Full text data of A1BG
A1BG
[Confidence: low (only semi-automatic identification from reviews)]
Alpha-1B-glycoprotein (Alpha-1-B glycoprotein; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Alpha-1B-glycoprotein (Alpha-1-B glycoprotein; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P04217
ID A1BG_HUMAN Reviewed; 495 AA.
AC P04217; A8K052; Q68CK0; Q8IYJ6; Q96P39;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 133.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y.,
RA Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N.,
RA Nakagawara A.;
RT "Expression profiling and differential screening between
RT hepatoblastomas and the corresponding normal livers: identification of
RT high expression of the PLK1 oncogene as a poor-prognostic indicator of
RT 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
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA 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
RT project: 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
RT to the 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.,
RA Borregaard N., Kjeldsen L.;
RT "Cysteine-rich secretory protein 3 is a ligand of alpha1B-glycoprotein
RT in human plasma.";
RL Biochemistry 43:12877-12886(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44 AND ASN-179, AND MASS
RP SPECTROMETRY.
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, AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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, STRUCTURE OF
RP CARBOHYDRATES, AND MASS SPECTROMETRY.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
RA Brinkmalm G., Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
CC -!- SUBUNIT: Interacts with CRISP3.
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- SIMILARITY: Contains 5 Ig-like V-type (immunoglobulin-like)
CC domains.
CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC polymorphism database;
CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename;=alpha1B";
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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 RefSeq; NP_570602.2; NM_130786.3.
DR UniGene; Hs.529161; -.
DR UniGene; Hs.709582; -.
DR ProteinModelPortal; P04217; -.
DR SMR; P04217; 28-195, 208-492.
DR IntAct; P04217; 9.
DR MINT; MINT-8247347; -.
DR STRING; 9606.ENSP00000263100; -.
DR MEROPS; I43.950; -.
DR PhosphoSite; P04217; -.
DR DMDM; 46577680; -.
DR DOSAC-COBS-2DPAGE; P04217; -.
DR REPRODUCTION-2DPAGE; IPI00022895; -.
DR SWISS-2DPAGE; P04217; -.
DR PaxDb; P04217; -.
DR PeptideAtlas; P04217; -.
DR PRIDE; P04217; -.
DR Ensembl; ENST00000263100; ENSP00000263100; ENSG00000121410.
DR GeneID; 1; -.
DR KEGG; hsa:1; -.
DR UCSC; uc002qsd.4; human.
DR CTD; 1; -.
DR GeneCards; GC19M058858; -.
DR HGNC; HGNC:5; A1BG.
DR HPA; CAB016673; -.
DR MIM; 138670; gene.
DR neXtProt; NX_P04217; -.
DR PharmGKB; PA24356; -.
DR eggNOG; NOG26440; -.
DR HOGENOM; HOG000152502; -.
DR HOVERGEN; HBG000037; -.
DR InParanoid; P04217; -.
DR OMA; ATFPVHR; -.
DR OrthoDB; EOG78SQGZ; -.
DR PhylomeDB; P04217; -.
DR GeneWiki; A1BG_(gene); -.
DR GenomeRNAi; 1; -.
DR NextBio; 1; -.
DR PRO; PR:P04217; -.
DR ArrayExpress; P04217; -.
DR Bgee; P04217; -.
DR CleanEx; HS_A1BG; -.
DR Genevestigator; P04217; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR016332; A1B_glyco/leuk_Ig-like_rcpt.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003598; Ig_sub2.
DR PIRSF; PIRSF001979; Alpha_1B_glycoprot_prd; 1.
DR SMART; SM00408; IGc2; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Polymorphism;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 21
FT CHAIN 22 495 Alpha-1B-glycoprotein.
FT /FTId=PRO_0000014502.
FT DOMAIN 22 113 Ig-like V-type 1.
FT DOMAIN 114 206 Ig-like V-type 2.
FT DOMAIN 207 299 Ig-like V-type 3.
FT DOMAIN 300 397 Ig-like V-type 4.
FT DOMAIN 398 495 Ig-like V-type 5.
FT CARBOHYD 44 44 N-linked (GlcNAc...) (complex).
FT CARBOHYD 179 179 N-linked (GlcNAc...).
FT CARBOHYD 363 363 N-linked (GlcNAc...).
FT CARBOHYD 371 371 N-linked (GlcNAc...).
FT DISULFID 49 93 Probable.
FT DISULFID 139 182
FT DISULFID 232 279
FT DISULFID 325 374
FT DISULFID 423 470 Probable.
FT VAR_SEQ 1 122 Missing (in isoform 2).
FT /FTId=VSP_040323.
FT VARIANT 52 52 H -> R (in dbSNP:rs893184).
FT /FTId=VAR_018369.
FT VARIANT 395 395 H -> R (in dbSNP:rs2241788).
FT /FTId=VAR_018370.
FT CONFLICT 105 105 S -> G (in Ref. 2; AAL07469).
FT CONFLICT 127 127 S -> P (in Ref. 2; AAL07469).
FT CONFLICT 146 146 V -> E (in Ref. 2; AAL07469).
FT CONFLICT 304 304 E -> G (in Ref. 3; BAF82106).
FT CONFLICT 413 413 V -> A (in Ref. 2; AAL07469).
FT CONFLICT 446 447 VR -> IP (in Ref. 2; AAL07469).
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
//
ID A1BG_HUMAN Reviewed; 495 AA.
AC P04217; A8K052; Q68CK0; Q8IYJ6; Q96P39;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 133.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y.,
RA Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N.,
RA Nakagawara A.;
RT "Expression profiling and differential screening between
RT hepatoblastomas and the corresponding normal livers: identification of
RT high expression of the PLK1 oncogene as a poor-prognostic indicator of
RT 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
RP 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA 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
RT project: 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
RT to the 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.,
RA Borregaard N., Kjeldsen L.;
RT "Cysteine-rich secretory protein 3 is a ligand of alpha1B-glycoprotein
RT in human plasma.";
RL Biochemistry 43:12877-12886(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44 AND ASN-179, AND MASS
RP SPECTROMETRY.
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, AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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, STRUCTURE OF
RP CARBOHYDRATES, AND MASS SPECTROMETRY.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
RA Brinkmalm G., Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
CC -!- SUBUNIT: Interacts with CRISP3.
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- SIMILARITY: Contains 5 Ig-like V-type (immunoglobulin-like)
CC domains.
CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC polymorphism database;
CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename;=alpha1B";
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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 RefSeq; NP_570602.2; NM_130786.3.
DR UniGene; Hs.529161; -.
DR UniGene; Hs.709582; -.
DR ProteinModelPortal; P04217; -.
DR SMR; P04217; 28-195, 208-492.
DR IntAct; P04217; 9.
DR MINT; MINT-8247347; -.
DR STRING; 9606.ENSP00000263100; -.
DR MEROPS; I43.950; -.
DR PhosphoSite; P04217; -.
DR DMDM; 46577680; -.
DR DOSAC-COBS-2DPAGE; P04217; -.
DR REPRODUCTION-2DPAGE; IPI00022895; -.
DR SWISS-2DPAGE; P04217; -.
DR PaxDb; P04217; -.
DR PeptideAtlas; P04217; -.
DR PRIDE; P04217; -.
DR Ensembl; ENST00000263100; ENSP00000263100; ENSG00000121410.
DR GeneID; 1; -.
DR KEGG; hsa:1; -.
DR UCSC; uc002qsd.4; human.
DR CTD; 1; -.
DR GeneCards; GC19M058858; -.
DR HGNC; HGNC:5; A1BG.
DR HPA; CAB016673; -.
DR MIM; 138670; gene.
DR neXtProt; NX_P04217; -.
DR PharmGKB; PA24356; -.
DR eggNOG; NOG26440; -.
DR HOGENOM; HOG000152502; -.
DR HOVERGEN; HBG000037; -.
DR InParanoid; P04217; -.
DR OMA; ATFPVHR; -.
DR OrthoDB; EOG78SQGZ; -.
DR PhylomeDB; P04217; -.
DR GeneWiki; A1BG_(gene); -.
DR GenomeRNAi; 1; -.
DR NextBio; 1; -.
DR PRO; PR:P04217; -.
DR ArrayExpress; P04217; -.
DR Bgee; P04217; -.
DR CleanEx; HS_A1BG; -.
DR Genevestigator; P04217; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR016332; A1B_glyco/leuk_Ig-like_rcpt.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003598; Ig_sub2.
DR PIRSF; PIRSF001979; Alpha_1B_glycoprot_prd; 1.
