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Protein

Centrosomal protein of 57 kDa

Gene

Cep57

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Centrosomal protein which may be required for microtubule attachment to centrosomes. May act by forming ring-like structures around microtubules. Mediates nuclear translocation and mitogenic activity of the internalized growth factor FGF2.2 Publications

GO - Molecular functioni

  • fibroblast growth factor binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • microtubule anchoring Source: InterPro
  • mitotic sister chromatid segregation Source: GO_Central
  • protein homooligomerization Source: UniProtKB
  • protein import into nucleus, translocation Source: UniProtKB
  • spermatid development Source: HGNC
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Centrosomal protein of 57 kDa
Short name:
Cep57
Alternative name(s):
Testis-specific protein 57
Translokin
Gene namesi
Name:Cep57
Synonyms:Kiaa0092, Tsp57
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1915551. Cep57.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: MGI
  • Golgi apparatus Source: MGI
  • microtubule Source: UniProtKB
  • microtubule cytoskeleton Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 500500Centrosomal protein of 57 kDaPRO_0000189533Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8CEE0.
MaxQBiQ8CEE0.
PaxDbiQ8CEE0.
PRIDEiQ8CEE0.

PTM databases

iPTMnetiQ8CEE0.
PhosphoSiteiQ8CEE0.

Expressioni

Tissue specificityi

Ubiquitous (at protein level). Expressed in testis, predominantly in round spermatids. Low expression is detected in other tissues.2 Publications

Gene expression databases

BgeeiQ8CEE0.
CleanExiMM_CEP57.
ExpressionAtlasiQ8CEE0. baseline and differential.
GenevisibleiQ8CEE0. MM.

Interactioni

Subunit structurei

Interacts with FGF2 and RAP80. Does not interact with FGF1 or FGF2 isoform 24 kDa (By similarity). Homodimer and homooligomer. Interacts with microtubules.By similarity2 Publications

GO - Molecular functioni

  • fibroblast growth factor binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi216689. 1 interaction.
STRINGi10090.ENSMUSP00000034398.

Structurei

3D structure databases

ProteinModelPortaliQ8CEE0.
SMRiQ8CEE0. Positions 355-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 239182centrosome localization domain (CLD)Add
BLAST
Regioni278 – 491214Mediates interaction with microtubulesAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili63 – 242180Sequence analysisAdd
BLAST
Coiled coili389 – 44961Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi259 – 2668Poly-Lys

Domaini

The C-terminal region mediates the interaction with microtubules and is able to nucleate and bundles microtubules in vitro.1 Publication
The centrosome localization domain (CLD) region mediates the localization to centrosomes and homooligomerization.1 Publication

Sequence similaritiesi

Belongs to the translokin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IESE. Eukaryota.
ENOG410XPJC. LUCA.
GeneTreeiENSGT00530000063695.
HOVERGENiHBG050917.
InParanoidiQ8CEE0.
KOiK16762.
OMAiCNDRVIN.
PhylomeDBiQ8CEE0.
TreeFamiTF329178.

Family and domain databases

InterProiIPR010597. Centrosomal_protein_57kDa.
IPR025913. Cep57_CLD.
IPR024957. Cep57_MT-bd_dom.
[Graphical view]
PANTHERiPTHR19336:SF11. PTHR19336:SF11. 1 hit.
PfamiPF14073. Cep57_CLD. 1 hit.
PF06657. Cep57_MT_bd. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CEE0-1) [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
MAAASVSAAS DSQFSSVLAE PSRSNGNMVR HSSSPYVLYP PDKPFLNSDL
60 70 80 90 100
RRSPNKPTFA YPESNSRAIF SALKNLQDKI RRLELERIQA EESVKTLSRE
110 120 130 140 150
TIEYKKVLDE QIQERENSKN EESKHNQELA SQLVAAENKC NLLEKQLEYM
160 170 180 190 200
RNMIKHAEME RTSVLEKQVS LERERQHDQT HVQSQLEKLD LLEQEYNKLT
210 220 230 240 250
AMQALAEKKM QELESKLREE EQERKRMQAR AAELQSGLEA NRLIFEDKTT
260 270 280 290 300
SCVSTSTRKI KKKKSKPPEK KGSRTYFGAQ PHYRLCLGDM PFVAGTSTSP
310 320 330 340 350
SHAVVANVQH VLHLMKHHSK ALCNDRVVNS VPLAKQACSR VSKSKKSVVP
360 370 380 390 400
PSSSVNEELS DVLQTLQDEF GQMSFDHQQL TKLIQESPTV ELKDNLECEL
410 420 430 440 450
EALVGRMEAK ANQITKVRKY QAQLEKQNID KQKKELKANK KTLDEEGNSS
460 470 480 490 500
GRSSGVPRTA SKKDLAKQRP GEKSRKNLQL LKDMQTIQNS LQSSNLCWDY
Length:500
Mass (Da):56,909
Last modified:December 21, 2004 - v2
Checksum:iD57490F4B22E7707
GO
Isoform 2 (identifier: Q8CEE0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.

