Centromere protein C 1 - Mus musculus (Mouse)

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P49452 (CENPC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Centromere protein C 1
Short name=CENP-C 1

Alternative name(s):
Centromere autoantigen C

Gene names

Name:	Cenpc1
Synonyms:	Cenpc

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	906 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. CENPC recruits DNA methylation and DNMT3B to both centromeric and pericentromeric satellite repeats and regulates the histone code in these regions By similarity.
Subunit structure	Oligomer By similarity. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Binds to DAXX By similarity. Interacts directly with CENPA By similarity.
Subcellular location	Nucleus By similarity. Chromosome › centromere By similarity. Chromosome › centromere › kinetochore By similarity. Note: Localizes exclusively in the kinetochore domain of centromeres By similarity.
Domain	The MIF2 homology domain II targets centromeres and binds the alpha satellite DNA in vivo. The MIF2 homology domain III can induce CENPC dimerization/oligomerization.
Sequence similarities	Belongs to the CENPC family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Kinetochore Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from sequence or structural similarity. Source: UniProtKB kinetochore assembly Inferred from sequence or structural similarity. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	centromeric heterochromatin Inferred from sequence or structural similarity. Source: UniProtKB condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell condensed nuclear chromosome, centromeric region Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: Compara kinetochore Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Pten	O08586	2	EBI-1186252,EBI-1186266

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 906

906

Centromere protein C 1

PRO_0000089475

Regions

Region

702 – 724

MIF2 homology domain II By similarity

Region

853 – 906

MIF2 homology domain III By similarity

Motif

228 – 242

Nuclear localization signal Potential

Motif

449 – 466

Nuclear localization signal Potential

Motif

525 – 540

Nuclear localization signal Potential

Motif

744 – 762

Nuclear localization signal Potential

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

404

Phosphoserine By similarity

Modified residue

505

Phosphoserine By similarity

Modified residue

673

Phosphoserine By similarity

Modified residue

728

Phosphoserine By similarity

Modified residue

737

Phosphoserine By similarity

Experimental info

Sequence conflict

S → M in AAC04314. Ref.1

Sequence conflict

185

L → S in AAC04314. Ref.1

Sequence conflict

418

K → T in AAC04314. Ref.1

Sequence conflict

450

K → R in AAC04314. Ref.1

Sequence conflict

488

C → R in AAC04314. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P49452 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0DCFE76496B33946
Show »

FASTA

906

102,154

        10         20         30         40         50         60 
MASFHLDHLK NYHRRYCRSS RAPNIHTKKG QNMLEILQDC FEDQSKASFL DDFTESLTSS 

        70         80         90        100        110        120 
TQKKKANYSQ SSSKKCPESH SKPVPVSSRT GEASLQASAE PSEAAGGSVQ ANEVHHGASD 

       130        140        150        160        170        180 
ELDLCVGSPV VLLDANVNTL QKAASPAGQK RVASVSRSPV DRQASNKNIS FKTRKRLNFE 

       190        200        210        220        230        240 
DKVTLSTAET ENSVLQVEDN LSKGQEGTSS EITQKRDDLS SDVQSRSKKN FSELFLETVK 

       250        260        270        280        290        300 
RKSKSSSVVR HTAAVPFSPP PPSDMKLLED EFIIDRSDRS FSSRLWVMIP SKDRHLSAHK 

       310        320        330        340        350        360 
PSPENTALLQ GKKSREKSHS LSAMTFARNT QSDKAHPIEE AQLSVEENPA TTCTDELEND 

       370        380        390        400        410        420 
CRSPENKMQS ETAKTPPAWE RTTKQSQRRV SKPKAAEELR KGQSSWENSN VSNTGQDKLQ 

       430        440        450        460        470        480 
INSKRNMKDC EEVRNEPNPK KQKPALENKK KTNSTQTNKE KSGKKFFSGG SKNKFVPKKV 

       490        500        510        520        530        540 
TLTSRRSCRI SQRPSEWWRV KSDESSVDRN PSKENNSPVV YPNKKKQTKR NHVSKRAGKK 

       550        560        570        580        590        600 
PGSSKRQKTE MSPRVQKSLN VKDSGGTVSG HDDTSRSQRK PLKIIEADPT QKSLAISRPK 

       610        620        630        640        650        660 
RGCKYRNNVM TSPNVHLKSH TEEYTSKTQM ESASNSEMSK RSVWEESGPS RFKNYEMPGS 

       670        680        690        700        710        720 
SNSEMGDEQD QKSLHFTTRS FNMVPDKKLH HKLVLPSNSP NVRRSNRIRL KPLEYWRGER 

       730        740        750        760        770        780 
VDYQESSSGQ LVLEIISPSS VPTKIKAQRN LGKVNKKVTK KPTHLNSHEK AKMELPLDMR 

       790        800        810        820        830        840 
LGDPFQATLA KDPETAELVP MDLIRPRDTY RFFVEQHGLK VFKTLDTIYF STGKLVLGPY 

       850        860        870        880        890        900 
EEKGKQHVGQ DILVFYVNFG DLLCTLHETP YKLTTGDSFY VPSGNHYNIK NLLNVESSLL 


FTQIKR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence homologies and linkage group conservation of the human and mouse Cenpc genes." McKay S., Thomson E., Cooke H. Genomics 22:36-40(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss.
[2]	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].
[3]	"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: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U03113 mRNA. Translation: AAC04314.1. CH466524 Genomic DNA. Translation: EDL37951.1. BC150700 mRNA. Translation: AAI50701.1.
IPI	IPI00114808.
PIR	A54654.
RefSeq	NP_031709.2. NM_007683.3.
UniGene	Mm.4649.
3D structure databases
ProteinModelPortal	P49452.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49452. 2 interactions.
STRING	10090.ENSMUSP00000031170.
PTM databases
PhosphoSite	P49452.
Proteomic databases
PRIDE	P49452.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031170; ENSMUSP00000031170; ENSMUSG00000029253.
GeneID	12617.
KEGG	mmu:12617.
Organism-specific databases
CTD	1060.
MGI	MGI:99700. Cenpc1.
Phylogenomic databases
eggNOG	NOG307418.
GeneTree	ENSGT00390000016737.
HOGENOM	HOG000090256.
HOVERGEN	HBG050891.
InParanoid	P49452.
KO	K11497.
OMA	WITIPRK.
OrthoDB	EOG4JM7P0.
Gene expression databases
ArrayExpress	P49452.
Bgee	P49452.
CleanEx	MM_CENPC1.
Genevestigator	P49452.
GermOnline	ENSMUSG00000029253. Mus musculus.
Family and domain databases
Gene3D	2.60.120.10. 1 hit.
InterPro	IPR025974. Mif2/CENP-C_cupin. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
Pfam	PF11699. Mif2. 1 hit. [Graphical view]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
ProtoNet	Search...
Other
NextBio	281786.
SOURCE	Search...

Entry information

Entry name

CENPC_MOUSE

Accession

Primary (citable) accession number: P49452
Secondary accession number(s): B9EK81

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents