CASK_HUMAN
ID CASK_HUMAN Reviewed; 182 AA.
AC P07498; Q13575;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Kappa-casein;
DE Flags: Precursor;
GN Name=CSN3; Synonyms=CASK, CSN10, CSNK;
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], AND VARIANT THR-145.
RA Menon R.S., Jeffers K.F., Chang Y.F., Ham R.G.;
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=1296818; DOI=10.3109/10425179209034024;
RA Bergstroem S., Hansson L., Hernell O., Loennerdal B., Nilsson A.K.,
RA Stroemqvist M.;
RT "Cloning and sequencing of human kappa-casein cDNA.";
RL DNA Seq. 3:245-246(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT LEU-110.
RX PubMed=8863730; DOI=10.1016/0378-1119(96)00351-4;
RA Edlund A., Johansson T., Leidvik B., Hansson L.;
RT "Structure of the human kappa-casein gene.";
RL Gene 174:65-69(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-75.
RC TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 25-182.
RX PubMed=4018271; DOI=10.1016/0014-5793(85)80872-3;
RA Brignon G., Chtourou A., Ribadeau-Dumas B.;
RT "Preparation and amino acid sequence of human kappa-casein.";
RL FEBS Lett. 188:48-54(1985).
RN [6]
RP PROTEIN SEQUENCE OF 118-182, AND GLYCOSYLATION AT THR-133; THR-143;
RP THR-148; THR-151; THR-157; THR-167 AND THR-169.
RX PubMed=7460900; DOI=10.1111/j.1432-1033.1980.tb04946.x;
RA Fiat A.-M., Jolles J., Aubert J.-P., Loucheux-Lefebvre M.H., Jolles P.;
RT "Localisation and importance of the sugar part of human casein.";
RL Eur. J. Biochem. 111:333-339(1980).
RN [7]
RP STRUCTURE BY NMR OF 108-125.
RX PubMed=10191473; DOI=10.1017/s0022029998003318;
RA Plowman J.E., Creamer L.K., Liddell M.J., Cross J.J.;
RT "Structural features of a peptide corresponding to human kappa-casein
RT residues 84-101 by 1H-nuclear magnetic resonance spectroscopy.";
RL J. Dairy Res. 66:53-63(1999).
CC -!- FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein
CC precipitation in milk.
CC -!- SUBUNIT: Heteromultimers composed of alpha-s1 casein and kappa casein
CC linked by disulfide bonds.
CC -!- INTERACTION:
CC P07498; Q93062: RBPMS; NbExp=4; IntAct=EBI-2602175, EBI-740322;
CC P07498; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-2602175, EBI-741480;
CC P07498; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-2602175, EBI-947187;
CC P07498; O95231: VENTX; NbExp=3; IntAct=EBI-2602175, EBI-10191303;
CC P07498; P36508: ZNF76; NbExp=3; IntAct=EBI-2602175, EBI-7254550;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the kappa-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";
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; M73628; AAA59456.1; -; mRNA.
DR EMBL; X66417; CAA47048.1; -; mRNA.
DR EMBL; U51899; AAC50772.1; -; Genomic_DNA.
DR EMBL; BC010935; AAH10935.1; -; mRNA.
DR CCDS; CCDS3538.1; -.
DR PIR; JC4957; KKHU.
DR RefSeq; NP_005203.2; NM_005212.2.
DR RefSeq; XP_011529922.1; XM_011531620.2.
DR RefSeq; XP_016863250.1; XM_017007761.1.
DR AlphaFoldDB; P07498; -.
DR BioGRID; 107835; 20.
DR IntAct; P07498; 9.
DR MINT; P07498; -.
DR STRING; 9606.ENSP00000304822; -.
DR ChEMBL; CHEMBL3621024; -.
DR DrugBank; DB12010; Fostamatinib.
DR Allergome; 1064; Hom s 8.
DR GlyConnect; 308; 11 O-Linked glycans.
DR GlyGen; P07498; 11 sites, 14 O-linked glycans (11 sites).
DR iPTMnet; P07498; -.
DR PhosphoSitePlus; P07498; -.
DR SwissPalm; P07498; -.
DR BioMuta; CSN3; -.
DR MassIVE; P07498; -.
DR PaxDb; P07498; -.
DR PeptideAtlas; P07498; -.
DR PRIDE; P07498; -.
