ID SERPH_HUMAN Reviewed; 418 AA. AC P50454; B3KVJ3; P29043; Q5XPB4; Q6NSJ6; Q8IY96; Q9NP88; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 27-MAR-2024, entry version 224. DE RecName: Full=Serpin H1; DE AltName: Full=47 kDa heat shock protein; DE AltName: Full=Arsenic-transactivated protein 3; DE Short=AsTP3; DE AltName: Full=Cell proliferation-inducing gene 14 protein; DE AltName: Full=Collagen-binding protein; DE Short=Colligin; DE AltName: Full=Rheumatoid arthritis-related antigen RA-A47; DE Flags: Precursor; GN Name=SERPINH1; Synonyms=CBP1, CBP2, HSP47, SERPINH2; ORFNames=PIG14; 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]. RC TISSUE=Fibroblast; RX PubMed=1309665; DOI=10.1016/0167-4781(92)90498-o; RA Clarke E., Sandwal B.D.; RT "Cloning of a human collagen-binding protein, and its homology with rat RT gp46, chick hsp47 and mouse J6 proteins."; RL Biochim. Biophys. Acta 1129:246-248(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7656593; DOI=10.1159/000134103; RA Ikegawa S., Sudo K., Okui K., Nakamura Y.; RT "Isolation, characterization and chromosomal assignment of human colligin-2 RT gene (CBP2)."; RL Cytogenet. Cell Genet. 71:182-186(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cartilage, and Fibroblast; RX PubMed=11052465; DOI=10.1007/s007740070004; RA Hattori T., Takahash K., Yutani Y., Fujisawa T., Nakanishi T., Takigawa M.; RT "Rheumatoid arthritis-related antigen 47kDa (RA-A47) is a product of RT colligin-2 and acts as a human HSP47."; RL J. Bone Miner. Metab. 18:328-334(2000). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wu S.-H., Cheng J., Zheng Y.-J., Zhang Y.-X., Liu Y., Zhong Y.-W.; RT "Cloning and identification of human AsTP3 gene transactivated by arsenic RT trioxide in HepG2 cells."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kim J.W.; RT "Identification of a human cell proliferation gene 14."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Ovary, and Skin; 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 [10] RP POLYMORPHISM IN PROMOTER, AND INVOLVEMENT IN PPROM. RX PubMed=16938879; DOI=10.1073/pnas.0603676103; RA Wang H., Parry S., Macones G., Sammel M.D., Kuivaniemi H., Tromp G., RA Argyropoulos G., Halder I., Shriver M.D., Romero R., Strauss J.F. III; RT "A functional SNP in the promoter of the SERPINH1 gene increases risk of RT preterm premature rupture of membranes in African Americans."; RL Proc. Natl. Acad. Sci. U.S.A. 103:13463-13467(2006). RN [11] 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] 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 [15] RP VARIANT OI10 PRO-78. RX PubMed=20188343; DOI=10.1016/j.ajhg.2010.01.034; RA Christiansen H.E., Schwarze U., Pyott S.M., AlSwaid A., Al Balwi M., RA Alrasheed S., Pepin M.G., Weis M.A., Eyre D.R., Byers P.H.; RT "Homozygosity for a missense mutation in SERPINH1, which encodes the RT collagen chaperone protein HSP47, results in severe recessive osteogenesis RT imperfecta."; RL Am. J. Hum. Genet. 86:389-398(2010). CC -!- FUNCTION: Binds specifically to collagen. Could be involved as a CC chaperone in the biosynthetic pathway of collagen. CC -!