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Protein

Centrosome-associated protein CEP250

Gene

Cep250

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

Functioni

Probably plays an important role in centrosome cohesion during interphase.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Centrosome-associated protein CEP250
Alternative name(s):
250 kDa centrosomal protein
Short name:
Cep250
Centrosomal Nek2-associated protein 1
Short name:
C-Nap1
Centrosomal protein 2
Intranuclear matrix protein
Gene namesi
Name:Cep250
Synonyms:Cep2, Inmp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:108084. Cep250.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: MGI
  • centrosome Source: MGI
  • cilium Source: UniProtKB-KW
  • extracellular exosome Source: MGI
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • protein complex Source: MGI
  • spindle pole centrosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24142414Centrosome-associated protein CEP250PRO_0000089488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2389 – 23891Phosphoserine; by NEK2By similarity
Modified residuei2393 – 23931Phosphoserine; by NEK2By similarity

Post-translational modificationi

C-terminal part is phosphorylated by NEK2. Dephosphorylated in vitro by the PP1 phosphatase (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ60952.
MaxQBiQ60952.
PaxDbiQ60952.
PRIDEiQ60952.

PTM databases

PhosphoSiteiQ60952.

Expressioni

Gene expression databases

BgeeiQ60952.
CleanExiMM_CEP250.
ExpressionAtlasiQ60952. baseline and differential.
GenevisibleiQ60952. MM.

Interactioni

Subunit structurei

Monomer and homodimer (Probable). Forms a complex in vitro with both NEK2 kinase and the PPP1CC catalytic subunit of protein phosphatase 1 (PP1). Interacts with CEP135 (By similarity). Interacts with CROCC/rootletin. Interacts with CNTLN (By similarity).By similarityCurated1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200766. 6 interactions.
IntActiQ60952. 8 interactions.
MINTiMINT-1748681.
STRINGi10090.ENSMUSP00000105248.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili91 – 15363Sequence analysisAdd
BLAST
Coiled coili248 – 357110Sequence analysisAdd
BLAST
Coiled coili400 – 1165766Sequence analysisAdd
BLAST
Coiled coili1237 – 2200964Sequence analysisAdd
BLAST
Coiled coili2231 – 229060Sequence analysisAdd
BLAST
Coiled coili2320 – 234526Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi43 – 289247Glu-richAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFAN. Eukaryota.
ENOG410XPG3. LUCA.
GeneTreeiENSGT00730000110800.
HOGENOMiHOG000246955.
HOVERGENiHBG081320.
InParanoidiQ60952.
KOiK16464.

Family and domain databases

InterProiIPR026048. CEP250.
[Graphical view]
PANTHERiPTHR23159:SF1. PTHR23159:SF1. 4 hits.

Sequencei

Sequence statusi: Complete.

