SCG1_HUMAN
ID SCG1_HUMAN Reviewed; 677 AA.
AC P05060; A8K021; Q59EU9; Q6IBS6; Q9BQV6; Q9UC25; Q9UJA6;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Secretogranin-1;
DE AltName: Full=Chromogranin-B;
DE Short=CgB;
DE AltName: Full=Secretogranin I;
DE Short=SgI;
DE Contains:
DE RecName: Full=PE-11;
DE Contains:
DE RecName: Full=GAWK peptide;
DE Contains:
DE RecName: Full=CCB peptide;
DE Flags: Precursor;
GN Name=CHGB; Synonyms=SCG1;
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], PROTEIN SEQUENCE OF 21-34; 85-93; 334-340 AND
RP 347-355, TISSUE SPECIFICITY, AND VARIANT ALA-243.
RC TISSUE=Adrenal medulla;
RX PubMed=3608978; DOI=10.1002/j.1460-2075.1987.tb02355.x;
RA Benedum U.M., Lamouroux A., Konecki D.S., Hille A., Baeuerle P.A.,
RA Frank R., Lottspeich F., Mallet J., Huttner W.B.;
RT "The primary structure of human secretogranin I (chromogranin B):
RT comparison with chromogranin A reveals homologous terminal domains and a
RT large intervening variable region.";
RL EMBO J. 6:1203-1211(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-93; GLN-178;
RP ALA-243; GLY-353 AND HIS-417.
RC TISSUE=Adrenal gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-243.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-93; GLN-178;
RP ALA-243; GLY-353 AND HIS-417.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-243.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-243.
RC TISSUE=Lung;
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 [8]
RP PROTEIN SEQUENCE OF 21-48.
RX PubMed=1882087; DOI=10.1016/0167-0115(91)90216-4;
RA Gill B.M., Barbosa J.A., Dinh T.Q., Garrod S., O'Connor D.T.;
RT "Chromogranin B: isolation from pheochromocytoma, N-terminal sequence,
RT tissue distribution and secretory vesicle processing.";
RL Regul. Pept. 33:223-235(1991).
RN [9]
RP PROTEIN SEQUENCE OF 334-385.
RX PubMed=7784254; DOI=10.1016/0196-9781(94)00176-6;
RA Woussen-Colle M.-C., Gourlet P., Vandermeers A., Vandermeers-Piret M.-C.,
RA D'Haens J., Velkeniers B., Robberecht P.;
RT "Identification of a new chromogranin B fragment (314-365) in endocrine
RT tumors.";
RL Peptides 16:231-236(1995).
RN [10]
RP PROTEIN SEQUENCE OF 440-513.
RC TISSUE=Pituitary;
RX PubMed=3970711; DOI=10.1016/0006-291x(85)90648-5;
RA Benjannet S., Leduc R., Lazure C., Seidah N.G., Marcinkiewicz M.,
RA Chretien M.;
RT "GAWK, a novel human pituitary polypeptide: isolation, immunocytochemical
RT localization and complete amino acid sequence.";
RL Biochem. Biophys. Res. Commun. 126:602-609(1985).
RN [11]
RP PROTEIN SEQUENCE OF 617-673.
RC TISSUE=Pituitary;
RX PubMed=3678488; DOI=10.1016/0014-5793(87)80438-6;
RA Benjannet S., Leduc R., Adrouche N., Falgueyret J.P., Marcinkiewicz M.,
RA Seidah N.G., Mbikay M., Lazure C., Chretien M.;
RT "Chromogranin B (secretogranin I), a putative precursor of two novel
RT pituitary peptides through processing at paired basic residues.";
RL FEBS Lett. 224:142-148(1987).
RN [12]
RP PHOSPHORYLATION AT SER-149 AND SER-405.
RC TISSUE=Pituitary;
RX PubMed=14997482; DOI=10.1002/pmic.200300584;
RA Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.;
RT "Identification and characterization of phosphorylated proteins in the
RT human pituitary.";
RL Proteomics 4:587-598(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-259; SER-263;
RP SER-311; SER-335; SER-405 AND SER-617, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [14]
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-405, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP PHOSPHORYLATION AT SER-130; SER-225; SER-367; SER-377; SER-380 AND TYR-401.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
CC -!- FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule
CC protein, which may be the precursor for other biologically active
CC peptides.
CC -!- INTERACTION:
CC P05060; Q8IXL6: FAM20C; NbExp=2; IntAct=EBI-712619, EBI-7147442;
CC P05060; Q5S007: LRRK2; NbExp=3; IntAct=EBI-712619, EBI-5323863;
CC P05060; Q15796: SMAD2; NbExp=2; IntAct=EBI-712619, EBI-1040141;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC secretory granules.
CC -!- TISSUE SPECIFICITY: Expressed in the adrenal medulla, and in
CC pheochromocytoma. Not expressed in liver. {ECO:0000269|PubMed:3608978}.
CC -!- PTM: Extensively processed by limited proteolysis at conserved basic
CC residues. Alternative processing are seen in different tissues (By
CC similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}.
CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92949.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y00064; CAA68271.1; -; mRNA.
DR EMBL; AK289386; BAF82075.1; -; mRNA.
DR EMBL; CR456726; CAG33007.1; -; mRNA.
DR EMBL; AB209712; BAD92949.1; ALT_INIT; mRNA.
DR EMBL; AL035461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10410.1; -; Genomic_DNA.
DR EMBL; BC000375; AAH00375.1; -; mRNA.
DR CCDS; CCDS13092.1; -.
DR PIR; A29264; CNHUB.
DR RefSeq; NP_001810.2; NM_001819.2.
DR AlphaFoldDB; P05060; -.
DR BioGRID; 107539; 36.
