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Protein OS-9 (Amplified in osteosarcoma 9)

 OS9_HUMAN               Reviewed;         667 AA.
Q13438; A6NDD1; A6NFR7; A6NLB2; A8K5Q9; B4DE28; B4DPX1; B4E1I6;
E7ENT8; E7EW91; F8VUH2; G3XA88; O00579; Q6IBL2; Q8IZ58; Q9BW99;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 156.
RecName: Full=Protein OS-9;
AltName: Full=Amplified in osteosarcoma 9;
Flags: Precursor;
Name=OS9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8634085;
DOI=10.1002/(SICI)1098-2744(199604)15:4<270::AID-MC4>3.0.CO;2-K;
Su Y.A., Hutter C.M., Trent J.M., Meltzer P.S.;
"Complete sequence analysis of a gene (OS-9) ubiquitously expressed in
human tissues and amplified in sarcomas.";
Mol. Carcinog. 15:270-275(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=9498564; DOI=10.1093/oxfordjournals.jbchem.a021880;
Kimura Y., Nakazawa M., Tsuchiya N., Asakawa S., Shimizu N.,
Yamada M.;
"Genomic organization of the OS-9 gene amplified in human sarcomas.";
J. Biochem. 122:1190-1195(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1),
CHARACTERIZATION, AND ALTERNATIVE SPLICING (ISOFORMS 2 AND 3).
TISSUE=Promyelocytic leukemia;
PubMed=9562620; DOI=10.1093/oxfordjournals.jbchem.a022019;
Kimura Y., Nakazawa M., Yamada M.;
"Cloning and characterization of three isoforms of OS-9 cDNA and
expression of the OS-9 gene in various human tumor cell lines.";
J. Biochem. 123:876-882(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4; 5; 6 AND 8),
AND VARIANT ASN-305.
TISSUE=Brain, Tongue, and Trachea;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Muscle;
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-667.
PubMed=9192850; DOI=10.1006/geno.1997.4727;
Elkahloun A.G., Krizman D.B., Wang Z., Hofmann T.A., Roe B.A.,
Meltzer P.S.;
"Transcript mapping in a 46-kb sequenced region at the core of 12q13.3
amplification in human cancers.";
Genomics 42:295-301(1997).
[10]
TISSUE SPECIFICITY.
PubMed=10403379; DOI=10.1016/S0014-5793(99)00700-0;
Nakayama T., Yaoi T., Kuwajima G., Yoshie O., Sakata T.;
"Ca2(+)-dependent interaction of N-copine, a member of the two C2
domain protein family, with OS-9, the product of a gene frequently
amplified in osteosarcoma.";
FEBS Lett. 453:77-80(1999).
[11]
FUNCTION IN TRPV4 MATURATION.
PubMed=17932042; DOI=10.1074/jbc.M703903200;
Wang Y., Fu X., Gaiser S., Koettgen M., Kramer-Zucker A., Walz G.,
Wegierski T.;
"OS-9 regulates the transit and polyubiquitination of TRPV4 in the
endoplasmic reticulum.";
J. Biol. Chem. 282:36561-36570(2007).
[12]
FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR
LOCATION, DISULFIDE BONDS, GLYCOSYLATION, INDUCTION, AND MUTAGENESIS
OF ARG-188.
PubMed=18417469; DOI=10.1074/jbc.M802272200;
Bernasconi R., Pertel T., Luban J., Molinari M.;
"A dual task for the Xbp1-responsive OS-9 variants in the mammalian
endoplasmic reticulum: inhibiting secretion of misfolded protein
conformers and enhancing their disposal.";
J. Biol. Chem. 283:16446-16454(2008).
[13]
INTERACTION WITH ERLEC1; HSPA5; SEL1L AND SYVN1.
PubMed=18502753; DOI=10.1074/jbc.M709336200;
Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K.;
"Human XTP3-B forms an endoplasmic reticulum quality control scaffold
with the HRD1-SEL1L ubiquitin ligase complex and BiP.";
J. Biol. Chem. 283:20914-20924(2008).
[14]
FUNCTION, INTERACTION WITH HSP90B1; SEL1L AND SYVN1, SUBCELLULAR
LOCATION, GLYCOSYLATION, AND MUTAGENESIS OF ARG-188.
