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Q8BT07 (CEP55_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centrosomal protein of 55 kDa

Short name=Cep55
Gene names
Name:Cep55
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in mitotic exit and cytokinesis. Not required for microtubule nucleation. Recruits PDCD6IP and TSG101 to midbody during cytokinesis By similarity.

Subunit structure

Homodimer. Interacts (phosphorylated on Ser-423 and Ser-426) with PLK1. Interacts with AKAP9; the interaction occurs in interphase and is lost upon mitotic entry. Interacts with PCNT; the interaction occurs in interphase and is lost upon mitotic entry. Interacts with PDCD6IP; the interaction is direct; CEP55 binds PDCD6IP in a 2:1 stoechiometry; PDCD6IP competes with TSG101 for the same binding site. Interacts with TSG101; TSG101 competes with PDCD6IP for the same binding site; interaction is required for cytokinesis. Interacts with MVB12A, VPS37B, VPS37C and VPS28 By similarity.

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Cleavage furrow By similarity. Midbody By similarity. Note: Present at the centrosomes at interphase. A small portion is associated preferentially with the mother centriole, whereas the majority localizes to the pericentriolar material. During mitosis, loss of affinity for the centrosome at the onset of prophase and diffusion throughout the cell. Dissociation from the centrosome is phosphorylation-dependent. May remain localized at the centrosome during mitosis in certain cell types. Appears at the cleavage furrow in late anaphase and in the midbody in cytokinesis By similarity.

Post-translational modification

There is a hierachy of phosphorylation, where both Ser-423 and Ser-426 are phosphorylated at the onset of mitosis, prior to Ser-434. Phosphorylation at Ser-423 and Ser-426 is required for dissociation from the centrosome at the G2/M boundary. Phosphorylation at the 3 sites, Ser-423, Ser-426 and Ser-434, is required for protein function at the final stages of cell division to complete cytokinesis successfully By similarity.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Tex14Q7M6U311EBI-2552328,EBI-6674575

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BT07-1)

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.
Isoform 2 (identifier: Q8BT07-2)

The sequence of this isoform differs from the canonical sequence as follows:
     397-397: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Centrosomal protein of 55 kDa
PRO_0000238665

Regions

Region157 – 23579Interaction with TSG101 By similarity
Region160 – 21455Interaction with PDCD6IP By similarity
Region354 – 462109Required for localization to the interphase centrosome and to the midbody during cytokinesis By similarity
Coiled coil50 – 400351 Potential

Amino acid modifications

Modified residue4231Phosphoserine By similarity
Modified residue4261Phosphoserine Ref.3
Modified residue4341Phosphoserine; alternate Ref.3
Modified residue4341Phosphoserine; by PLK1; alternate Probable

Natural variations

Alternative sequence3971Missing in isoform 2.
VSP_018630
Natural variant551G → D. Ref.1 Ref.2

Experimental info

Sequence conflict701R → G in BAC40417. Ref.1
Sequence conflict1061E → K in BAC40417. Ref.1
Sequence conflict1571A → P in BAC25819. Ref.1
Sequence conflict2531A → T in AAH26966. Ref.2
Sequence conflict2591L → V in AAH26966. Ref.2
Sequence conflict3001T → M in AAH26966. Ref.2
Sequence conflict4061E → D in BAC25819. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: 5D2308BFCEADA08B

FASTA46253,930
        10         20         30         40         50         60 
MSSRSPKDLI KSKWGSRPSS SKSDTALEKF KGEIAAFKTS LDEITSGKGK MAEKGRSRLL 

        70         80         90        100        110        120 
EKIQVLEAER EKNVYYLLEK DKEIQRLKDH LRSRYSSSSL FEQLEEKTKE CEKKQQLLES 

       130        140        150        160        170        180 
LSKETDVLKN QLSATTKRLS ELESKASTLH LSQSMPANCF NSSMNSIHEK EMQLKDALEK 

       190        200        210        220        230        240 
NQQWLVYDQQ REAYVKGLLA KIFELEKRTE TAAASLTQQM KKIESEGYLQ VEKQKYDHLL 

