SAMD9_HUMAN
ID SAMD9_HUMAN Reviewed; 1589 AA.
AC Q5K651; A2RU68; Q5K649; Q6P080; Q75N21; Q8IVG6; Q9NXS8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Sterile alpha motif domain-containing protein 9;
DE Short=SAM domain-containing protein 9;
GN Name=SAMD9; Synonyms=C7orf5, DRIF1, KIAA2004, OEF1;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17407603; DOI=10.1186/1471-2164-8-92;
RA Li C.F., MacDonald J.R., Wei R.Y., Ray J., Lau K., Kandel C., Koffman R.,
RA Bell S., Scherer S.W., Alman B.A.;
RT "Human sterile alpha motif domain 9, a novel gene identified as down-
RT regulated in aggressive fibromatosis, is absent in the mouse.";
RL BMC Genomics 8:92-92(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Aortic endothelium;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum, and Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 955-1589.
RC TISSUE=Colon;
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 [8]
RP FUNCTION, INDUCTION, AND VARIANT NFTC GLU-1495.
RX PubMed=18094730; DOI=10.1038/sj.jid.5701203;
RA Chefetz I., Ben Amitai D., Browning S., Skorecki K., Adir N., Thomas M.G.,
RA Kogleck L., Topaz O., Indelman M., Uitto J., Richard G., Bradman N.,
RA Sprecher E.;
RT "Normophosphatemic familial tumoral calcinosis is caused by deleterious
RT mutations in SAMD9, encoding a TNF-alpha responsive protein.";
RL J. Invest. Dermatol. 128:1423-1429(2008).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT NFTC GLU-1495,
RP AND CHARACTERIZATION OF VARIANT NFTC GLU-1495.
RX PubMed=16960814; DOI=10.1086/508069;
RA Topaz O., Indelman M., Chefetz I., Geiger D., Metzker A., Altschuler Y.,
RA Choder M., Bercovich D., Uitto J., Bergman R., Richard G., Sprecher E.;
RT "A deleterious mutation in SAMD9 causes normophosphatemic familial tumoral
RT calcinosis.";
RL Am. J. Hum. Genet. 79:759-764(2006).
RN [10]
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., Buerckstuemmer T.,
RA 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 [11]
RP FUNCTION, INDUCTION BY IFNG, AND INTERACTION WITH RGL2.
RX PubMed=21160498; DOI=10.1038/jid.2010.387;
RA Hershkovitz D., Gross Y., Nahum S., Yehezkel S., Sarig O., Uitto J.,
RA Sprecher E.;
RT "Functional characterization of SAMD9, a protein deficient in
RT normophosphatemic familial tumoral calcinosis.";
RL J. Invest. Dermatol. 131:662-669(2011).
RN [12]
RP FUNCTION IN ENDOSOME FUSION, AND INTERACTION WITH EEA1.
RX PubMed=24029230; DOI=10.1016/j.ccr.2013.08.011;
RA Nagamachi A., Matsui H., Asou H., Ozaki Y., Aki D., Kanai A., Takubo K.,
RA Suda T., Nakamura T., Wolff L., Honda H., Inaba T.;
RT "Haploinsufficiency of SAMD9L, an endosome fusion facilitator, causes
RT myeloid malignancies in mice mimicking human diseases with monosomy 7.";
RL Cancer Cell 24:305-317(2013).
RN [13]
RP INVOLVEMENT IN MIRAGE, VARIANTS MIRAGE GLN-459; ASN-769; TYR-834; LYS-974;
RP VAL-1195; LEU-1280; LYS-1286 AND TRP-1293, AND CHARACTERIZATION OF VARIANTS
RP MIRAGE GLN-459; ASN-769; TYR-834; LYS-974; VAL-1195; LEU-1280; LYS-1286 AND
RP TRP-1293.