Q60952-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METGSPGLNM KPQSLQLVLE GQVLALQQQM AENQAASWRK LKNSQEAQKR
60 70 80 90 100
QATLVRKLQA KVLQYRSWCQ DLEKRLEATG GLIPQRWESV EEPNLEQLLI
110 120 130 140 150
RLEEEQQRCE SLVEVNTELR LHMEKADVVN KALQEDVEKL TVDWSRARDE
160 170 180 190 200
LVRKESQWRM EQEFFKGYLR GEHGRLLNLW REVVTFRRHF LKMKSATDRD
210 220 230 240 250
LTELKAEHAR LSGSLLTCCL RLTLRAQSRE SSGSGRTEES EPARLLLLVA
260 270 280 290 300
KTQALEKEAH EKSQELMQLK SHGDLEKAEL QDRVTELSAL LTQSQKQNED
310 320 330 340 350
YEKMVKALRE TMEILETNHA ELMEHEASLS RNAQEEKLSL QQVIKAITQA
360 370 380 390 400
LASVEEEDTV TQSSGHEDSL QSDCNGLSQF DPQDPDRALT LVQSVLTRRQ
410 420 430 440 450
QAVQDLRQQL SGCQEAMSFL QQQHDQWEEE GRALREKLQK LTGERDALAG
460 470 480 490 500
QTVGLQGEVD SLSRERELLQ KARGELQQQL EVLEQEAWRL RRMNMELQLQ
510 520 530 540 550
GDSAQGEKLE QQEELHLAVR ERERLQETLV GLEAKQSESL SELLTLREAL
560 570 580 590 600
ESSRLEGELL KQERVEVAAA LARAEQSIVE LSGSENSLKA EVADLRAAAV
610 620 630 640 650
KLGALNEALA LDKVELNQQL LQLEQENQSL CSRVEAAEQL RSALQVDLAE
660 670 680 690 700
AERRREALWE KKTQLETQLQ KAEEAGAELQ AELRGTREEK EELKDKLSEA
710 720 730 740 750
HHQQETATAH LEQLHQDAER QEETLARAVQ EKEALVRERA ALEVRLQAVE
760 770 780 790 800
RDRQDLTEHV LGLRSAKEQL ESNLFEAQQQ NSVIQVTKGQ LEVQIQTIIQ
810 820 830 840 850
AKEVIQGEVK CLKLELDAER TRAEQEWDAV ARQLAQAEQE GQASLERQKV
860 870 880 890 900
AHEEEVNRLQ EKWEKERSWL QQELDKTLET LERERAELET KLREQQTEME
910 920 930 940 950
AIRAQREEER SQADSALYQM QLETEKERVS LLETLLRTQK ELADASQQLE
960 970 980 990 1000
RLRQDMKIQK LKEQETTGML QAQLQETQQE LKEAAQQHRD DLAAFQKDKL
1010 1020 1030 1040 1050
DLQKQVEDLM SQLVAHDDSQ RLVKEEIEEK VKVAQECSRI QKELEKENAS
1060 1070 1080 1090 1100
LALSLVEKEK RLLILQEADS VRQQELSSLR QDIQEAQEGQ RELGVQVELL
1110 1120 1130 1140 1150
RQEVKEKEAD FVAREAQLLE ELEASRVAEQ QLRASLWAQE AKATQLQLQL
1160 1170 1180 1190 1200
RSTESQLEAL VAEQQPENQA QAQLASLCSV LQQALGSACE SRPELRGGGD
1210 1220 1230 1240 1250
SAPTLWGPDP DQNGASRLFK RWSLPTALSP EAVALALQKL HQDVWKARQA
1260 1270 1280 1290 1300
RDDLRDQVQK LVQRLTDTEA QKSQVHSELQ DLQRQLSQSQ EEKSKWEGRQ
1310 1320 1330 1340 1350
NSLESELRDL HETAASLQSR LRQAELQKME AQNDRELLQA SKEKLSAQVE
1360 1370 1380 1390 1400
HLQACVAEAQ AQADAAAVLE EDLRTARSAL KLKNEELESE RERAQALQEQ
1410 1420 1430 1440 1450
GELKVAQGKA LQENLALLAQ TLSNREREVE TLQAEVQELE KQREMQKAAL
1460 1470 1480 1490 1500
ELLSLDLKKR SREVDLQQEQ IQELEQCRSV LEHLPMAVQE REQKLSVQRD
1510 1520 1530 1540 1550
QIRELENDRE AQRSVLEHQL LDLEQKAQVI ESQRGQIQDL KKQLGTLECL
1560 1570 1580 1590 1600
ALELEESHHK VESQQKMITE LEGQREMQRV ALTHLTLDLE ERSQELQAQS
1610 1620 1630 1640 1650
SQLHELENHS THLAKELQER DQEVTSQRQQ IDELQKQQEQ LAQALERKGQ
1660 1670 1680 1690 1700
ELVLQKERIQ VLEDQRTLQT KILEEDLEQI KHSLRERSQE LASQWQLVHE
1710 1720 1730 1740 1750
RADDGKSPSK GQRGSLEHLK LILRDKEKEV ECQQERIQEL QGHMGQLEQQ
1760 1770 1780 1790 1800
LQGLHRKVGE TSLLLTHREQ ETATLQQHLQ EAKEQGELRE QVLQGQLEEA
1810 1820 1830 1840 1850
QRDLAQRDHE LETLRQEKQQ TQDQEESMKL KTSALQAALE QAHATLKERQ
1860 1870 1880 1890 1900
GELEEHREQV RRLQEELEVE GRQVRALEEV LGDLRAESRE HEKAVLALQQ
1910 1920 1930 1940 1950
RCAEQAQEHE AEARTLQDSW LQAQATLTEQ EQELAALRAE NQYSRRQEEA
1960 1970 1980 1990 2000
AVSQAEALQE ALSKAQAALQ EKEQSLLEQA ELSHTLEAST AALQATLDTC
2010 2020 2030 2040 2050
QASARQLEEA LRIREGEIQA QALQHHEVTQ HLQQELCQKK EELRQLLEKA
2060 2070 2080 2090 2100
GARRSQENGI QEKQSLEQER QEETRRLLES LKELQLTVAQ REEEILMLRE
2110 2120 2130 2140 2150
ASSPRHRALP AEKPALQPLP AQQELERLQT ALRQTEAREI EWREKAQDLA
2160 2170 2180 2190 2200
LSLAQSKASI SSLQEITMFL QASVLERESE QQRLQEELVL SRQALEEQQS
2210 2220 2230 2240 2250
GGPHSTSRAD QGPKVGQGSQ SGEVETEPSP GVEEKERLTQ RLERLQQAVA
2260 2270 2280 2290 2300
ELEVDRSKLQ CHNAQLRTAL EQVERERRKL KRDSVRASRA GSLEARETMT
2310 2320 2330 2340 2350
SSPTQQDGRG SQRGSSDSVL VVELQREVAL LRAQLALERK QRQDYIARSV
2360 2370 2380 2390 2400
QTSRELAGLH HSLSHSLLTV AQAPEATVLE AETRKLDESL NQSLTSPGPC
2410
LLHPSLDTTQ NTHR
Length:2,414
Mass (Da):276,814
Last modified:July 27, 2011 - v4
Checksum:i7B76E9E781D731CC
GO