- INTERACTION: CC P50454; P54819: AK2; NbExp=3; IntAct=EBI-350723, EBI-1056291; CC P50454; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-350723, EBI-2875816; CC P50454; P54253: ATXN1; NbExp=3; IntAct=EBI-350723, EBI-930964; CC P50454; P54252: ATXN3; NbExp=3; IntAct=EBI-350723, EBI-946046; CC P50454; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-350723, EBI-742750; CC P50454; P12830: CDH1; NbExp=3; IntAct=EBI-350723, EBI-727477; CC P50454; Q8NE08: COL25A1; NbExp=3; IntAct=EBI-350723, EBI-25836642; CC P50454; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-350723, EBI-9087876; CC P50454; P49184: DNASE1L1; NbExp=3; IntAct=EBI-350723, EBI-20894690; CC P50454; P15036: ETS2; NbExp=3; IntAct=EBI-350723, EBI-1646991; CC P50454; Q969W3: FAM104A; NbExp=3; IntAct=EBI-350723, EBI-10281506; CC P50454; O75874: IDH1; NbExp=3; IntAct=EBI-350723, EBI-715695; CC P50454; Q6PI98: INO80C; NbExp=3; IntAct=EBI-350723, EBI-722540; CC P50454; P06756: ITGAV; NbExp=3; IntAct=EBI-350723, EBI-298282; CC P50454; P23276: KEL; NbExp=3; IntAct=EBI-350723, EBI-746662; CC P50454; O60259: KLK8; NbExp=3; IntAct=EBI-350723, EBI-3915857; CC P50454; Q9NPC7: MYNN; NbExp=3; IntAct=EBI-350723, EBI-3446748; CC P50454; Q16549: PCSK7; NbExp=3; IntAct=EBI-350723, EBI-8059854; CC P50454; Q9NUD9: PIGV; NbExp=3; IntAct=EBI-350723, EBI-25836582; CC P50454; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-350723, EBI-18063495; CC P50454; Q13200: PSMD2; NbExp=4; IntAct=EBI-350723, EBI-357648; CC P50454; P21246: PTN; NbExp=3; IntAct=EBI-350723, EBI-473725; CC P50454; Q13702-2: RAPSN; NbExp=3; IntAct=EBI-350723, EBI-22012855; CC P50454; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-350723, EBI-17589229; CC P50454; P61513: RPL37A; NbExp=3; IntAct=EBI-350723, EBI-356793; CC P50454; Q8NC51: SERBP1; NbExp=3; IntAct=EBI-350723, EBI-523558; CC P50454; Q16586: SGCA; NbExp=3; IntAct=EBI-350723, EBI-5663553; CC P50454; Q99720-4: SIGMAR1; NbExp=3; IntAct=EBI-350723, EBI-25831036; CC P50454; Q8NCS7: SLC44A5; NbExp=3; IntAct=EBI-350723, EBI-21504521; CC P50454; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-350723, EBI-12938570; CC P50454; Q7Z614-3: SNX20; NbExp=3; IntAct=EBI-350723, EBI-12336127; CC P50454; O43463: SUV39H1; NbExp=3; IntAct=EBI-350723, EBI-349968; CC P50454; P25490: YY1; NbExp=3; IntAct=EBI-350723, EBI-765538; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. CC -!- INDUCTION: By heat shock. CC -!- POLYMORPHISM: A functional SNP in the promoter of SERPINH1 is CC associated in African Americans with an increased risk for preterm CC premature rupture of membranes (PPROM) [MIM:610504]. PPROM is defined CC as rupture of the membranes before 37 weeks of gestation. SERPINH1 with CC the -656 T allele displays significantly reduced promoter activity CC compared to the major -656 C allele. Prematurity is correlated with an CC increased frequency of the -656 T allele. CC -!- DISEASE: Osteogenesis imperfecta 10 (OI10) [MIM:613848]: A form of CC osteogenesis imperfecta, a connective tissue disorder characterized by CC low bone mass, bone fragility and susceptibility to fractures after CC minimal trauma. Disease severity ranges from very mild forms without CC fractures to intrauterine fractures and perinatal lethality. CC Extraskeletal manifestations, which affect a variable number of CC patients, are dentinogenesis imperfecta, hearing loss, and blue CC sclerae. OI10 is an autosomal recessive form characterized by multiple CC bone deformities and fractures, generalized osteopenia, dentinogenesis CC imperfecta, and blue sclerae. {ECO:0000269|PubMed:20188343}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database; Note=The CC SERPINH1 gene homepage; CC URL="https://www.LOVD.nl/SERPINH1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X61598; CAA43795.1; -; mRNA. DR EMBL; D83174; BAA11829.1; -; mRNA. DR EMBL; AB044778; BAA96788.1; -; mRNA. DR