RX PubMed=27182967; DOI=10.1038/ng.3569;
RA Narumi S., Amano N., Ishii T., Katsumata N., Muroya K., Adachi M.,
RA Toyoshima K., Tanaka Y., Fukuzawa R., Miyako K., Kinjo S., Ohga S.,
RA Ihara K., Inoue H., Kinjo T., Hara T., Kohno M., Yamada S., Urano H.,
RA Kitagawa Y., Tsugawa K., Higa A., Miyawaki M., Okutani T., Kizaki Z.,
RA Hamada H., Kihara M., Shiga K., Yamaguchi T., Kenmochi M., Kitajima H.,
RA Fukami M., Shimizu A., Kudoh J., Shibata S., Okano H., Miyake N.,
RA Matsumoto N., Hasegawa T.;
RT "SAMD9 mutations cause a novel multisystem disorder, MIRAGE syndrome, and
RT are associated with loss of chromosome 7.";
RL Nat. Genet. 48:792-797(2016).
RN [14]
RP INVOLVEMENT IN M7MLS2, AND VARIANT M7MLS2 GLU-676.
RX PubMed=30046003; DOI=10.1172/jci.insight.121086;
RA Wong J.C., Bryant V., Lamprecht T., Ma J., Walsh M., Schwartz J.,
RA Del Pilar Alzamora M., Mullighan C.G., Loh M.L., Ribeiro R., Downing J.R.,
RA Carroll W.L., Davis J., Gold S., Rogers P.C., Israels S., Yanofsky R.,
RA Shannon K., Klco J.M.;
RT "Germline SAMD9 and SAMD9L mutations are associated with extensive genetic
RT evolution and diverse hematologic outcomes.";
RL JCI Insight 3:0-0(2018).
CC -!- FUNCTION: May play a role in the inflammatory response to tissue injury
CC and the control of extra-osseous calcification, acting as a downstream
CC target of TNF-alpha signaling. Involved in the regulation of EGR1, in
CC coordination with RGL2. May be involved in endosome fusion.
CC {ECO:0000269|PubMed:16960814, ECO:0000269|PubMed:18094730,
CC ECO:0000269|PubMed:21160498, ECO:0000269|PubMed:24029230}.
CC -!- SUBUNIT: Interacts with RGL2 (PubMed:21160498). Interacts with EEA1
CC (PubMed:24029230). {ECO:0000269|PubMed:21160498,
CC ECO:0000269|PubMed:24029230}.
CC -!- INTERACTION:
CC Q5K651; Q15075: EEA1; NbExp=2; IntAct=EBI-2814750, EBI-298113;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16960814,
CC ECO:0000269|PubMed:17407603}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Very low levels are detected in
CC skeletal muscle. Not detected in brain. Down-regulated in aggressive
CC fibromatosis, as well as in breast and colon cancers. Up-regulated in
CC fibroblasts from patients with normophosphatemic tumoral calcinosis
CC (NFTC). {ECO:0000269|PubMed:16960814, ECO:0000269|PubMed:17407603}.
CC -!- INDUCTION: Up-regulated by TNF-alpha through p38 MAPKs and NF-kappa-B.
CC Up-regulated by osmotic shock. Induced by IFNG.
CC {ECO:0000269|PubMed:18094730, ECO:0000269|PubMed:21160498}.
CC -!- DISEASE: Tumoral calcinosis, normophosphatemic, familial (NFTC)
CC [MIM:610455]: An uncommon, life-threatening disorder characterized by
CC progressive deposition of calcified masses in cutaneous and
CC subcutaneous tissues. Serum phosphate levels are normal. Clinical
CC features include painful calcified ulcerative lesions and massive
CC calcium deposition in the mid- and lower dermis, severe skin and bone
CC infections, erythematous papular skin eruption in infancy,
CC conjunctivitis, and gingivitis. NFTC shows a striking resemblance to
CC acquired dystrophic calcinosis, in which tissue calcification occurs as
CC a consequence of tissue injury/inflammation.
CC {ECO:0000269|PubMed:16960814, ECO:0000269|PubMed:18094730}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: MIRAGE syndrome (MIRAGE) [MIM:617053]: A form of syndromic
CC adrenal hypoplasia characterized by myelodysplasia, infection,
CC restriction of growth, adrenal hypoplasia, genital phenotypes, and
CC enteropathy. {ECO:0000269|PubMed:27182967}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Monosomy 7 myelodysplasia and leukemia syndrome 2 (M7MLS2)
CC [MIM:619041]: A hematologic disorder manifesting in early childhood and
CC characterized by bone marrow dyspoiesis, pancytopenia, myelodysplastic
CC syndrome or acute myelogenous leukemia, associated with monosomy 7 in
CC the bone marrow. Disease severity is highly variable. Inheritance is
CC autosomal dominant with incomplete penetrance.
