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P10598 (CASB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-casein
Gene names
Name:Csn2
Synonyms:Csnb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Important role in determination of the surface properties of the casein micelles.

Subcellular location

Secreted.

Tissue specificity

Mammary gland specific. Secreted in milk.

Sequence similarities

Belongs to the beta-casein family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionMilk protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from direct assay PubMed 16106354PubMed 16698927. Source: MGI

   Molecular_functiontransporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 By similarity
Chain16 – 231216Beta-casein
PRO_0000004477

Amino acid modifications

Modified residue231Phosphoserine By similarity
Modified residue261Phosphothreonine By similarity
Modified residue281Phosphoserine By similarity
Modified residue301Phosphoserine By similarity
Modified residue311Phosphoserine By similarity

Experimental info

Sequence conflict31V → T in AAH19189. Ref.5
Sequence conflict411Missing in BAB32374. Ref.4
Sequence conflict411Missing in BAB32375. Ref.4
Sequence conflict411Missing in AAH19114. Ref.5
Sequence conflict411Missing in AAH19189. Ref.5
Sequence conflict1451S → C in BAB32374. Ref.4
Sequence conflict1561Q → R in AAH13332. Ref.5
Sequence conflict165 – 1662VV → GG in BAB32375. Ref.4
Sequence conflict1921L → V in BAB32374. Ref.4
Sequence conflict2181T → P in BAB32374. Ref.4
Sequence conflict2181T → P in BAB32375. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P10598 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 7DD7DFF0766A9422

FASTA23125,337
        10         20         30         40         50         60 
MKVFILACLV ALALARETTF TVSSETDSIS SEESVEHINE QKLQKVNLMG QLQAEDVLQA 

        70         80         90        100        110        120 
KVHSSIQSQP QAFPYAQAQT ISCNPVPQNI QPIAQPPVVP SLGPVISPEL ESFLKAKATI 

       130        140        150        160        170        180 
LPKHKQMPLL NSETVLRLIN SQIPSLASLA NLHLPQSLVQ LLAQVVQAFP QTHLVSSQTQ 

       190        200        210        220        230 
LSLPQSKVLY FLQQVAPFLP QDMSVQDLLQ YLELLNPTVQ FPATPQHSVS V 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a cDNA encoding mouse beta casein."
Yoshimura M., Banerjee M.R., Oka T.
Nucleic Acids Res. 14:8224-8224(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation and structural analysis of the mouse beta-casein gene."
Yoshimura M., Oka T.
Gene 78:267-275(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Transfection of beta-casein chimeric gene and hormonal induction of its expression in primary murine mammary epithelial cells."
Yoshimura M., Oka T.
Proc. Natl. Acad. Sci. U.S.A. 87:3670-3674(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C3H/HeN.
Tissue: Liver.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[5]"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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04490 mRNA. Translation: CAA28178.1.
X13484 Genomic DNA. Translation: CAA31840.1.
AK021324 mRNA. Translation: BAB32374.1.
AK021328 mRNA. Translation: BAB32375.1.
AK052803 mRNA. Translation: BAC35152.1.
AK052805 mRNA. Translation: BAC35153.1.
AK085694 mRNA. Translation: BAC39508.1.
AK085729 mRNA. Translation: BAC39522.1.
AK142616 mRNA. Translation: BAE25131.1.
AK142620 mRNA. Translation: BAE25133.1.
AK142635 mRNA. Translation: BAE25141.1.
AK164747 mRNA. Translation: BAE37898.1.
AK164791 mRNA. Translation: BAE37917.1.
AK164792 mRNA. Translation: BAE37918.1.
AK164793 mRNA. Translation: BAE37919.1.
AK164794 mRNA. Translation: BAE37920.1.
BC013332 mRNA. Translation: AAH13332.1.
BC019114 mRNA. Translation: AAH19114.1.
BC019189 mRNA. Translation: AAH19189.1.
BC021153 mRNA. Translation: AAH21153.1.
PIRJU0061.
RefSeqNP_001272949.1. NM_001286020.1.
NP_001272950.1. NM_001286021.1.
NP_001272952.1. NM_001286023.1.
NP_034102.1. NM_009972.2.
UniGeneMm.268737.

3D structure databases

ProteinModelPortalP10598.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198938. 2 interactions.

PTM databases

PhosphoSiteP10598.

Proteomic databases

PaxDbP10598.
PRIDEP10598.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000082370; ENSMUSP00000080976; ENSMUSG00000063157.
GeneID12991.
KEGGmmu:12991.
UCSCuc008xyu.1. mouse.

Organism-specific databases

CTD1447.
MGIMGI:88541. Csn2.

Phylogenomic databases

eggNOGNOG45871.
GeneTreeENSGT00390000001890.
HOVERGENHBG004973.
InParanoidP10598.
KOK17107.
OMAEIMEVPK.
OrthoDBEOG7W6WP2.
PhylomeDBP10598.
TreeFamTF336929.

Gene expression databases

BgeeP10598.
CleanExMM_CSN2.
GenevestigatorP10598.

Family and domain databases

InterProIPR001588. Casein.
IPR016345. Casein_beta.
[Graphical view]
PANTHERPTHR11500. PTHR11500. 1 hit.
PfamPF00363. Casein. 1 hit.
[Graphical view]
PIRSFPIRSF002372. Beta-casein. 1 hit.
PROSITEPS00306. CASEIN_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCSN2. mouse.
NextBio282788.
PROP10598.
SOURCESearch...

Entry information

Entry nameCASB_MOUSE
AccessionPrimary (citable) accession number: P10598
Secondary accession number(s): Q543D9 expand/collapse secondary AC list , Q8VCT6, Q8VCU8, Q91VI5, Q922Y5, Q9D1U6, Q9D1U7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot