VTGGEETRDT MDLESSSSEE EKEDDDDALV
PDSKQGKPQS ATDYSDPDNV DDGLFIVDIP KTNNDKEVNA EHHIKGKGRG VQESKRGLVQ
DKTELEDENQ EGMTVHSSVH SNNLNSMPAA EKGKDTLKSA YDDTENDLKG AAIHISKGML
HEEKPGEQIL EGGSESESAQ KAAGNQMNDR KIQQESLGSA PLMGDDHPNA SRDSVEGDAL
VNGAKLHTLS VEHQREELKE ELVLKTQNQP RFSSPDEIDL PRELEDEVPI LGRNLPWQQE
RDVAATASKQ MSEKIRLSEG EAKEDSLDEE FFHHKAMQGT EVGQTDQTDS TGGPAFLSKV
EEDDYPSEEL LEDENAINAK RSKEKNPGNQ GRQFDVNLQV PDRAVLGTIH PDPEIEESKQ
ETSMILDSEK TSETAAKGVN TGGREPNTMV EKERPLADKK AQRPFERSDF SDSIKIQTPE
LGEVFQNKDS DYLKNDNPEE HLKTSGLAGE PEGELSKEDH ENTEKYMGTE SQGSAAAEPE
DDSFHWTPHT SVEPGHSDKR EDLLIISSFF KEQQSLQRFQ KYFNVHELEA LLQEMSSKLK
SAQQESLPYN MEKVLDKVFR ASESQILSIA EKMLDTRVAE NRDLGMNENN IFEEAAVLDD
IQDLIYFVRY KHSTAEETAT LVMAPPLEEG LGGAMEEMQP LHEDNFSREK TAELNVQVPE
EPTHLDQRVI GDTHASEVSQ KPNTEKDLDP GPVTTEDTPM DAIDANKQPE TAAEEPASVT
PLENAILLIY SFMFYLTKSL VATLPDDVQP GPDFYGLPWK PVFITAFLGI ASFAIFLWRT
VLVVKDRVYQ VTEQQISEKL KTIMKENTEL VQKLSNYEQK IKESKKHVQE TRKQNMILSD
EAIKYKDKIK TLEKNQEILD DTAKNLRVML ESEREQNVKN QDLISENKKS IEKLKDVISM
NASEFSEVQI ALNEAKLSEE KVKSECHRVQ EENARLKKKK EQLQQEIEDW SKLHAELSEQ
IKSFEKSQKD LEVALTHKDD NINALTNCIT QLNLLECESE SEGQNKGGND SDELANGEVG
GDRNEKMKNQ IKQMMDVSRT QTAISVVEED LKLLQLKLRA SVSTKCNLED QVKKLEDDRN
SLQAAKAGLE DECKTLRQKV EILNELYQQK EMALQKKLSQ EEYERQEREH RLSAADEKAV
SAAEEVKTYK RRIEEMEDEL QKTERSFKNQ IATHEKKAHE NWLKARAAER AIAEEKREAA
NLRHKLLELT QKMAMLQEEP VIVKPMPGKP NTQNPPRRGP LSQNGSFGPS PVSGGECSPP
LTVEPPVRPL SATLNRRDMP RSEFGSVDGP LPHPRWSAEA SGKPSPSDPG SGTATMMNSS
SRGSSPTRVL DEGKVNMAPK GPPPFPGVPL MSTPMGGPVP PPIRYGPPPQ LCGPFGPRPL
PPPFGPGMRP PLGLREFAPG VPPGRRDLPL HPRGFLPGHA PFRPLGSLGP REYFIPGTRL
PPPTHGPQEY PPPPAVRDLL PSGSRDEPPP ASQSTSQDCS QALKQSP


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