DR ProteomicsDB; 52011; -.
DR TopDownProteomics; P07498; -.
DR Antibodypedia; 24320; 100 antibodies from 21 providers.
DR DNASU; 1448; -.
DR Ensembl; ENST00000304954.4; ENSP00000304822.3; ENSG00000171209.4.
DR Ensembl; ENST00000689459.1; ENSP00000508633.1; ENSG00000171209.4.
DR GeneID; 1448; -.
DR KEGG; hsa:1448; -.
DR MANE-Select; ENST00000304954.4; ENSP00000304822.3; NM_001394997.1; NP_001381926.1.
DR UCSC; uc003hfe.5; human.
DR CTD; 1448; -.
DR DisGeNET; 1448; -.
DR GeneCards; CSN3; -.
DR HGNC; HGNC:2446; CSN3.
DR HPA; ENSG00000171209; Tissue enriched (breast).
DR MIM; 601695; gene.
DR neXtProt; NX_P07498; -.
DR OpenTargets; ENSG00000171209; -.
DR PharmGKB; PA26949; -.
DR VEuPathDB; HostDB:ENSG00000171209; -.
DR eggNOG; ENOG502TM2T; Eukaryota.
DR GeneTree; ENSGT00390000009184; -.
DR HOGENOM; CLU_103388_0_0_1; -.
DR InParanoid; P07498; -.
DR OMA; HPSFIAI; -.
DR OrthoDB; 1540917at2759; -.
DR PhylomeDB; P07498; -.
DR TreeFam; TF338369; -.
DR PathwayCommons; P07498; -.
DR Reactome; R-HSA-5223345; Miscellaneous transport and binding events.
DR SignaLink; P07498; -.
DR BioGRID-ORCS; 1448; 12 hits in 1056 CRISPR screens.
DR ChiTaRS; CSN3; human.
DR GeneWiki; CSN3_(gene); -.
DR GenomeRNAi; 1448; -.
DR Pharos; P07498; Tbio.
DR PRO; PR:P07498; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P07498; protein.
DR Bgee; ENSG00000171209; Expressed in buccal mucosa cell and 63 other tissues.
DR Genevisible; P07498; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0007595; P:lactation; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR InterPro; IPR000117; Casein_kappa.
DR PANTHER; PTHR11470; PTHR11470; 1.
DR Pfam; PF00997; Casein_kappa; 1.
DR PIRSF; PIRSF002374; Casein_kappa; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Milk protein;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT CHAIN 21..182
FT /note="Kappa-casein"
FT /id="PRO_0000004498"
FT SITE 117..118
FT /note="Cleavage; by chymosin/rennin"
FT MOD_RES 157
FT /note="Phosphothreonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT CARBOHYD 133
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7460900"
FT CARBOHYD 143
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7460900"
FT CARBOHYD 148
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7460900"
FT CARBOHYD 151
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7460900"
FT CARBOHYD 157
FT /note="O-linked (GalNAc...) threonine; alternate"
FT /evidence="ECO:0000269|PubMed:7460900"
FT CARBOHYD 167
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7460900"
FT CARBOHYD 169
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7460900"
FT CARBOHYD 178
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02668"
FT VARIANT 75
FT /note="Y -> C (in dbSNP:rs17850702)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026338"
FT VARIANT 110
FT /note="R -> L (in dbSNP:rs1048152)"
FT /evidence="ECO:0000269|PubMed:8863730"
FT /id="VAR_026339"
FT VARIANT 145
FT /note="A -> T (in dbSNP:rs3775739)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_026340"
FT CONFLICT 25..27
FT /note="QKQ -> EQK (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="D -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="F -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="S -> T (in Ref. 5; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="T -> P (in Ref. 5; AA sequence and 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..181
FT /note="TPPT -> PTTS (in Ref. 5; AA sequence and 6; AA
FT sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 20305 MW; 8A1609D2D5C94895 CRC64;
MKSFLLVVNA LALTLPFLAV EVQNQKQPAC HENDERPFYQ KTAPYVPMYY VPNSYPYYGT
NLYQRRPAIA INNPYVPRTY YANPAVVRPH AQIPQRQYLP NSHPPTVVRR PNLHPSFIAI
PPKKIQDKII IPTINTIATV EPTPAPATEP TVDSVVTPEA FSESIITSTP ETTTVAVTPP
TA