DR SMART; SM00408; IGc2; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Polymorphism;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 21
FT CHAIN 22 495 Alpha-1B-glycoprotein.
FT /FTId=PRO_0000014502.
FT DOMAIN 22 113 Ig-like V-type 1.
FT DOMAIN 114 206 Ig-like V-type 2.
FT DOMAIN 207 299 Ig-like V-type 3.
FT DOMAIN 300 397 Ig-like V-type 4.
FT DOMAIN 398 495 Ig-like V-type 5.
FT CARBOHYD 44 44 N-linked (GlcNAc...) (complex).
FT CARBOHYD 179 179 N-linked (GlcNAc...).
FT CARBOHYD 363 363 N-linked (GlcNAc...).
FT CARBOHYD 371 371 N-linked (GlcNAc...).
FT DISULFID 49 93 Probable.
FT DISULFID 139 182
FT DISULFID 232 279
FT DISULFID 325 374
FT DISULFID 423 470 Probable.
FT VAR_SEQ 1 122 Missing (in isoform 2).
FT /FTId=VSP_040323.
FT VARIANT 52 52 H -> R (in dbSNP:rs893184).
FT /FTId=VAR_018369.
FT VARIANT 395 395 H -> R (in dbSNP:rs2241788).
FT /FTId=VAR_018370.
FT CONFLICT 105 105 S -> G (in Ref. 2; AAL07469).
FT CONFLICT 127 127 S -> P (in Ref. 2; AAL07469).
FT CONFLICT 146 146 V -> E (in Ref. 2; AAL07469).
FT CONFLICT 304 304 E -> G (in Ref. 3; BAF82106).
FT CONFLICT 413 413 V -> A (in Ref. 2; AAL07469).
FT CONFLICT 446 447 VR -> IP (in Ref. 2; AAL07469).
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
//
MIM
138670
*RECORD*
*FIELD* NO
138670
*FIELD* TI
*138670 ALPHA-1-B-GLYCOPROTEIN; A1BG
;;GAB;;
A1B;;
ABG
*FIELD* TX
The complete amino acid sequence of alpha-1B-glycoprotein, a plasma
read moreprotein of unknown function, was determined by Ishioka et al. (1986).
Sequence homology to immunoglobulins was recognized.
Alpha-1B-glycoprotein is present in normal adult plasma at an average
concentration of 22 mg/dl. Gahne et al. (1987) observed genetic
polymorphism of A1B using one-dimensional horizontal polyacrylamide gel
electrophoresis followed by Western blotting with specific antiserum.
Three different phenotypes, designated 1-1, 1-2, and 2-2, were observed.
Family data supported the hypothesis that the three phenotypes are
determined by 2 codominant alleles at an autosomal locus. In pigs the
homologous locus is linked to malignant hyperthermia (145600). Several
other linkages in pigs and in horses suggest that human chromosomes 19,
6, and 1 are 'candidate chromosomes' for bearing the human A1B. Juneja
et al. (1988) found a higher degree of A1B polymorphism in American
blacks than in Caucasian populations. They described new alleles. Eiberg
et al. (1989) reported exclusion data for localization of the
alpha-1B-glycoprotein gene polymorphism. Eiberg et al. (1989) found
linkage between A1BG and Lutheran blood group (111150); lod = 3.06 at
theta = 0.05 in males, and lod = 1.42 at theta = 0.10 in females. They
suggested that the most likely order of genes on chromosome 19 is
C3--SE--LU--A1BG.
*FIELD* SA
Eiberg et al. (1989)
*FIELD* RF
1. Eiberg, H.; Bisgaard, M. L.; Mohr, J.: Linkage between alpha-1-B-glycoprotein
(A1BG) and Lutheran (LU) red blood group system: assignment to chromosome
19: new genetic variants of A1BG. Clin. Genet. 36: 415-418, 1989.
2. Eiberg, H.; Nielsen, L. S.; Gahne, B.; Juneja, R. K.; Mohr, J.
: Exclusion data for the alpha-1-B glycoprotein (A1BG) polymorphism.
(Abstract) Cytogenet. Cell Genet. 51: 994 only, 1989.
3. Gahne, B.; Juneja, R. K.; Stratil, A.: Genetic polymorphism of
human plasma alpha-1-B-glycoprotein: phenotyping by immunoblotting
or by a simple method of 2-D electrophoresis. Hum. Genet. 76: 111-115,
1987.
4. Ishioka, N.; Takahashi, N.; Putnam, F. W.: Amino acid sequence
of human plasma alpha-1B-glycoprotein: homology to the immunoglobulin
supergene family. Proc. Nat. Acad. Sci. 83: 2363-2367, 1986.
5. Juneja, R. K.; Weitkamp, L. R.; Stratil, A.; Gahne, B.; Guttormsen,
S. A.: Further studies of the plasma alpha-1-B-glycoprotein polymorphism:
two new alleles and allele frequencies in Caucasians and in American
blacks. Hum. Hered. 38: 267-272, 1988.
*FIELD* CD
Victor A. McKusick: 6/25/1986
*FIELD* ED
alopez: 08/19/1998
supermim: 3/16/1992
supermim: 3/20/1990
supermim: 1/25/1990
supermim: 1/4/1990
ddp: 10/27/1989
*RECORD*
*FIELD* NO
138670
*FIELD* TI
*138670 ALPHA-1-B-GLYCOPROTEIN; A1BG
;;GAB;;
A1B;;
ABG
*FIELD* TX
The complete amino acid sequence of alpha-1B-glycoprotein, a plasma
read moreprotein of unknown function, was determined by Ishioka et al. (1986).
Sequence homology to immunoglobulins was recognized.
Alpha-1B-glycoprotein is present in normal adult plasma at an average
concentration of 22 mg/dl. Gahne et al. (1987) observed genetic
polymorphism of A1B using one-dimensional horizontal polyacrylamide gel
electrophoresis followed by Western blotting with specific antiserum.
Three different phenotypes, designated 1-1, 1-2, and 2-2, were observed.
Family data supported the hypothesis that the three phenotypes are
determined by 2 codominant alleles at an autosomal locus. In pigs the
homologous locus is linked to malignant hyperthermia (145600). Several
other linkages in pigs and in horses suggest that human chromosomes 19,
6, and 1 are 'candidate chromosomes' for bearing the human A1B. Juneja
et al. (1988) found a higher degree of A1B polymorphism in American
blacks than in Caucasian populations. They described new alleles. Eiberg
et al. (1989) reported exclusion data for localization of the
alpha-1B-glycoprotein gene polymorphism. Eiberg et al. (1989) found
linkage between A1BG and Lutheran blood group (111150); lod = 3.06 at
theta = 0.05 in males, and lod = 1.42 at theta = 0.10 in females. They
suggested that the most likely order of genes on chromosome 19 is
C3--SE--LU--A1BG.
*FIELD* SA
Eiberg et al. (1989)
*FIELD* RF
1. Eiberg, H.; Bisgaard, M. L.; Mohr, J.: Linkage between alpha-1-B-glycoprotein
(A1BG) and Lutheran (LU) red blood group system: assignment to chromosome
19: new genetic variants of A1BG. Clin. Genet. 36: 415-418, 1989.
2. Eiberg, H.; Nielsen, L. S.; Gahne, B.; Juneja, R. K.; Mohr, J.
: Exclusion data for the alpha-1-B glycoprotein (A1BG) polymorphism.
(Abstract) Cytogenet. Cell Genet. 51: 994 only, 1989.
3. Gahne, B.; Juneja, R. K.; Stratil, A.: Genetic polymorphism of
human plasma alpha-1-B-glycoprotein: phenotyping by immunoblotting
or by a simple method of 2-D electrophoresis. Hum. Genet. 76: 111-115,
1987.
4. Ishioka, N.; Takahashi, N.; Putnam, F. W.: Amino acid sequence
of human plasma alpha-1B-glycoprotein: homology to the immunoglobulin
supergene family. Proc. Nat. Acad. Sci. 83: 2363-2367, 1986.
5. Juneja, R. K.; Weitkamp, L. R.; Stratil, A.; Gahne, B.; Guttormsen,
S. A.: Further studies of the plasma alpha-1-B-glycoprotein polymorphism:
two new alleles and allele frequencies in Caucasians and in American
blacks. Hum. Hered. 38: 267-272, 1988.
*FIELD* CD
Victor A. McKusick: 6/25/1986
*FIELD* ED
alopez: 08/19/1998
supermim: 3/16/1992
supermim: 3/20/1990
supermim: 1/25/1990
supermim: 1/4/1990
ddp: 10/27/1989