       250        260        270        280        290        300 
ENAKKDLEVE RQAVTQLRLE LDEFRRKYEE ARKEVEDLNQ LLSSQRKADI QHLEEDKQKT 

       310        320        330        340        350        360 
ERIQKLREES SIFKGKLEEE RKRSEELLSQ VRILYDSLLK HQEEQARVAL LEQQMQACTL 

       370        380        390        400        410        420 
DFENEKLDRQ NMQHQLYVIL KELRKAKSQI TQLESLKQLH GFTITEQPFP LQREPESRVK 

       430        440        450        460 
ATSPKSPSAA LNDSLVECPK CSVQYPATEH RDLLVHVEYC MK 

« Hide

Isoform 2 [UniParc].

Checksum: C0816F19989B4FA1
Show »

FASTA46153,802

References

[1]"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] (ISOFORM 1), VARIANT ASP-55.
Strain: C57BL/6J and NOD.
Tissue: Embryo, Lung and Thymus.
[2]"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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 76-462 (ISOFORM 1), VARIANT ASP-55.
Strain: Czech II and FVB/N.
Tissue: Mammary tumor.
[3]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426 AND SER-434, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004655 mRNA. Translation: BAB23446.1.
AK028216 mRNA. Translation: BAC25819.1.
AK088548 mRNA. Translation: BAC40417.1.
BC026966 mRNA. Translation: AAH26966.1.
BC031396 mRNA. Translation: AAH31396.1.
CCDSCCDS29782.1. [Q8BT07-2]
CCDS50429.1. [Q8BT07-1]
RefSeqNP_001157834.1. NM_001164362.1. [Q8BT07-1]
NP_082569.1. NM_028293.1. [Q8BT07-1]
NP_083036.2. NM_028760.2. [Q8BT07-2]
XP_006527459.1. XM_006527396.1. [Q8BT07-1]
XP_006527460.1. XM_006527397.1. [Q8BT07-1]
XP_006527461.1. XM_006527398.1. [Q8BT07-1]
XP_006527462.1. XM_006527399.1. [Q8BT07-1]
XP_006527463.1. XM_006527400.1. [Q8BT07-1]
XP_006527464.1. XM_006527401.1. [Q8BT07-1]
UniGeneMm.9916.

3D structure databases

ProteinModelPortalQ8BT07.
SMRQ8BT07. Positions 167-208.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid216498. 16 interactions.
IntActQ8BT07. 22 interactions.

PTM databases

PhosphoSiteQ8BT07.

Proteomic databases

MaxQBQ8BT07.
PaxDbQ8BT07.
PRIDEQ8BT07.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000096096; ENSMUSP00000093802; ENSMUSG00000024989. [Q8BT07-1]
ENSMUST00000116506; ENSMUSP00000112205; ENSMUSG00000024989. [Q8BT07-2]
ENSMUST00000169673; ENSMUSP00000127961; ENSMUSG00000024989. [Q8BT07-1]
GeneID74107.
KEGGmmu:74107.
UCSCuc008hiy.2. mouse. [Q8BT07-1]
uc008hja.2. mouse. [Q8BT07-2]

Organism-specific databases

CTD55165.
MGIMGI:1921357. Cep55.

Phylogenomic databases

eggNOGNOG135886.
GeneTreeENSGT00510000047961.
HOGENOMHOG000111547.
HOVERGENHBG081092.
InParanoidQ8BT07.
KOK16456.
OMAINISEVW.
OrthoDBEOG7H4DTJ.
PhylomeDBQ8BT07.
TreeFamTF331107.

Gene expression databases

BgeeQ8BT07.
CleanExMM_CEP55.
GenevestigatorQ8BT07.

Family and domain databases

InterProIPR022008. EABR.
[Graphical view]
PfamPF12180. EABR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio339796.
PROQ8BT07.
SOURCESearch...

Entry information

Entry nameCEP55_MOUSE
AccessionPrimary (citable) accession number: Q8BT07
Secondary accession number(s): Q8C2J0 expand/collapse secondary AC list , Q8K2I8, Q8R2Y4, Q9DBZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 30, 2006
Last modified: July 9, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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