Show »
Length:473
Mass (Da):54,286
Checksum:iA86766EF40E0DB90
GO
Isoform 3 (identifier: Q8CEE0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-149: Missing.

Show »
Length:351
Mass (Da):39,996
Checksum:iB61E0BFD2C309ABC
GO

Sequence cautioni

The sequence AAH50785.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC97863.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51S → P in BAB29596 (PubMed:16141072).Curated
Sequence conflicti16 – 249SVLAEPSRS → VRGGGASRC in AAP32743 (PubMed:12954732).Curated
Sequence conflicti295 – 2962GT → EK in AAO73939 (PubMed:12717444).Curated
Sequence conflicti353 – 3531S → N in BAC25962 (PubMed:16141072).Curated
Sequence conflicti386 – 3861E → K in BAB29652 (PubMed:16141072).Curated
Sequence conflicti417 – 4171V → F in BAB29652 (PubMed:16141072).Curated
Sequence conflicti425 – 4251E → K in BAB29652 (PubMed:16141072).Curated
Sequence conflicti431 – 4311K → R in BAB29652 (PubMed:16141072).Curated
Sequence conflicti435 – 4351E → K in BAB29652 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 149149Missing in isoform 3. 2 PublicationsVSP_012265Add
BLAST
Alternative sequencei1 – 2727Missing in isoform 2. 1 PublicationVSP_012266Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY225093 mRNA. Translation: AAO73939.1.
AY251192 mRNA. Translation: AAP32743.1.
AK014873 mRNA. Translation: BAB29596.1.
AK014982 mRNA. Translation: BAB29652.1.
AK016484 mRNA. Translation: BAB30264.1.
AK028458 mRNA. Translation: BAC25962.1.
CT010488 Genomic DNA. Translation: CAX15658.1.
CH466522 Genomic DNA. Translation: EDL24979.1.
BC050785 mRNA. Translation: AAH50785.1. Different initiation.
AK129053 mRNA. Translation: BAC97863.1. Different initiation.
CCDSiCCDS52724.1. [Q8CEE0-1]
RefSeqiNP_001297650.1. NM_001310721.1.
NP_080941.3. NM_026665.4. [Q8CEE0-1]
XP_006510712.1. XM_006510649.1. [Q8CEE0-3]
UniGeneiMm.157212.