Sequence cautioni

The sequence AAB41824.1 differs from that shown. Reason: Frameshift at positions 1843, 1914, 1924, 2341 and 2371. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911E → K in BAC32417 (PubMed:16141072).Curated
Sequence conflicti369 – 3691S → L in ABA29340 (PubMed:16339073).Curated
Sequence conflicti424 – 4241H → R in ABA29340 (PubMed:16339073).Curated
Sequence conflicti437 – 4371K → R in ABA29340 (PubMed:16339073).Curated
Sequence conflicti454 – 4541G → D in ABA29340 (PubMed:16339073).Curated
Sequence conflicti508 – 5081K → R in ABA29340 (PubMed:16339073).Curated
Sequence conflicti615 – 6151E → G in ABA29340 (PubMed:16339073).Curated
Sequence conflicti645 – 6451Q → R in ABA29340 (PubMed:16339073).Curated
Sequence conflicti1837 – 18371A → P in AAB41824 (PubMed:8950169).Curated
Sequence conflicti1864 – 18641Q → R in AAB41824 (PubMed:8950169).Curated
Sequence conflicti1924 – 19252QA → RP in AAB41824 (PubMed:8950169).Curated
Sequence conflicti1966 – 19661Q → E in BAE23916 (PubMed:16141072).Curated
Sequence conflicti1974 – 19741Q → H in AAH57582 (PubMed:15489334).Curated
Sequence conflicti2003 – 20031S → R in ABA29340 (PubMed:16339073).Curated
Sequence conflicti2003 – 20031S → R in AAB41824 (PubMed:8950169).Curated
Sequence conflicti2040 – 20401K → E in ABA29340 (PubMed:16339073).Curated
Sequence conflicti2040 – 20401K → E in AAB41824 (PubMed:8950169).Curated
Sequence conflicti2105 – 21051R → S in ABA29340 (PubMed:16339073).Curated
Sequence conflicti2105 – 21051R → S in AAB41824 (PubMed:8950169).Curated
Sequence conflicti2192 – 21921R → S in AAB41824 (PubMed:8950169).Curated
Sequence conflicti2218 – 22181G → E in AAB41824 (PubMed:8950169).Curated
Sequence conflicti2221 – 22211S → P in ABA29340 (PubMed:16339073).Curated
Sequence conflicti2221 – 22211S → P in AAB41824 (PubMed:8950169).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ148475 mRNA. Translation: ABA29340.1.
AL833786 Genomic DNA. No translation available.
AK045557 mRNA. Translation: BAC32417.1.
AK139187 mRNA. Translation: BAE23916.1.
U33198 mRNA. Translation: AAB41824.1. Frameshift.
BC057582 mRNA. Translation: AAH57582.1.
CCDSiCCDS50771.1.
RefSeqiNP_001123471.1. NM_001129999.1.
NP_032409.3. NM_008383.3.
NP_796191.2. NM_177217.3.
UniGeneiMm.288729.

