CASB_HUMAN
ID CASB_HUMAN Reviewed; 226 AA.
AC P05814; Q4VAZ9; Q9UCM5;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 4.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Beta-casein;
DE Flags: Precursor;
GN Name=CSN2; Synonyms=CASB;
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].
RX PubMed=2387396; DOI=10.1016/0014-5793(90)81142-b;
RA Loennerdal B., Bergstroem S., Andersson Y., Hjalmarsson K., Sundqvist A.K.,
RA Hernell O.;
RT "Cloning and sequencing of a cDNA encoding human milk beta-casein.";
RL FEBS Lett. 269:153-156(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8112603; DOI=10.1016/0378-1119(94)90754-4;
RA Hansson L., Edlund A., Johansson T., Hernell O., Stroemqvist M.,
RA Lindquist S., Loennerdal B., Bergstroem S.;
RT "Structure of the human beta-casein encoding gene.";
RL Gene 139:193-199(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RA Menon R.S.;
RL Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RA Kwiatkowski D.J.;
RT "A high resolution linkage map of human 9q34.1.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 16-226, AND PHOSPHORYLATION AT THR-18; SER-21; SER-23;
RP SER-24 AND SER-25.
RX PubMed=6715339; DOI=10.1016/s0021-9258(17)42966-8;
RA Greenberg R., Groves M.L., Dower H.J.;
RT "Human beta-casein. Amino acid sequence and identification of
RT phosphorylation sites.";
RL J. Biol. Chem. 259:5132-5138(1984).
RN [7]
RP PROTEIN SEQUENCE OF 18-33, PHOSPHORYLATION AT THR-18; SER-21; SER-23;
RP SER-24 AND SER-25, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18847231; DOI=10.1021/pr800387s;
RA Poth A.G., Deeth H.C., Alewood P.F., Holland J.W.;
RT "Analysis of the human casein phosphoproteome by 2-D electrophoresis and
RT MALDI-TOF/TOF MS reveals new phosphoforms.";
RL J. Proteome Res. 7:5017-5027(2008).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 161-226.
RC TISSUE=Mammary gland;
RX PubMed=2717418; DOI=10.1093/nar/17.7.2869;
RA Menon R.S., Ham R.G.;
RT "Human beta-casein: partial cDNA sequence and apparent polymorphism.";
RL Nucleic Acids Res. 17:2869-2869(1989).
RN [9]
RP PROTEIN SEQUENCE OF 176-215.
RX PubMed=1369431; DOI=10.1271/bbb.56.1140;
RA Azuma N., Yamauchi K.;
RT "Plasmin cleavage of human beta-casein.";
RL Biosci. Biotechnol. Biochem. 56:1140-1141(1992).
CC -!- FUNCTION: Important role in determination of the surface properties of
CC the casein micelles.
CC -!- INTERACTION:
CC P05814; Q14192: FHL2; NbExp=4; IntAct=EBI-1642112, EBI-701903;
CC P05814; Q9UHD9: UBQLN2; NbExp=6; IntAct=EBI-1642112, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC -!- PTM: Form 1-P is phosphorylated once; half of the molecules are
CC phosphorylated on Ser-24, half on Ser-25. {ECO:0000269|PubMed:18847231,
CC ECO:0000269|PubMed:6715339}.
CC -!- SIMILARITY: Belongs to the beta-casein family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Of buttons, digestion and
CC glue - Issue 16 of November 2001;
CC URL="https://web.expasy.org/spotlight/back_issues/016";
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DR EMBL; X55739; CAA39270.1; -; mRNA.
DR EMBL; AF027807; AAC82978.1; -; Genomic_DNA.
DR EMBL; X17070; CAA34916.1; -; mRNA.
DR EMBL; BC069554; AAH69554.1; -; mRNA.
DR EMBL; BC096194; AAH96194.1; -; mRNA.
DR EMBL; BC096195; AAH96195.1; -; mRNA.
DR EMBL; BC096196; AAH96196.1; -; mRNA.
DR EMBL; BC096197; AAH96197.1; -; mRNA.
DR EMBL; X13766; CAA32017.1; -; mRNA.
DR CCDS; CCDS3532.1; -.
DR PIR; I53730; KBHU.
DR RefSeq; NP_001289699.1; NM_001302770.1.
DR RefSeq; NP_001882.1; NM_001891.3.
DR RefSeq; XP_016863249.1; XM_017007760.1.
DR AlphaFoldDB; P05814; -.
DR BioGRID; 107834; 43.
DR IntAct; P05814; 15.
DR MINT; P05814; -.
DR STRING; 9606.ENSP00000341030; -.
DR Allergome; 1064; Hom s 8.
DR iPTMnet; P05814; -.
DR PhosphoSitePlus; P05814; -.
DR BioMuta; CSN2; -.
DR DMDM; 115661; -.
DR MassIVE; P05814; -.
DR PaxDb; P05814; -.
DR PeptideAtlas; P05814; -.
DR PRIDE; P05814; -.
DR ProteomicsDB; 51861; -.