EMBL; AB044779; BAA96789.1; -; mRNA. DR EMBL; AY744367; AAU95378.1; -; mRNA. DR EMBL; AY264853; AAP93914.1; -; mRNA. DR EMBL; BT007094; AAP35758.1; -; mRNA. DR EMBL; AK122936; BAG53805.1; -; mRNA. DR EMBL; CH471076; EAW74974.1; -; Genomic_DNA. DR EMBL; BC014623; AAH14623.1; -; mRNA. DR EMBL; BC036298; AAH36298.2; -; mRNA. DR EMBL; BC070087; AAH70087.1; -; mRNA. DR CCDS; CCDS8239.1; -. DR PIR; I52968; I52968. DR PIR; S20608; S20608. DR RefSeq; NP_001193943.1; NM_001207014.1. DR RefSeq; NP_001226.2; NM_001235.3. DR RefSeq; XP_011543629.1; XM_011545327.1. DR AlphaFoldDB; P50454; -. DR SMR; P50454; -. DR BioGRID; 107318; 299. DR IntAct; P50454; 143. DR MINT; P50454; -. DR STRING; 9606.ENSP00000434412; -. DR BindingDB; P50454; -. DR ChEMBL; CHEMBL5286; -. DR MEROPS; I04.035; -. DR MEROPS; I04.036; -. DR GlyConnect; 658; 26 N-Linked glycans (2 sites). DR GlyCosmos; P50454; 2 sites, 28 glycans. DR GlyGen; P50454; 6 sites, 28 N-linked glycans (2 sites), 1 O-linked glycan (4 sites). DR iPTMnet; P50454; -. DR MetOSite; P50454; -. DR PhosphoSitePlus; P50454; -. DR SwissPalm; P50454; -. DR BioMuta; SERPINH1; -. DR DMDM; 20141241; -. DR DOSAC-COBS-2DPAGE; P50454; -. DR CPTAC; CPTAC-272; -. DR CPTAC; CPTAC-273; -. DR EPD; P50454; -. DR jPOST; P50454; -. DR MassIVE; P50454; -. DR MaxQB; P50454; -. DR PaxDb; 9606-ENSP00000434412; -. DR PeptideAtlas; P50454; -. DR ProteomicsDB; 56229; -. DR Pumba; P50454; -. DR TopDownProteomics; P50454; -. DR Antibodypedia; 3838; 583 antibodies from 36 providers. DR DNASU; 871; -. DR Ensembl; ENST00000358171.8; ENSP00000350894.4; ENSG00000149257.16. DR Ensembl; ENST00000524558.5; ENSP00000434412.1; ENSG00000149257.16. DR Ensembl; ENST00000533603.5; ENSP00000434657.1; ENSG00000149257.16. DR GeneID; 871; -. DR KEGG; hsa:871; -. DR MANE-Select; ENST00000358171.8; ENSP00000350894.4; NM_001235.5; NP_001226.2. DR UCSC; uc001owr.4; human. DR AGR; HGNC:1546; -. DR CTD; 871; -. DR DisGeNET; 871; -. DR GeneCards; SERPINH1; -. DR HGNC; HGNC:1546; SERPINH1. DR HPA; ENSG00000149257; Low tissue specificity. DR MalaCards; SERPINH1; -. DR MIM; 600943; gene. DR MIM; 610504; phenotype. DR MIM; 613848; phenotype. DR neXtProt; NX_P50454; -. DR OpenTargets; ENSG00000149257; -. DR Orphanet; 216812; Osteogenesis imperfecta type 3. DR PharmGKB; PA35034; -. DR VEuPathDB; HostDB:ENSG00000149257; -. DR eggNOG; KOG2392; Eukaryota. DR GeneTree; ENSGT00940000156163; -. DR HOGENOM; CLU_023330_2_0_1; -. DR InParanoid; P50454; -. DR OMA; WDEKFHE; -. DR OrthoDB; 3218836at2759; -. DR PhylomeDB; P50454; -. DR TreeFam; TF343094; -. DR PathwayCommons; P50454; -. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR SignaLink; P50454; -. DR BioGRID-ORCS; 871; 11 hits in 1169 CRISPR screens. DR ChiTaRS; SERPINH1; human. DR GeneWiki; Heat_shock_protein_47; -. DR GenomeRNAi; 871; -. DR Pharos; P50454; Tbio. DR PRO; PR:P50454; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P50454; Protein. DR Bgee; ENSG00000149257; Expressed in stromal cell of endometrium and 190 other cell types or tissues. DR ExpressionAtlas; P50454; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IEA:InterPro. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0005518; F:collagen binding; NAS:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central. DR GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl. DR GO; GO:0003433; P:chondrocyte development involved in endochondral bone morphogenesis; IEA:Ensembl. DR GO; GO:0032964; P:collagen biosynthetic process; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central. DR GO; GO:0051604; P:protein maturation; IEA:Ensembl. DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc. DR CDD; cd02046; serpinH1_CBP1; 1. DR Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1. DR Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1. DR InterPro; IPR023795; Serpin_CS. DR InterPro; IPR023796; Serpin_dom. DR InterPro; IPR000215; Serpin_fam. DR InterPro; IPR033830; Serpin_H1_serpin_dom. DR InterPro; IPR036186; Serpin_sf. DR InterPro; IPR042178; Serpin_sf_1. DR InterPro; IPR042185; Serpin_sf_2. DR PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1. DR PANTHER; PTHR11461:SF27; SERPIN H1; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; Serpins; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00284; SERPIN; 1. DR UCD-2DPAGE; P50454; -. DR Genevisible; P50454; HS. PE 1: Evidence at protein level; KW Acetylation; Chaperone; Endoplasmic reticulum; Glycoprotein; KW Osteogenesis imperfecta; Phosphoprotein; Reference proteome; Signal; KW Stress response. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..418 FT /note="Serpin H1" FT /id="PRO_0000032520" FT MOTIF 415..418 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT SITE 377..378 FT /note="Reactive bond homolog" FT /evidence="ECO:0000250" FT MOD_RES 94 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P19324" FT MOD_RES 141 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 207 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P19324" FT MOD_RES 296 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P19324" FT MOD_RES 319 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P19324" FT CARBOHYD 120 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 125 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 41 FT /note="A -> P (in dbSNP:rs7105528)" FT /id="VAR_028445" FT VARIANT 78 FT /note="L -> P (in OI10; dbSNP:rs137853892)" FT /evidence="ECO:0000269|PubMed:20188343" FT /id="VAR_063602" FT CONFLICT 7..10 FT /note="LSAF -> GTL (in Ref. 1; CAA43795)" FT /evidence="ECO:0000305" FT CONFLICT 14..15 FT /note="EA -> AV (in Ref. 1; CAA43795)" FT /evidence="ECO:0000305" FT CONFLICT 25..26 FT /note="AA -> VE (in Ref. 1; CAA43795)" FT /evidence="ECO:0000305" FT CONFLICT 38 FT /note="P -> S (in Ref. 1; CAA43795)" FT /evidence="ECO:0000305" FT CONFLICT 41 FT /note="A -> T (in Ref. 1; CAA43795)" FT /evidence="ECO:0000305" FT CONFLICT 46..48 FT /note="RSA -> PST (in Ref. 1; CAA43795)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="R -> P (in Ref. 1; CAA43795)" FT /evidence="ECO:0000305" FT CONFLICT 168..169 FT /note="SA -> RP (in Ref. 2; BAA11829)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="M -> T (in Ref. 1; CAA43795)" FT /evidence="ECO:0000305" FT CONFLICT 255 FT /note="I -> L (in Ref. 1; CAA43795)" FT /evidence="ECO:0000305" FT CONFLICT 270 FT /note="L -> F (in Ref. 9; AAH70087)" FT /evidence="ECO:0000305" FT CONFLICT 409 FT /note="P -> L (in Ref. 1; CAA43795)" FT /evidence="ECO:0000305" SQ SEQUENCE 418 AA; 46441 MW; B7719FCA13A55DEB CRC64; MRSLLLLSAF CLLEAALAAE VKKPAAAAAP GTAEKLSPKA ATLAERSAGL AFSLYQAMAK DQAVENILVS PVVVASSLGL VSLGGKATTA SQAKAVLSAE QLRDEEVHAG LGELLRSLSN STARNVTWKL GSRLYGPSSV SFADDFVRSS KQHYNCEHSK INFRDKRSAL QSINEWAAQT TDGKLPEVTK DVERTDGALL VNAMFFKPHW DEKFHHKMVD NRGFMVTRSY TVGVMMMHRT GLYNYYDDEK EKLQIVEMPL AHKLSSLIIL MPHHVEPLER LEKLLTKEQL KIWMGKMQKK AVAISLPKGV VEVTHDLQKH LAGLGLTEAI DKNKADLSRM SGKKDLYLAS VFHATAFELD TDGNPFDQDI YGREELRSPK LFYADHPFIF LVRDTQSGSL LFIGRLVRPK GDKMRDEL //