A1BG_HUMAN
ID A1BG_HUMAN Reviewed; 495 AA.
AC P04217; A8K052; Q68CK0; Q8IYJ6; Q96P39;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Alpha-1B-glycoprotein;
DE AltName: Full=Alpha-1-B glycoprotein;
DE Flags: Precursor;
GN Name=A1BG;
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] (ISOFORM 1).
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-52.
RA Zhao Y., Sun D.;
RT "Molecular cloning and characterization of the human A1BG gene.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-52.
RC TISSUE=Mammary 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
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 [6]
RP PROTEIN SEQUENCE OF 22-495, DISULFIDE BONDS, GLYCOSYLATION AT ASN-44;
RP ASN-179; ASN-363 AND ASN-371, AND VARIANT ARG-52.
RX PubMed=3458201; DOI=10.1073/pnas.83.8.2363;
RA Ishioka N., Takahashi N., Putnam F.W.;
RT "Amino acid sequence of human plasma alpha 1B-glycoprotein: homology to the
RT immunoglobulin supergene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2363-2367(1986).
RN [7]
RP INTERACTION WITH CRISP3.
RX PubMed=15461460; DOI=10.1021/bi048823e;
RA Udby L., Sorensen O.E., Pass J., Johnsen A.H., Behrendt N., Borregaard N.,
RA Kjeldsen L.;
RT "Cysteine-rich secretory protein 3 is a ligand of alpha1B-glycoprotein in
RT human plasma.";
RL Biochemistry 43:12877-12886(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44 AND ASN-179.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44; ASN-179; ASN-363 AND
RP ASN-371.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44, AND STRUCTURE OF
RP CARBOHYDRATES.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [11]
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).
CC -!- SUBUNIT: Interacts with CRISP3. {ECO:0000269|PubMed:15461460}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04217-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04217-2; Sequence=VSP_040323;
CC -!- TISSUE SPECIFICITY: Plasma.
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DR EMBL; AB073611; BAD38648.1; -; mRNA.
DR EMBL; AF414429; AAL07469.1; -; mRNA.
DR EMBL; AK289417; BAF82106.1; -; mRNA.
DR EMBL; AC010642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035719; AAH35719.1; -; mRNA.
DR CCDS; CCDS12976.1; -. [P04217-1]
DR RefSeq; NP_570602.2; NM_130786.3. [P04217-1]
DR AlphaFoldDB; P04217; -.
DR SMR; P04217; -.
DR BioGRID; 106523; 33.
DR IntAct; P04217; 19.
DR MINT; P04217; -.
DR STRING; 9606.ENSP00000263100; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR MEROPS; I43.950; -.
DR GlyConnect; 780; 9 N-Linked glycans (4 sites).
DR GlyGen; P04217; 5 sites, 24 N-linked glycans (4 sites), 2 O-linked glycans (1 site).
DR iPTMnet; P04217; -.
DR PhosphoSitePlus; P04217; -.
DR BioMuta; A1BG; -.
DR DMDM; 317373553; -.
DR DOSAC-COBS-2DPAGE; P04217; -.
DR REPRODUCTION-2DPAGE; IPI00022895; -.
DR SWISS-2DPAGE; P04217; -.
DR CPTAC; non-CPTAC-1064; -.
DR jPOST; P04217; -.
DR MassIVE; P04217; -.
DR PaxDb; P04217; -.
DR PeptideAtlas; P04217; -.
DR PRIDE; P04217; -.
DR ProteomicsDB; 51684; -. [P04217-1]
DR ProteomicsDB; 51685; -. [P04217-2]
DR Antibodypedia; 3284; 448 antibodies from 37 providers.
DR Ensembl; ENST00000263100.8; ENSP00000263100.2; ENSG00000121410.12. [P04217-1]
DR GeneID; 1; -.
DR KEGG; hsa:1; -.
DR MANE-Select; ENST00000263100.8; ENSP00000263100.2; NM_130786.4; NP_570602.2.
DR CTD; 1; -.
DR DisGeNET; 1; -.
DR GeneCards; A1BG; -.
DR HGNC; HGNC:5; A1BG.
DR HPA; ENSG00000121410; Tissue enriched (liver).
DR MIM; 138670; gene.
DR neXtProt; NX_P04217; -.