PubMed=18264092; DOI=10.1038/ncb1689;
Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R.;
"OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L
ubiquitin ligase complex for ERAD.";
Nat. Cell Biol. 10:272-282(2008).
[15]
FUNCTION AS A LECTIN, AND MUTAGENESIS OF ARG-188.
PubMed=19346256; DOI=10.1074/jbc.M809725200;
Hosokawa N., Kamiya Y., Kamiya D., Kato K., Nagata K.;
"Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-
associated degradation, recognizes mannose-trimmed N-glycans.";
J. Biol. Chem. 284:17061-17068(2009).
[16]
FUNCTION IN MISFOLDED GLYCOPROTEIN UBIQUITINATION, SUBCELLULAR
LOCATION, GLYCOSYLATION, INTERACTION WITH DERL2; HRD1 AND SEL1L, AND
INDUCTION BY ER STRESS.
PubMed=19084021; DOI=10.1016/j.jmb.2008.11.045;
Alcock F., Swanton E.;
"Mammalian OS-9 is upregulated in response to endoplasmic reticulum
stress and facilitates ubiquitination of misfolded glycoproteins.";
J. Mol. Biol. 385:1032-1042(2009).
[17]
INTERACTION WITH CREB3.
PubMed=20546900; DOI=10.1016/j.molimm.2010.04.019;
Eleveld-Trancikova D., Sanecka A., van Hout-Kuijer M.A., Looman M.W.,
Hendriks I.A., Jansen B.J., Adema G.J.;
"DC-STAMP interacts with ER-resident transcription factor LUMAN which
becomes activated during DC maturation.";
Mol. Immunol. 47:1963-1973(2010).
[18]
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]
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).
[20]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 108-229 IN COMPLEX WITH
MANNOPENTAOSE, FUNCTION, AND DISULFIDE BONDS.
PubMed=21172656; DOI=10.1016/j.molcel.2010.11.017;
Satoh T., Chen Y., Hu D., Hanashima S., Yamamoto K., Yamaguchi Y.;
"Structural basis for oligosaccharide recognition of misfolded
glycoproteins by OS-9 in ER-associated degradation.";
Mol. Cell 40:905-916(2010).
-!- FUNCTION: Lectin which functions in endoplasmic reticulum (ER)
quality control and ER-associated degradation (ERAD). May bind
terminally misfolded non-glycosylated proteins as well as
improperly folded glycoproteins, retain them in the ER, and
possibly transfer them to the ubiquitination machinery and promote
their degradation. Possible targets include TRPV4.
{ECO:0000269|PubMed:17932042, ECO:0000269|PubMed:18264092,
ECO:0000269|PubMed:18417469, ECO:0000269|PubMed:19084021,
ECO:0000269|PubMed:19346256, ECO:0000269|PubMed:21172656}.
-!- SUBUNIT: Interacts (via C-terminus) with CPNE6 (via second C2
domain); this interaction occurs in a calcium-dependent manner in
vitro (By similarity). Probably part of the HRD1 ubiquitin ligase
complex composed at least of SYVN1/HRD1 and SEL1L with which it
interacts directly (PubMed:18502753, PubMed:18264092,
PubMed:19084021). Through this complex it may interact with ERLEC1
and HSPA5 (PubMed:18502753). Interacts with DERL2
(PubMed:19084021). Interacts with HSP90B1 (PubMed:18264092).
Interacts with CREB3 (PubMed:20546900). Interacts with SYVN1
(PubMed:18264092). {ECO:0000250|UniProtKB:Q8K2C7,
ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18502753,
ECO:0000269|PubMed:19084021, ECO:0000269|PubMed:20546900}.