CC {ECO:0000269|PubMed:30046003}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Germline mutations in
CC SAMD9 with a suppressive effect on the cell cycle are associated with
CC somatic loss of the chromosome 7 harboring the mutant allele. This
CC results in the deletion of several genes and predisposes to the
CC development of myelodysplastic syndrome and acute myelogenous leukemia.
CC {ECO:0000269|PubMed:30046003}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH65769.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAQ04689.3; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=BAA90932.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC23101.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF445355; AAQ04637.1; -; mRNA.
DR EMBL; AF453311; AAQ04689.3; ALT_SEQ; mRNA.
DR EMBL; AB095925; BAC23101.1; ALT_INIT; mRNA.
DR EMBL; AC000119; AAQ96842.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24145.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76826.1; -; Genomic_DNA.
DR EMBL; BC065769; AAH65769.1; ALT_SEQ; mRNA.
DR EMBL; BC132773; AAI32774.1; -; mRNA.
DR EMBL; BC132775; AAI32776.1; -; mRNA.
DR EMBL; BC150249; AAI50250.1; -; mRNA.
DR EMBL; AK000080; BAA90932.1; ALT_INIT; mRNA.
DR CCDS; CCDS34680.1; -.
DR RefSeq; NP_001180236.1; NM_001193307.1.
DR RefSeq; NP_060124.2; NM_017654.3.
DR PDB; 7KSP; X-ray; 2.80 A; A/B=156-385.
DR PDBsum; 7KSP; -.
DR AlphaFoldDB; Q5K651; -.
DR SMR; Q5K651; -.
DR BioGRID; 120166; 22.
DR IntAct; Q5K651; 9.
DR STRING; 9606.ENSP00000369292; -.
DR GlyGen; Q5K651; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5K651; -.
DR MetOSite; Q5K651; -.
DR PhosphoSitePlus; Q5K651; -.
DR BioMuta; SAMD9; -.
DR DMDM; 71153739; -.
DR EPD; Q5K651; -.
DR jPOST; Q5K651; -.
DR MassIVE; Q5K651; -.
DR MaxQB; Q5K651; -.
DR PaxDb; Q5K651; -.
DR PeptideAtlas; Q5K651; -.
DR PRIDE; Q5K651; -.
DR ProteomicsDB; 63547; -.
DR Antibodypedia; 15642; 126 antibodies from 21 providers.
DR DNASU; 54809; -.
DR Ensembl; ENST00000379958.3; ENSP00000369292.2; ENSG00000205413.8.
DR Ensembl; ENST00000620985.4; ENSP00000484636.1; ENSG00000205413.8.
DR GeneID; 54809; -.
DR KEGG; hsa:54809; -.
DR MANE-Select; ENST00000379958.3; ENSP00000369292.2; NM_017654.4; NP_060124.2.
DR UCSC; uc003umf.4; human.
DR CTD; 54809; -.
DR DisGeNET; 54809; -.
DR GeneCards; SAMD9; -.
DR GeneReviews; SAMD9; -.
DR HGNC; HGNC:1348; SAMD9.
DR HPA; ENSG00000205413; Tissue enhanced (esophagus).
DR MalaCards; SAMD9; -.
DR MIM; 610455; phenotype.
DR MIM; 610456; gene.
DR MIM; 617053; phenotype.
DR MIM; 619041; phenotype.
DR neXtProt; NX_Q5K651; -.
DR OpenTargets; ENSG00000205413; -.
DR Orphanet; 306658; Familial normophosphatemic tumoral calcinosis.
DR Orphanet; 494433; MIRAGE syndrome.
DR PharmGKB; PA25948; -.
DR VEuPathDB; HostDB:ENSG00000205413; -.
DR eggNOG; ENOG502QPY6; Eukaryota.
DR GeneTree; ENSGT00390000013973; -.