DR OpenTargets; ENSG00000121410; -.
DR PharmGKB; PA24356; -.
DR VEuPathDB; HostDB:ENSG00000121410; -.
DR eggNOG; ENOG502RYEX; Eukaryota.
DR GeneTree; ENSGT01050000244944; -.
DR HOGENOM; CLU_042929_1_0_1; -.
DR InParanoid; P04217; -.
DR OMA; RCRYRSW; -.
DR OrthoDB; 227725at2759; -.
DR PhylomeDB; P04217; -.
DR TreeFam; TF336644; -.
DR PathwayCommons; P04217; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P04217; -.
DR BioGRID-ORCS; 1; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; A1BG; human.
DR GeneWiki; A1BG_(gene); -.
DR GenomeRNAi; 1; -.
DR Pharos; P04217; Tbio.
DR PRO; PR:P04217; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P04217; protein.
DR Bgee; ENSG00000121410; Expressed in right lobe of liver and 92 other tissues.
DR ExpressionAtlas; P04217; baseline and differential.
DR Genevisible; P04217; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR016332; A1B_glyco/leuk_Ig-like_rcpt.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 1.
DR PIRSF; PIRSF001979; Alpha_1B_glycoprot_prd; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:3458201"
FT CHAIN 22..495
FT /note="Alpha-1B-glycoprotein"
FT /id="PRO_0000014502"
FT DOMAIN 22..113
FT /note="Ig-like V-type 1"
FT DOMAIN 114..206
FT /note="Ig-like V-type 2"
FT DOMAIN 207..299
FT /note="Ig-like V-type 3"
FT DOMAIN 300..397
FT /note="Ig-like V-type 4"
FT DOMAIN 398..495
FT /note="Ig-like V-type 5"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19838169,
FT ECO:0000269|PubMed:3458201"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3458201"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:3458201"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:3458201"
FT DISULFID 49..93
FT /evidence="ECO:0000305|PubMed:3458201"
FT DISULFID 139..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:3458201"
FT DISULFID 232..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:3458201"
FT DISULFID 325..374
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:3458201"
FT DISULFID 423..470
FT /evidence="ECO:0000305|PubMed:3458201"
FT VAR_SEQ 1..122
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040323"
FT VARIANT 52
FT /note="H -> R (in dbSNP:rs893184)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:3458201, ECO:0000269|Ref.2"
FT /id="VAR_018369"
FT VARIANT 395
FT /note="H -> R (in dbSNP:rs2241788)"
FT /id="VAR_018370"
FT CONFLICT 105
FT /note="S -> G (in Ref. 2; AAL07469)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="S -> P (in Ref. 2; AAL07469)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="V -> E (in Ref. 2; AAL07469)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="E -> G (in Ref. 3; BAF82106)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="V -> A (in Ref. 2; AAL07469)"
FT /evidence="ECO:0000305"
FT CONFLICT 446..447
FT /note="VR -> IP (in Ref. 2; AAL07469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 54254 MW; 8E611BDC3BC824C8 CRC64;
MSMLVVFLLL WGVTWGPVTE AAIFYETQPS LWAESESLLK PLANVTLTCQ AHLETPDFQL
FKNGVAQEPV HLDSPAIKHQ FLLTGDTQGR YRCRSGLSTG WTQLSKLLEL TGPKSLPAPW
LSMAPVSWIT PGLKTTAVCR GVLRGVTFLL RREGDHEFLE VPEAQEDVEA TFPVHQPGNY
SCSYRTDGEG ALSEPSATVT IEELAAPPPP VLMHHGESSQ VLHPGNKVTL TCVAPLSGVD
FQLRRGEKEL LVPRSSTSPD RIFFHLNAVA LGDGGHYTCR YRLHDNQNGW SGDSAPVELI
LSDETLPAPE FSPEPESGRA LRLRCLAPLE GARFALVRED RGGRRVHRFQ SPAGTEALFE
LHNISVADSA NYSCVYVDLK PPFGGSAPSE RLELHVDGPP PRPQLRATWS GAVLAGRDAV
LRCEGPIPDV TFELLREGET KAVKTVRTPG AAANLELIFV GPQHAGNYRC RYRSWVPHTF
ESELSDPVEL LVAES
