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Protein

Alpha-S1-casein

Gene

CSN1S1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important role in the capacity of milk to transport calcium phosphate.
Casoxin D acts as opioid antagonist and has vasorelaxing activity mediated by bradykinin B1 receptors.

GO - Molecular functioni

  1. transporter activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Milk protein

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-S1-casein
Cleaved into the following chain:
Gene namesi
Name:CSN1S1
Synonyms:CASA, CSN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:2445. CSN1S1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26948.

Protein family/group databases

Allergomei1064. Hom s 8.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 15152 PublicationsAdd
BLAST
Chaini16 – 185170Alpha-S1-caseinPRO_0000004450Add
BLAST
Peptidei158 – 1647Casoxin-DPRO_0000004451

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphoserine1 Publication
Modified residuei33 – 331Phosphoserine3 Publications
Modified residuei41 – 411Phosphoserine4 Publications
Modified residuei71 – 711PhosphoserineBy similarity
Modified residuei86 – 861Phosphoserine1 Publication
Modified residuei88 – 881Phosphoserine2 Publications
Modified residuei89 – 891Phosphoserine1 Publication
Modified residuei90 – 901Phosphoserine2 Publications
Modified residuei91 – 911Phosphoserine1 Publication

Post-translational modificationi

Not glycosylated.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP47710.
PRIDEiP47710.

PTM databases

PhosphoSiteiP47710.

Miscellaneous databases

PMAP-CutDBP47710.

Expressioni

Tissue specificityi

Mammary gland specific. Secreted in milk.

Gene expression databases

BgeeiP47710.
CleanExiHS_CSN1S1.
ExpressionAtlasiP47710. baseline.
GenevestigatoriP47710.

Organism-specific databases

HPAiHPA035659.

Interactioni

Subunit structurei

Heteromultimers of alpha-s1 casein and kappa-casein; disulfide-linked.

Protein-protein interaction databases

BioGridi107833. 12 interactions.
IntActiP47710. 2 interactions.
STRINGi9606.ENSP00000246891.

Structurei

3D structure databases

ProteinModelPortaliP47710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alpha-casein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG73245.
GeneTreeiENSGT00390000017378.
HOGENOMiHOG000115954.
HOVERGENiHBG005242.
InParanoidiP47710.
KOiK17281.
OMAiSKCAEQF.
OrthoDBiEOG7W1561.
PhylomeDBiP47710.
TreeFamiTF340763.

Family and domain databases

InterProiIPR026999. Alpha-s1_casein.
IPR001588. Casein.
[Graphical view]
PANTHERiPTHR10240. PTHR10240. 1 hit.
PROSITEiPS00306. CASEIN_ALPHA_BETA. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P47710-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRLLILTCLV AVALARPKLP LRYPERLQNP SESSEPIPLE SREEYMNGMN
60 70 80 90 100
RQRNILREKQ TDEIKDTRNE STQNCVVAEP EKMESSISSS SEEMSLSKCA
110 120 130 140 150
EQFCRLNEYN QLQLQAAHAQ EQIRRMNENS HVQVPFQQLN QLAAYPYAVW
160 170 180
YYPQIMQYVP FPPFSDISNP TAHENYEKNN VMLQW
Length:185
Mass (Da):21,671
Last modified:January 31, 1996 - v1
Checksum:iA7717899CDC7D563
GO
Isoform 2 (identifier: P47710-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     52-52: Missing.

Show »
Length:184
Mass (Da):21,543
Checksum:i9427BB3C275D7B86
GO
Isoform 3 (identifier: P47710-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     66-73: Missing.

Show »
Length:177
Mass (Da):20,740
Checksum:iCF67025C444CC8CF
GO
Isoform 4 (identifier: P47710-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     52-52: Missing.
     93-100: Missing.

Show »
Length:176
Mass (Da):20,693
Checksum:i1E03F910FA37C369
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801P → S in AAY68392 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti117 – 1171A → V.1 Publication
Corresponds to variant rs10030475 [ dbSNP | Ensembl ].
VAR_048614

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei52 – 521Missing in isoform 2 and isoform 4. 3 PublicationsVSP_000795
Alternative sequencei66 – 738Missing in isoform 3. 2 PublicationsVSP_000796
Alternative sequencei93 – 1008Missing in isoform 4. 1 PublicationVSP_046130

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78416 mRNA. Translation: CAA55185.1.
U23157 mRNA. Translation: AAA69477.1.
DQ064604 mRNA. Translation: AAY68392.1.
AC108941 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05599.1.
BC128227 mRNA. Translation: AAI28228.1.
BC128228 mRNA. Translation: AAI28229.1.
X98084 mRNA. Translation: CAA66708.1.
CCDSiCCDS47067.1. [P47710-1]
CCDS54769.1. [P47710-4]
PIRiS56013.
RefSeqiNP_001020275.1. NM_001025104.1. [P47710-4]
NP_001881.1. NM_001890.1. [P47710-1]
XP_006714152.1. XM_006714089.1. [P47710-2]
XP_006714153.1. XM_006714090.1. [P47710-3]
UniGeneiHs.3155.

Genome annotation databases

EnsembliENST00000246891; ENSP00000246891; ENSG00000126545. [P47710-1]
ENST00000444405; ENSP00000413157; ENSG00000126545. [P47710-4]
ENST00000507763; ENSP00000422611; ENSG00000126545. [P47710-4]
GeneIDi1446.
KEGGihsa:1446.
UCSCiuc003hep.1. human. [P47710-1]
uc003heq.1. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

Of buttons, digestion and glue - Issue 16 of November 2001

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78416 mRNA. Translation: CAA55185.1.
U23157 mRNA. Translation: AAA69477.1.
DQ064604 mRNA. Translation: AAY68392.1.
AC108941 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05599.1.
BC128227 mRNA. Translation: AAI28228.1.
BC128228 mRNA. Translation: AAI28229.1.
X98084 mRNA. Translation: CAA66708.1.
CCDSiCCDS47067.1. [P47710-1]
CCDS54769.1. [P47710-4]
PIRiS56013.
RefSeqiNP_001020275.1. NM_001025104.1. [P47710-4]
NP_001881.1. NM_001890.1. [P47710-1]
XP_006714152.1. XM_006714089.1. [P47710-2]
XP_006714153.1. XM_006714090.1. [P47710-3]
UniGeneiHs.3155.

3D structure databases

ProteinModelPortaliP47710.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107833. 12 interactions.
IntActiP47710. 2 interactions.
STRINGi9606.ENSP00000246891.

Protein family/group databases

Allergomei1064. Hom s 8.

PTM databases

PhosphoSiteiP47710.

Proteomic databases

PaxDbiP47710.
PRIDEiP47710.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000246891; ENSP00000246891; ENSG00000126545. [P47710-1]
ENST00000444405; ENSP00000413157; ENSG00000126545. [P47710-4]
ENST00000507763; ENSP00000422611; ENSG00000126545. [P47710-4]
GeneIDi1446.
KEGGihsa:1446.
UCSCiuc003hep.1. human. [P47710-1]
uc003heq.1. human.

Organism-specific databases

CTDi1446.
GeneCardsiGC04P070845.
HGNCiHGNC:2445. CSN1S1.
HPAiHPA035659.
MIMi115450. gene.
neXtProtiNX_P47710.
PharmGKBiPA26948.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG73245.
GeneTreeiENSGT00390000017378.
HOGENOMiHOG000115954.
HOVERGENiHBG005242.
InParanoidiP47710.
KOiK17281.
OMAiSKCAEQF.
OrthoDBiEOG7W1561.
PhylomeDBiP47710.
TreeFamiTF340763.

Miscellaneous databases

GeneWikiiCSN1S1.
GenomeRNAii1446.
NextBioi5941.
PMAP-CutDBP47710.
PROiP47710.
SOURCEiSearch...

Gene expression databases

BgeeiP47710.
CleanExiHS_CSN1S1.
ExpressionAtlasiP47710. baseline.
GenevestigatoriP47710.

Family and domain databases

InterProiIPR026999. Alpha-s1_casein.
IPR001588. Casein.
[Graphical view]
PANTHERiPTHR10240. PTHR10240. 1 hit.
PROSITEiPS00306. CASEIN_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of three types of human alpha s1-casein mRNA transcripts."
    Johnsen L.B., Rasmussen L.K., Petersen T.E., Berglund L.
    Biochem. J. 309:237-242(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Mammary gland.
  2. Yu D.Y., Jeong S., Lee K.K., Lonnerdal B.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  3. Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Wen S., Li H., Yang S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-117.
  7. "The gene encoding alpha s1-casein is expressed in human mammary epithelial cells during lactation."
    Martin P., Brignon G., Furet J.-P., Leroux C.
    Lait 76:525-537(1995)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-185 (ISOFORMS 1; 2 AND 3).
  8. "Human alpha S1-casein like protein: purification and N-terminal sequence determination."
    Cavaletto M., Cantisani A., Giuffrida G., Napolitano L., Conti A.
    Biol. Chem. Hoppe-Seyler 375:149-151(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-29.
  9. "Human alpha s1-casein: purification and characterization."
    Rasmussen L.K., Due H.A., Petersen T.E.
    Comp. Biochem. Physiol. 111B:75-81(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-29 AND 99-105, CHARACTERIZATION.
  10. "On studying protein phosphorylation patterns using bottom-up LC-MS/MS: the case of human alpha-casein."
    Kjeldsen F., Savitski M.M., Nielsen M.L., Shi L., Zubarev R.A.
    Analyst 132:768-776(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-42 AND 83-98, PHOSPHORYLATION AT SER-33; SER-41; SER-88 AND SER-90, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Analysis of the human casein phosphoproteome by 2-D electrophoresis and MALDI-TOF/TOF MS reveals new phosphoforms."
    Poth A.G., Deeth H.C., Alewood P.F., Holland J.W.
    J. Proteome Res. 7:5017-5027(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-48, PHOSPHORYLATION AT SER-31; SER-33; SER-41; SER-86; SER-88; SER-89; SER-90 AND SER-91, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "The phosphorylation pattern of human alphas1-casein is markedly different from the ruminant species."
    Sorensen E.S., Moller L., Vinther M., Petersen T.E., Rasmussen L.K.
    Eur. J. Biochem. 270:3651-3655(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-33 AND SER-41, LACK OF GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "Genomic organization and chromosomal localization of the human casein gene family."
    Fujiwara Y., Miwa M., Nogami M., Okumura K., Nobori T., Suzuki T., Ueda M.
    Hum. Genet. 99:368-373(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOMIC ORGANIZATION, CHROMOSOMAL LOCATION.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiCASA1_HUMAN
AccessioniPrimary (citable) accession number: P47710
Secondary accession number(s): A1A510
, A1A511, E9PB60, Q4PNR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1996
Last sequence update: January 31, 1996
Last modified: March 3, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

In milk, the alpha s1- and beta-caseins precipitate in presence of calcium (so-called calcium-sensitive caseins). Kappa-casein prevents the precipitation of the other caseins by calcium through the formation of large stable colloidal particles termed micelles.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.