Genome annotation databases

EnsembliENSMUST00000034398; ENSMUSP00000034398; ENSMUSG00000031922. [Q8CEE0-1]
ENSMUST00000124883; ENSMUSP00000119081; ENSMUSG00000031922. [Q8CEE0-3]
ENSMUST00000148086; ENSMUSP00000114665; ENSMUSG00000031922. [Q8CEE0-2]
GeneIDi74360.
KEGGimmu:74360.
UCSCiuc009oea.2. mouse. [Q8CEE0-3]
uc009oeb.2. mouse. [Q8CEE0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY225093 mRNA. Translation: AAO73939.1.
AY251192 mRNA. Translation: AAP32743.1.
AK014873 mRNA. Translation: BAB29596.1.
AK014982 mRNA. Translation: BAB29652.1.
AK016484 mRNA. Translation: BAB30264.1.
AK028458 mRNA. Translation: BAC25962.1.
CT010488 Genomic DNA. Translation: CAX15658.1.
CH466522 Genomic DNA. Translation: EDL24979.1.
BC050785 mRNA. Translation: AAH50785.1. Different initiation.
AK129053 mRNA. Translation: BAC97863.1. Different initiation.
CCDSiCCDS52724.1. [Q8CEE0-1]
RefSeqiNP_001297650.1. NM_001310721.1.
NP_080941.3. NM_026665.4. [Q8CEE0-1]
XP_006510712.1. XM_006510649.1. [Q8CEE0-3]
UniGeneiMm.157212.

3D structure databases

ProteinModelPortaliQ8CEE0.
SMRiQ8CEE0. Positions 355-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216689. 1 interaction.
STRINGi10090.ENSMUSP00000034398.

PTM databases

iPTMnetiQ8CEE0.
PhosphoSiteiQ8CEE0.

Proteomic databases

EPDiQ8CEE0.
MaxQBiQ8CEE0.
PaxDbiQ8CEE0.
PRIDEiQ8CEE0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034398; ENSMUSP00000034398; ENSMUSG00000031922. [Q8CEE0-1]
ENSMUST00000124883; ENSMUSP00000119081; ENSMUSG00000031922. [Q8CEE0-3]
ENSMUST00000148086; ENSMUSP00000114665; ENSMUSG00000031922. [Q8CEE0-2]
GeneIDi74360.
KEGGimmu:74360.
UCSCiuc009oea.2. mouse. [Q8CEE0-3]
uc009oeb.2. mouse. [Q8CEE0-1]

Organism-specific databases

CTDi9702.
MGIiMGI:1915551. Cep57.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IESE. Eukaryota.
ENOG410XPJC. LUCA.
GeneTreeiENSGT00530000063695.
HOVERGENiHBG050917.
InParanoidiQ8CEE0.
KOiK16762.
OMAiCNDRVIN.
PhylomeDBiQ8CEE0.
TreeFamiTF329178.

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-8854518. AURKA Activation by TPX2.

Miscellaneous databases

ChiTaRSiCep57. mouse.
PROiQ8CEE0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CEE0.
CleanExiMM_CEP57.
ExpressionAtlasiQ8CEE0. baseline and differential.
GenevisibleiQ8CEE0. MM.

Family and domain databases

InterProiIPR010597. Centrosomal_protein_57kDa.
IPR025913. Cep57_CLD.
IPR024957. Cep57_MT-bd_dom.
[Graphical view]
PANTHERiPTHR19336:SF11. PTHR19336:SF11. 1 hit.
PfamiPF14073. Cep57_CLD. 1 hit.
PF06657. Cep57_MT_bd. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN FGF2 TRAFFICKING.
    Strain: C57BL/6J.
  2. "Tsp57: a novel gene induced during a specific stage of spermatogenesis."
    Kim Y.-S., Nakanishi G., Oudes A.J., Kim K.H., Wang H., Kilpatrick D.L., Jetten A.M.
    Biol. Reprod. 70:106-113(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH RAP80.
    Strain: Swiss Webster.
    Tissue: Testis.
  3. "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.
    , 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] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Skin and Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Testis.
  7. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-257 (ISOFORM 1).
    Tissue: Embryonic tail.
  8. "Cep57, a multidomain protein with unique microtubule and centrosomal localization domains."
    Momotani K., Khromov A.S., Miyake T., Stukenberg P.T., Somlyo A.V.
    Biochem. J. 412:265-273(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, SUBUNIT, INTERACTION WITH MICROTUBULES.

Entry informationi

Entry nameiCEP57_MOUSE
AccessioniPrimary (citable) accession number: Q8CEE0
Secondary accession number(s): B8JJE6
, Q6ZQJ3, Q7TN18, Q80X65, Q810F2, Q9D4J4, Q9D5S4, Q9D5W5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: July 6, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.