SERPH_HUMAN
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 03-AUG-2022, entry version 215.
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;
CC Note=Serpin H1 (SERPINH1);
CC URL="http://oi.gene.le.ac.uk/home.php?select_db=SERPINH1";
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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; 219.
DR IntAct; P50454; 122.
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 GlyGen; P50454; 3 sites, 28 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P50454; -.
DR MetOSite; P50454; -.
DR PhosphoSitePlus; P50454; -.
DR SwissPalm; P50454; -.
DR BioMuta; SERPINH1; -.
DR DMDM; 20141241; -.
DR DOSAC-COBS-2DPAGE; P50454; -.
DR UCD-2DPAGE; P50454; -.
DR CPTAC; CPTAC-272; -.
DR CPTAC; CPTAC-273; -.
DR EPD; P50454; -.
DR jPOST; P50454; -.
DR MassIVE; P50454; -.
DR MaxQB; P50454; -.
DR PaxDb; P50454; -.
DR PeptideAtlas; P50454; -.
DR PRIDE; P50454; -.
DR ProteomicsDB; 56229; -.
DR TopDownProteomics; P50454; -.
DR Antibodypedia; 3838; 532 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 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; 1124079at2759; -.
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 1089 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 188 other tissues.
DR ExpressionAtlas; P50454; baseline and differential.
DR Genevisible; P50454; HS.
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:0010951; P:negative regulation of endopeptidase activity; 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; -; 1.
DR Gene3D; 3.30.497.10; -; 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 InterPro; IPR033547; SERPINH1.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR PANTHER; PTHR11461:SF27; PTHR11461:SF27; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00284; SERPIN; 1.
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