DR InParanoid; Q5K651; -.
DR OMA; KFSVFVR; -.
DR OrthoDB; 29718at2759; -.
DR PhylomeDB; Q5K651; -.
DR TreeFam; TF331842; -.
DR PathwayCommons; Q5K651; -.
DR SignaLink; Q5K651; -.
DR BioGRID-ORCS; 54809; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; SAMD9; human.
DR GeneWiki; SAMD9; -.
DR GenomeRNAi; 54809; -.
DR Pharos; Q5K651; Tbio.
DR PRO; PR:Q5K651; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q5K651; protein.
DR Bgee; ENSG00000205413; Expressed in esophagus squamous epithelium and 176 other tissues.
DR ExpressionAtlas; Q5K651; baseline and differential.
DR Genevisible; Q5K651; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0034058; P:endosomal vesicle fusion; IDA:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; Reference proteome.
FT CHAIN 1..1589
FT /note="Sterile alpha motif domain-containing protein 9"
FT /id="PRO_0000097573"
FT DOMAIN 14..78
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 83..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 143
FT /note="I -> T (in dbSNP:rs6969691)"
FT /id="VAR_031526"
FT VARIANT 449
FT /note="N -> S (in dbSNP:rs10239435)"
FT /id="VAR_031527"
FT VARIANT 459
FT /note="R -> Q (in MIRAGE; decreased cell proliferation;
FT changed endosome organization)"
FT /evidence="ECO:0000269|PubMed:27182967"
FT /id="VAR_077885"
FT VARIANT 549
FT /note="V -> L (in dbSNP:rs10279499)"
FT /id="VAR_031528"
FT VARIANT 676
FT /note="K -> E (in M7MLS2)"
FT /evidence="ECO:0000269|PubMed:30046003"
FT /id="VAR_085147"
FT VARIANT 769
FT /note="D -> N (in MIRAGE; decreased cell proliferation;
FT changed endosome organization)"
FT /evidence="ECO:0000269|PubMed:27182967"
FT /id="VAR_077886"
FT VARIANT 834
FT /note="N -> Y (in MIRAGE; decreased cell proliferation;
FT changed endosome organization)"
FT /evidence="ECO:0000269|PubMed:27182967"
FT /id="VAR_077887"
FT VARIANT 974
FT /note="E -> K (in MIRAGE; decreased cell proliferation;
FT changed endosome organization; dbSNP:rs1554336981)"
FT /evidence="ECO:0000269|PubMed:27182967"
FT /id="VAR_077888"
FT VARIANT 1195
FT /note="A -> V (in MIRAGE; decreased cell proliferation;
FT changed endosome organization)"
FT /evidence="ECO:0000269|PubMed:27182967"
FT /id="VAR_077889"
FT VARIANT 1280
FT /note="P -> L (in MIRAGE; decreased cell proliferation;
FT changed endosome organization)"
FT /evidence="ECO:0000269|PubMed:27182967"
FT /id="VAR_077890"
FT VARIANT 1286
FT /note="Q -> K (in MIRAGE; decreased cell proliferation;
FT changed endosome organization)"
FT /evidence="ECO:0000269|PubMed:27182967"
FT /id="VAR_077891"
FT VARIANT 1293
FT /note="R -> W (in MIRAGE; decreased cell proliferation;
FT changed endosome organization)"
FT /evidence="ECO:0000269|PubMed:27182967"
FT /id="VAR_077813"
FT VARIANT 1495
FT /note="K -> E (in NFTC; loss of cytoplasmic expression;