-!- INTERACTION:
Q9GZT9:EGLN1; NbExp=4; IntAct=EBI-725454, EBI-1174818;
Q9H6Z9:EGLN3; NbExp=2; IntAct=EBI-725454, EBI-1175354;
O75460-1:ERN1; NbExp=2; IntAct=EBI-725454, EBI-15600828;
Q16665:HIF1A; NbExp=9; IntAct=EBI-725454, EBI-447269;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469,
ECO:0000269|PubMed:19084021}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1; Synonyms=OS-9-1;
IsoId=Q13438-1; Sequence=Displayed;
Note=Major isoform.;
Name=2; Synonyms=OS-9-2;
IsoId=Q13438-2; Sequence=VSP_004353;
Note=Major isoform.;
Name=3; Synonyms=OS-9-3;
IsoId=Q13438-3; Sequence=VSP_004352, VSP_004353;
Name=4;
IsoId=Q13438-4; Sequence=VSP_004352;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q13438-5; Sequence=VSP_044701, VSP_044702, VSP_004353;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q13438-6; Sequence=VSP_046001, VSP_004353;
Note=No experimental confirmation available.;
Name=7;
IsoId=Q13438-7; Sequence=VSP_044702, VSP_004353;
Note=Gene prediction based on EST data.;
Name=8;
IsoId=Q13438-8; Sequence=VSP_046770, VSP_004352, VSP_004353;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Found as well in all
tumor cell lines analyzed, amplified in sarcomas. Highly expressed
in osteosarcoma SJSA-1 and rhabdomyosarcoma Rh30 cell lines.
Isoform 2 is the major isoform detected in all cell types
examined.
-!- INDUCTION: Up-regulated in response to endoplasmic reticulum
stress (at protein level). {ECO:0000269|PubMed:18417469,
ECO:0000269|PubMed:19084021}.
-!- PTM: Intramolecular disulfide bonds.
-!- PTM: Isoform 1 and isoform 2 are N-glycosylated.
{ECO:0000269|PubMed:18264092, ECO:0000269|PubMed:18417469,
ECO:0000269|PubMed:19084021}.
-!- SIMILARITY: Belongs to the OS-9 family. {ECO:0000305}.
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EMBL; U41635; AAB06495.1; -; mRNA.
EMBL; AB002805; BAA24362.1; -; Genomic_DNA.
EMBL; AB002806; BAA24363.1; -; mRNA.
EMBL; AK291374; BAF84063.1; -; mRNA.
EMBL; AK293435; BAG56939.1; -; mRNA.
EMBL; AK296770; BAG59349.1; -; mRNA.
EMBL; AK298532; BAG60733.1; -; mRNA.
EMBL; AK303858; BAG64798.1; -; mRNA.
EMBL; CR456791; CAG33072.1; -; mRNA.
EMBL; AC025165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW97045.1; -; Genomic_DNA.
EMBL; CH471054; EAW97046.1; -; Genomic_DNA.
EMBL; CH471054; EAW97047.1; -; Genomic_DNA.
EMBL; BC000532; AAH00532.1; -; mRNA.
EMBL; BC007254; AAH07254.1; -; mRNA.
EMBL; BC023513; AAH23513.2; -; mRNA.
EMBL; U81031; AAC39523.2; -; Genomic_DNA.
CCDS; CCDS31843.1; -. [Q13438-1]
CCDS; CCDS31844.1; -. [Q13438-2]
CCDS; CCDS31845.1; -. [Q13438-4]
CCDS; CCDS31846.1; -. [Q13438-3]
CCDS; CCDS58246.1; -. [Q13438-6]
CCDS; CCDS58247.1; -. [Q13438-7]
CCDS; CCDS58248.1; -. [Q13438-5]
CCDS; CCDS58249.1; -. [Q13438-8]
PIR; JC5889; JC5889.
RefSeq; NP_001017956.1; NM_001017956.2. [Q13438-2]
RefSeq; NP_001017957.1; NM_001017957.2. [Q13438-3]
RefSeq; NP_001017958.1; NM_001017958.2. [Q13438-4]
RefSeq; NP_001248349.1; NM_001261420.1. [Q13438-7]
RefSeq; NP_001248350.1; NM_001261421.1. [Q13438-5]
RefSeq; NP_001248351.1; NM_001261422.1. [Q13438-6]
RefSeq; NP_001248352.1; NM_001261423.1. [Q13438-8]
RefSeq; NP_006803.1; NM_006812.3. [Q13438-1]
UniGene; Hs.527861; -.
PDB; 3AIH; X-ray; 2.10 A; A/B=108-229.