Genome annotation databases

EnsembliENSMUST00000094421; ENSMUSP00000091988; ENSMUSG00000038241.
GeneIDi16328.
KEGGimmu:16328.
UCSCiuc008nlu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ148475 mRNA. Translation: ABA29340.1.
AL833786 Genomic DNA. No translation available.
AK045557 mRNA. Translation: BAC32417.1.
AK139187 mRNA. Translation: BAE23916.1.
U33198 mRNA. Translation: AAB41824.1. Frameshift.
BC057582 mRNA. Translation: AAH57582.1.
CCDSiCCDS50771.1.
RefSeqiNP_001123471.1. NM_001129999.1.
NP_032409.3. NM_008383.3.
NP_796191.2. NM_177217.3.
UniGeneiMm.288729.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200766. 6 interactions.
IntActiQ60952. 8 interactions.
MINTiMINT-1748681.
STRINGi10090.ENSMUSP00000105248.

PTM databases

PhosphoSiteiQ60952.

Proteomic databases

EPDiQ60952.
MaxQBiQ60952.
PaxDbiQ60952.
PRIDEiQ60952.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000094421; ENSMUSP00000091988; ENSMUSG00000038241.
GeneIDi16328.
KEGGimmu:16328.
UCSCiuc008nlu.2. mouse.

Organism-specific databases

CTDi11190.
MGIiMGI:108084. Cep250.

Phylogenomic databases

eggNOGiENOG410IFAN. Eukaryota.
ENOG410XPG3. LUCA.
GeneTreeiENSGT00730000110800.
HOGENOMiHOG000246955.
HOVERGENiHBG081320.
InParanoidiQ60952.
KOiK16464.

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.

Miscellaneous databases

ChiTaRSiCep250. mouse.
NextBioi289406.
PROiQ60952.
SOURCEiSearch...

Gene expression databases

BgeeiQ60952.
CleanExiMM_CEP250.
ExpressionAtlasiQ60952. baseline and differential.
GenevisibleiQ60952. MM.

Family and domain databases

InterProiIPR026048. CEP250.
[Graphical view]
PANTHERiPTHR23159:SF1. PTHR23159:SF1. 4 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rootletin interacts with C-Nap1 and may function as a physical linker between the pair of centrioles/basal bodies in cells."
    Yang J., Adamian M., Li T.
    Mol. Biol. Cell 17:1033-1040(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH CROCC.
    Strain: C57BL/6 X 129/Sv.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] OF 1-686 AND 1966-2414.
    Strain: C57BL/6J.
    Tissue: Cerebellum and Corpora quadrigemina.
  4. "INMP, a novel intranuclear matrix protein related to the family of intermediate filament-like proteins: molecular cloning and sequence analysis."
    Menz K., Radomski N., Jost E.
    Biochim. Biophys. Acta 1309:14-20(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1806-2414.
    Tissue: Macrophage.
  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] OF 1872-2414.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiCP250_MOUSE
AccessioniPrimary (citable) accession number: Q60952
Secondary accession number(s): E9QMB2
, Q2I8G3, Q3UTR4, Q6PFF6, Q8BLC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: July 27, 2011
Last modified: April 13, 2016
This is version 116 of the entry and version 4 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

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.