DR Antibodypedia; 24273; 219 antibodies from 24 providers.
DR DNASU; 1447; -.
DR Ensembl; ENST00000353151.4; ENSP00000341030.3; ENSG00000135222.7.
DR Ensembl; ENST00000635174.1; ENSP00000489488.1; ENSG00000283030.1.
DR GeneID; 1447; -.
DR KEGG; hsa:1447; -.
DR MANE-Select; ENST00000353151.4; ENSP00000341030.3; NM_001891.4; NP_001882.1.
DR CTD; 1447; -.
DR DisGeNET; 1447; -.
DR GeneCards; CSN2; -.
DR HGNC; HGNC:2447; CSN2.
DR HPA; ENSG00000135222; Tissue enriched (breast).
DR MIM; 115460; gene.
DR neXtProt; NX_P05814; -.
DR OpenTargets; ENSG00000135222; -.
DR PharmGKB; PA26950; -.
DR VEuPathDB; HostDB:ENSG00000135222; -.
DR eggNOG; ENOG502RU0R; Eukaryota.
DR GeneTree; ENSGT00390000001890; -.
DR HOGENOM; CLU_106775_0_0_1; -.
DR InParanoid; P05814; -.
DR OMA; LMHQIPQ; -.
DR OrthoDB; 1336883at2759; -.
DR PhylomeDB; P05814; -.
DR TreeFam; TF336929; -.
DR PathwayCommons; P05814; -.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
DR SignaLink; P05814; -.
DR BioGRID-ORCS; 1447; 10 hits in 1049 CRISPR screens.
DR GeneWiki; CSN2; -.
DR GenomeRNAi; 1447; -.
DR Pharos; P05814; Tbio.
DR PRO; PR:P05814; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P05814; protein.
DR Bgee; ENSG00000135222; Expressed in tonsil and 37 other tissues.
DR ExpressionAtlas; P05814; baseline and differential.
DR Genevisible; P05814; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:CAFA.
DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
DR GO; GO:0006816; P:calcium ion transport; TAS:ProtInc.
DR GO; GO:0007595; P:lactation; IDA:UniProtKB.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IDA:CAFA.
DR InterPro; IPR001588; Casein.
DR InterPro; IPR016345; Casein_beta.
DR InterPro; IPR031305; Casein_CS.
DR PANTHER; PTHR11500; PTHR11500; 1.
DR Pfam; PF00363; Casein; 1.
DR PIRSF; PIRSF002372; Beta-casein; 1.
DR PROSITE; PS00306; CASEIN_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Milk protein; Phosphoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:6715339"
FT CHAIN 16..226
FT /note="Beta-casein"
FT /evidence="ECO:0000269|PubMed:6715339"
FT /id="PRO_0000004475"
FT MOD_RES 18
FT /note="Phosphothreonine; in form 5-P"
FT /evidence="ECO:0000269|PubMed:18847231,
FT ECO:0000269|PubMed:6715339"
FT MOD_RES 21
FT /note="Phosphoserine; in form 4-P and form 5-P"
FT /evidence="ECO:0000269|PubMed:18847231,
FT ECO:0000269|PubMed:6715339"
FT MOD_RES 23
FT /note="Phosphoserine; in form 3-P, form 4-P and form 5-P"
FT /evidence="ECO:0000269|PubMed:18847231,
FT ECO:0000269|PubMed:6715339"
FT MOD_RES 24
FT /note="Phosphoserine; in form 1-P, form 2-P, form 3-P, form
FT 4-P and form 5-P"
FT /evidence="ECO:0000269|PubMed:18847231,
FT ECO:0000269|PubMed:6715339"
FT MOD_RES 25
FT /note="Phosphoserine; in form 1-P, form 2-P, form 3-P, form
FT 4-P and form 5-P"
FT /evidence="ECO:0000269|PubMed:18847231,
FT ECO:0000269|PubMed:6715339"
FT CONFLICT 30
FT /note="T -> P (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="Missing (in Ref. 1; CAA39270)"
FT /evidence="ECO:0000305"
FT CONFLICT 48..50
FT /note="EDE -> TDQ (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> Q (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="L -> V (in Ref. 3; CAA34916)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="H -> Q (in Ref. 3; CAA34916)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="L -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 182..184
FT /note="QVV -> EVL (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="Q -> V (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="T -> P (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..222
FT /note="TQPLAPVHN -> PEPSTTZABH (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 25382 MW; 2619C524EA1358E8 CRC64;
MKVLILACLV ALALARETIE SLSSSEESIT EYKQKVEKVK HEDQQQGEDE HQDKIYPSFQ
PQPLIYPFVE PIPYGFLPQN ILPLAQPAVV LPVPQPEIME VPKAKDTVYT KGRVMPVLKS
PTIPFFDPQI PKLTDLENLH LPLPLLQPLM QQVPQPIPQT LALPPQPLWS VPQPKVLPIP
QQVVPYPQRA VPVQALLLNQ ELLLNPTHQI YPVTQPLAPV HNPISV