FT dbSNP:rs121918554)"
FT /evidence="ECO:0000269|PubMed:16960814,
FT ECO:0000269|PubMed:18094730"
FT /id="VAR_031529"
FT CONFLICT 1577
FT /note="S -> P (in Ref. 7; BAA90932)"
FT /evidence="ECO:0000305"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:7KSP"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:7KSP"
FT HELIX 208..229
FT /evidence="ECO:0007829|PDB:7KSP"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:7KSP"
FT HELIX 254..271
FT /evidence="ECO:0007829|PDB:7KSP"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:7KSP"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:7KSP"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:7KSP"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:7KSP"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:7KSP"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:7KSP"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:7KSP"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:7KSP"
FT HELIX 366..379
FT /evidence="ECO:0007829|PDB:7KSP"
SQ SEQUENCE 1589 AA; 184281 MW; CF3EF341ED092167 CRC64;
MAKQLNLPEN TDDWTKEDVN QWLESHKIDQ KHREILTEQD VNGAVLKWLK KEHLVDMGIT
HGPAIQIEEL FKELRKTAIE DSIQTSKMGK PSKNAPKDQT VSQKERRETS KQKQKGKENP
DMANPSAMST TAKGSKSLKV ELIEDKIDYT KERQPSIDLT CVSYPFDEFS NPYRYKLDFS
LQPETGPGNL IDPIHEFKAF TNTATATEED VKMKFSNEVF RFASACMNSR TNGTIHFGVK
DKPHGKIVGI KVTNDTKEAL INHFNLMINK YFEDHQVQQA KKCIREPRFV EVLLPNSTLS
DRFVIEVDII PQFSECQYDY FQIKMQNYNN KIWEQSKKFS LFVRDGTSSK DITKNKVDFR
AFKADFKTLA ESRKAAEEKF RAKTNKKERE GPKLVKLLTG NQDLLDNSYY EQYILVTNKC
HPDQTKHLDF LKEIKWFAVL EFDPESNING VVKAYKESRV ANLHFPSVYV EQKTTPNETI
STLNLYHQPS WIFCNGRLDL DSEKYKPFDP SSWQRERASD VRKLISFLTH EDIMPRGKFL
VVFLLLSSVD DPRDPLIETF CAFYQDLKGM ENILCICVHP HIFQGWKDLL EARLIKHQDE
ISSQCISALS LEEINGTILK LKSVTQSSKR LLPSIGLSTV LLKKEEDIMT ALEIICENEC
EGTLLEKDKN KFLEFKASKE EDFYRGGKVS WWNFYFSSES YSSPFVKRDK YERLEAMIQN
CADSSKPTST KIIHLYHHPG CGGTTLAMHI LWELRKKFRC AVLKNKTVDF SEIGEQVTSL
ITYGAMNRQE YVPVLLLVDD FEEQDNVYLL QYSIQTAIAK KYIRYEKPLV IILNCMRSQN
PEKSARIPDS IAVIQQLSPK EQRAFELKLK EIKEQHKNFE DFYSFMIMKT NFNKEYIENV
VRNILKGQNI FTKEAKLFSF LALLNSYVPD TTISLSQCEK FLGIGNKKAF WGTEKFEDKM
GTYSTILIKT EVIECGNYCG VRIIHSLIAE FSLEELKKSY HLNKSQIMLD MLTENLFFDT
GMGKSKFLQD MHTLLLTRHR DEHEGETGNW FSPFIEALHK DEGNEAVEAV LLESIHRFNP
NAFICQALAR HFYIKKKDFG NALNWAKQAK IIEPDNSYIS DTLGQVYKSK IRWWIEENGG
NGNISVDDLI ALLDLAEHAS SAFKESQQQS EDREYEVKER LYPKSKRRYD TYNIAGYQGE
IEVGLYTIQI LQLIPFFDNK NELSKRYMVN FVSGSSDIPG DPNNEYKLAL KNYIPYLTKL
KFSLKKSFDF FDEYFVLLKP RNNIKQNEEA KTRRKVAGYF KKYVDIFCLL EESQNNTGLG
SKFSEPLQVE RCRRNLVALK ADKFSGLLEY LIKSQEDAIS TMKCIVNEYT FLLEQCTVKI
QSKEKLNFIL ANIILSCIQP TSRLVKPVEK LKDQLREVLQ PIGLTYQFSE PYFLASLLFW
PENQQLDQHS EQMKEYAQAL KNSFKGQYKH MHRTKQPIAY FFLGKGKRLE RLVHKGKIDQ
CFKKTPDINS LWQSGDVWKE EKVQELLLRL QGRAENNCLY IEYGINEKIT IPITPAFLGQ
LRSGRSIEKV SFYLGFSIGG PLAYDIEIV