DR IntAct; P05060; 38.
DR MINT; P05060; -.
DR STRING; 9606.ENSP00000368244; -.
DR GlyConnect; 1727; 1 N-Linked glycan (1 site).
DR GlyGen; P05060; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; P05060; -.
DR PhosphoSitePlus; P05060; -.
DR BioMuta; CHGB; -.
DR DMDM; 311033509; -.
DR EPD; P05060; -.
DR jPOST; P05060; -.
DR MassIVE; P05060; -.
DR PaxDb; P05060; -.
DR PeptideAtlas; P05060; -.
DR PRIDE; P05060; -.
DR ProteomicsDB; 51772; -.
DR Antibodypedia; 2170; 246 antibodies from 33 providers.
DR DNASU; 1114; -.
DR Ensembl; ENST00000378961.9; ENSP00000368244.4; ENSG00000089199.10.
DR GeneID; 1114; -.
DR KEGG; hsa:1114; -.
DR MANE-Select; ENST00000378961.9; ENSP00000368244.4; NM_001819.3; NP_001810.2.
DR UCSC; uc002wmg.4; human.
DR CTD; 1114; -.
DR DisGeNET; 1114; -.
DR GeneCards; CHGB; -.
DR HGNC; HGNC:1930; CHGB.
DR HPA; ENSG00000089199; Group enriched (adrenal gland, pituitary gland).
DR MIM; 118920; gene.
DR neXtProt; NX_P05060; -.
DR OpenTargets; ENSG00000089199; -.
DR PharmGKB; PA26462; -.
DR VEuPathDB; HostDB:ENSG00000089199; -.
DR eggNOG; ENOG502QRBF; Eukaryota.
DR GeneTree; ENSGT00940000154206; -.
DR HOGENOM; CLU_026095_0_0_1; -.
DR InParanoid; P05060; -.
DR OMA; WGYEKRS; -.
DR OrthoDB; 670416at2759; -.
DR PhylomeDB; P05060; -.
DR TreeFam; TF336596; -.
DR PathwayCommons; P05060; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P05060; -.
DR BioGRID-ORCS; 1114; 13 hits in 1072 CRISPR screens.
DR ChiTaRS; CHGB; human.
DR GeneWiki; Secretoneurin; -.
DR GenomeRNAi; 1114; -.
DR Pharos; P05060; Tbio.
DR PRO; PR:P05060; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P05060; protein.
DR Bgee; ENSG00000089199; Expressed in paraflocculus and 140 other tissues.
DR ExpressionAtlas; P05060; baseline and differential.
DR Genevisible; P05060; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; TAS:ProtInc.
DR InterPro; IPR001819; Chromogranin_AB.
DR InterPro; IPR018054; Chromogranin_CS.
DR InterPro; IPR001990; Granin.
DR PANTHER; PTHR10583; PTHR10583; 1.
DR Pfam; PF01271; Granin; 1.
DR PRINTS; PR00659; CHROMOGRANIN.
DR PROSITE; PS00422; GRANINS_1; 1.
DR PROSITE; PS00423; GRANINS_2; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Phosphoprotein; Reference proteome; Secreted;
KW Signal; Sulfation.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1882087,
FT ECO:0000269|PubMed:3608978"
FT CHAIN 21..677
FT /note="Secretogranin-1"
FT /id="PRO_0000005438"
FT PEPTIDE 440..513
FT /note="GAWK peptide"
FT /id="PRO_0000005439"
FT PEPTIDE 575..585
FT /note="PE-11"
FT /evidence="ECO:0000250|UniProtKB:P16014"
FT /id="PRO_0000432730"
FT PEPTIDE 617..673
FT /note="CCB peptide"
FT /id="PRO_0000005440"
FT REGION 64..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..120
FT /note="O-glycosylated at one site"
FT REGION 475..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35314"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 130
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14997482,
FT ECO:0007744|PubMed:16807684"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 225
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807684"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807684"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807684"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807684"
FT MOD_RES 341
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35314"
FT MOD_RES 367
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 377
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 380
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 401
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14997482,
FT ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:24275569"
FT MOD_RES 474
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 566
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16807684"
FT MOD_RES 624
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35314"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT DISULFID 36..57
FT VARIANT 93
FT /note="S -> T (in dbSNP:rs6085324)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_043578"
FT VARIANT 117
FT /note="K -> N (in dbSNP:rs236150)"
FT /id="VAR_024414"
FT VARIANT 145
FT /note="D -> N (in dbSNP:rs6133278)"
FT /id="VAR_028235"
FT VARIANT 178
FT /note="R -> Q (in dbSNP:rs910122)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_020287"
FT VARIANT 200
FT /note="N -> H (in dbSNP:rs881118)"
FT /id="VAR_028236"
FT VARIANT 232
FT /note="R -> Q (in dbSNP:rs6139873)"
FT /id="VAR_028237"
FT VARIANT 243
FT /note="T -> A (in dbSNP:rs236151)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:3608978,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.6"
FT /id="VAR_024415"
FT VARIANT 353
FT /note="A -> G (in dbSNP:rs236152)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_024416"
FT VARIANT 413
FT /note="P -> L (in dbSNP:rs742710)"
FT /id="VAR_028238"
FT VARIANT 417
FT /note="R -> H (in dbSNP:rs742711)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_022012"
FT CONFLICT 24
FT /note="D -> E (in Ref. 2; BAF82075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 677 AA; 78276 MW; BFDC97F7B21245B3 CRC64;
MQPTLLLSLL GAVGLAAVNS MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV
LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT
EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE
DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG
EETGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP
SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE
RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR
GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP
GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD
NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ
YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA
AMDLELQKIA EKFSQRG