PDBsum; 3AIH; -.
ProteinModelPortal; Q13438; -.
SMR; Q13438; -.
BioGrid; 116156; 134.
CORUM; Q13438; -.
DIP; DIP-37493N; -.
IntAct; Q13438; 36.
MINT; MINT-1187753; -.
STRING; 9606.ENSP00000318165; -.
TCDB; 8.A.67.1.1; the os-9 quality control (erad) protein (os-9) family.
iPTMnet; Q13438; -.
PhosphoSitePlus; Q13438; -.
BioMuta; OS9; -.
DMDM; 3024310; -.
EPD; Q13438; -.
MaxQB; Q13438; -.
PaxDb; Q13438; -.
PeptideAtlas; Q13438; -.
PRIDE; Q13438; -.
DNASU; 10956; -.
Ensembl; ENST00000257966; ENSP00000257966; ENSG00000135506. [Q13438-7]
Ensembl; ENST00000315970; ENSP00000318165; ENSG00000135506. [Q13438-1]
Ensembl; ENST00000389142; ENSP00000373794; ENSG00000135506. [Q13438-3]
Ensembl; ENST00000389146; ENSP00000373798; ENSG00000135506. [Q13438-4]
Ensembl; ENST00000435406; ENSP00000389632; ENSG00000135506. [Q13438-6]
Ensembl; ENST00000439210; ENSP00000407360; ENSG00000135506. [Q13438-8]
Ensembl; ENST00000551035; ENSP00000447866; ENSG00000135506. [Q13438-5]
Ensembl; ENST00000552285; ENSP00000450010; ENSG00000135506. [Q13438-2]
GeneID; 10956; -.
KEGG; hsa:10956; -.
UCSC; uc001spj.4; human. [Q13438-1]
CTD; 10956; -.
DisGeNET; 10956; -.
EuPathDB; HostDB:ENSG00000135506.15; -.
GeneCards; OS9; -.
HGNC; HGNC:16994; OS9.
HPA; CAB011518; -.
HPA; HPA013694; -.
MIM; 609677; gene.
neXtProt; NX_Q13438; -.
OpenTargets; ENSG00000135506; -.
PharmGKB; PA164724245; -.
eggNOG; KOG3394; Eukaryota.
eggNOG; ENOG410XR8A; LUCA.
GeneTree; ENSGT00530000063603; -.
HOGENOM; HOG000293348; -.
HOVERGEN; HBG000974; -.
InParanoid; Q13438; -.
KO; K10088; -.
OMA; RYHSQTY; -.
OrthoDB; EOG091G02WQ; -.
PhylomeDB; Q13438; -.
TreeFam; TF314309; -.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
ChiTaRS; OS9; human.
EvolutionaryTrace; Q13438; -.
GeneWiki; OS9_(gene); -.
GenomeRNAi; 10956; -.
PRO; PR:Q13438; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000135506; -.
ExpressionAtlas; Q13438; baseline and differential.
Genevisible; Q13438; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; NAS:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
GO; GO:0006621; P:protein retention in ER lumen; IDA:UniProtKB.
GO; GO:0006605; P:protein targeting; IEA:Ensembl.
GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
Gene3D; 2.70.130.10; -; 1.
InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
InterPro; IPR012913; OS9-like.
Pfam; PF07915; PRKCSH; 1.
SUPFAM; SSF50911; SSF50911; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Lectin; Polymorphism;
Reference proteome; Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 667 Protein OS-9.
/FTId=PRO_0000021951.
DOMAIN 108 178 PRKCSH.
COMPBIAS 414 429 Asp/Glu-rich (acidic).
BINDING 130 130 Carbohydrate.
BINDING 182 182 Carbohydrate.
BINDING 188 188 Carbohydrate.
BINDING 212 212 Carbohydrate.
BINDING 218 218 Carbohydrate.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 110 123
DISULFID 181 216
DISULFID 196 228
VAR_SEQ 55 113 Missing (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046770.
VAR_SEQ 142 193 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046001.
VAR_SEQ 161 193 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044701.
VAR_SEQ 263 263 A -> AV (in isoform 5 and isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044702.
VAR_SEQ 456 470 Missing (in isoform 3, isoform 4 and
isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_004352.
VAR_SEQ 534 588 Missing (in isoform 2, isoform 3, isoform
5, isoform 6, isoform 7 and isoform 8).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.5}.
/FTId=VSP_004353.
VARIANT 305 305 D -> N (in dbSNP:rs141986192).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_069062.
VARIANT 398 398 R -> W (in dbSNP:rs1804598).
/FTId=VAR_011897.
VARIANT 454 454 S -> L (in dbSNP:rs34764811).
/FTId=VAR_034364.
MUTAGEN 188 188 R->A: Loss of glycan-binding activity and
partial inhibition of ERAD of the
misfolded glycoprotein NHK
(PubMed:19346256). Reduced interaction
with SEL1L (PubMed:18264092) not
confirmed in (PubMed:19346256).
{ECO:0000269|PubMed:18264092,
ECO:0000269|PubMed:18417469,
ECO:0000269|PubMed:19346256}.
CONFLICT 7 7 L -> V (in Ref. 5; CAG33072).
{ECO:0000305}.
CONFLICT 194 194 F -> V (in Ref. 4; BAG64798).
{ECO:0000305}.
CONFLICT 371 371 E -> G (in Ref. 4; BAG56939).
{ECO:0000305}.
CONFLICT 497 497 L -> F (in Ref. 4; BAG64798).
{ECO:0000305}.
CONFLICT 522 522 V -> I (in Ref. 4; BAG60733).
{ECO:0000305}.
CONFLICT 653 653 S -> P (in Ref. 4; BAG56939).
{ECO:0000305}.
STRAND 111 115 {ECO:0000244|PDB:3AIH}.
STRAND 118 123 {ECO:0000244|PDB:3AIH}.
TURN 124 126 {ECO:0000244|PDB:3AIH}.
STRAND 127 131 {ECO:0000244|PDB:3AIH}.
STRAND 143 155 {ECO:0000244|PDB:3AIH}.
STRAND 169 176 {ECO:0000244|PDB:3AIH}.
TURN 182 184 {ECO:0000244|PDB:3AIH}.
STRAND 189 196 {ECO:0000244|PDB:3AIH}.
STRAND 206 214 {ECO:0000244|PDB:3AIH}.
STRAND 217 224 {ECO:0000244|PDB:3AIH}.
HELIX 225 227 {ECO:0000244|PDB:3AIH}.
SEQUENCE 667 AA; 75562 MW; 65BA3F66CEC58756 CRC64;
MAAETLLSSL LGLLLLGLLL PASLTGGVGS LNLEELSEMR YGIEILPLPV MGGQSQSSDV
VIVSSKYKQR YECRLPAGAI HFQREREEET PAYQGPGIPE LLSPMRDAPC LLKTKDWWTY
EFCYGRHIQQ YHMEDSEIKG EVLYLGYYQS AFDWDDETAK ASKQHRLKRY HSQTYGNGSK
CDLNGRPREA EVRFLCDEGA GISGDYIDRV DEPLSCSYVL TIRTPRLCPH PLLRPPPSAA
PQAILCHPSL QPEEYMAYVQ RQADSKQYGD KIIEELQDLG PQVWSETKSG VAPQKMAGAS
PTKDDSKDSD FWKMLNEPED QAPGGEEVPA EEQDPSPEAA DSASGAPNDF QNNVQVKVIR
SPADLIRFIE ELKGGTKKGK PNIGQEQPVD DAAEVPQREP EKERGDPERQ REMEEEEDED
EDEDEDEDER QLLGEFEKEL EGILLPSDRD RLRSEVKAGM ERELENIIQE TEKELDPDGL
KKESERDRAM LALTSTLNKL IKRLEEKQSP ELVKKHKKKR VVPKKPPPSP QPTEEDPEHR
VRVRVTKLRL GGPNQDLTVL EMKRENPQLK QIEGLVKELL EREGLTAAGK IEIKIVRPWA
EGTEEGARWL TDEDTRNLKE IFFNILVPGA EEAQKERQRQ KELESNYRRV WGSPGGEGTG
DLDEFDF


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