Reviewed, UniProtKB/Swiss-Prot Q9BV73 (CP250_HUMAN)

Names and origin

Protein names

Recommended name:
Centrosome-associated protein CEP250

Alternative name(s):
250 kDa centrosomal protein
Short name=Cep250
Centrosomal protein 2
Centrosomal Nek2-associated protein 1
Short name=C-Nap1

Gene names

Name:	CEP250
Synonyms:	CEP2, CNAP1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2442 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably plays an important role in centrosome cohesion during interphase.
Subunit structure	Monomer and homodimer Probable. Interacts with CROCC/rootletin By similarity. Forms a complex in vitro with both NEK2 kinase and the PPP1CC catalytic subunit of protein phosphatase 1 (PP1). Interacts with CEP135. Ref.2 Ref.4 Ref.6
Subcellular location	Cytoplasm › perinuclear region. Cytoplasm › cytoskeleton › centrosome › centriole. Cytoplasm › cytoskeleton › cilium basal body. Note: Component of the core centrosome. In interphase cells, it specifically associates with the proximal ends of both mother and daughter centrioles. Associates with the centrosome in interphase cells. In mitotic cells, it dissociates from the mitotic spindle poles. At the end of cell division, it reaccumulates at centrosomes. In photoreceptors, found at the proximal ends of basal bodies. Ref.2
Tissue specificity	Ubiquitously and weakly expressed.
Post-translational modification	Differentially phosphorylated during cell cycle. Phosphorylation may regulate association/dissociation from centrosome. During M phase of mitosis, C-terminal part is phosphorylated by NEK2, suggesting that it may trigger the dissociation from the mitotic centrosome. Dephosphorylated in vitro by the PP1 phosphatase. Ref.4 Ref.5 Ref.7
Miscellaneous	Antibodies against CEP2 are present in sera from patients with autoimmune diseases that developed autoantibodies against centrosomal proteins.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cell projection Cilium Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	centriole-centriole cohesion Ref.6 Inferred from mutant phenotype. Source: UniProtKB mitotic cell cycle Ref.5 Inferred from direct assay. Source: UniProtKB protein localization Ref.6 Inferred from mutant phenotype. Source: UniProtKB regulation of centriole-centriole cohesion Ref.2 Inferred from direct assay. Source: UniProtKB
Cellular component	centriole Ref.6 Inferred from direct assay. Source: UniProtKB cilium Inferred from electronic annotation. Source: UniProtKB-KW cytosol Inferred from Experiment. Source: Reactome microtubule basal body Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell protein complex Ref.4 Inferred from mutant phenotype. Source: UniProtKB
Molecular function	protein C-terminus binding Ref.6 Inferred from physical interaction. Source: UniProtKB protein kinase binding Ref.2 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BV73-1)

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: Q9BV73-2)

The sequence of this isoform differs from the canonical sequence as follows:
     863-918: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2442	2442	Centrosome-associated protein CEP250		PRO_0000089487
Regions
	Coiled coil	95 – 158	64	Potential
	Coiled coil	244 – 352	109	Potential
	Coiled coil	395 – 1172	778	Potential
	Coiled coil	1243 – 2227	985	Potential
	Coiled coil	2262 – 2376	115	Potential
	Compositional bias	246 – 250	5	Poly-Leu
	Compositional bias	464 – 2171	1708	Gln/Glu-rich
Amino acid modifications
	Modified residue	1048	1	N6-acetyllysine Ref.8
	Modified residue	2229	1	Phosphoserine Ref.7
	Modified residue	2259	1	Phosphoserine Ref.7
Natural variations
	Alternative sequence	863 – 918	56	Missing in isoform 2.		VSP_007372
	Natural variant	995	1	Q → H: dbSNP rs2296403.		VAR_015649
	Natural variant	1072	1	Q → E: dbSNP rs17092706.		VAR_050898
	Natural variant	1441	1	R → Q: dbSNP rs3748433.		VAR_021858
Experimental info
	Sequence conflict	120	1	L → I in AAC06349. Ref.1
	Sequence conflict	136	1	E → A in AAC06349. Ref.1
	Sequence conflict	365	1	H → L in AAC06349. Ref.1
	Sequence conflict	372	1	D → E in AAC06349. Ref.1
	Sequence conflict	509	1	E → D in AAC07988. Ref.2
	Sequence conflict	552	1	S → I in AAC06349. Ref.1
	Sequence conflict	757	1	E → A in AAC06349. Ref.1
	Sequence conflict	784 – 787	4	EVTK → DEPQ in AAC06349. Ref.1
	Sequence conflict	1153	1	Q → H in AAC06349. Ref.1
	Sequence conflict	1246	1	H → L in AAC06349. Ref.1
	Sequence conflict	1513	1	L → P in AAC06349. Ref.1
	Sequence conflict	2082	1	Q → L in AAC06349. Ref.1
	Sequence conflict	2345	1	D → N in AAC06349. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 9, 2003. Version 2. Checksum: BC2B8A36E07B8272	FASTA	2,442	281,137
	10 20 30 40 50 60 METRSPGLNN MKPQSLQLVL EEQVLALQQQ MAENQAASWR KLKNSQEAQQ RQATLVRKLQ 70 80 90 100 110 120 AKVLQYRSWC QELEKRLEAT GGPIPQRWEN VEEPNLDELL VRLEEEQQRC ESLAEVNTQL 130 140 150 160 170 180 RLHMEKADVV NKALREDVEK LTVDWSRARD ELMRKESQWQ MEQEFFKGYL KGEHGRLLSL 190 200 210 220 230 240 WREVVTFRRH FLEMKSATDR DLMELKAEHV RLSGSLLTCC LRLTVGAQSR EPNGSGRMDG 250 260 270 280 290 300 REPAQLLLLL AKTQELEKEA HERSQELIQL KSQGDLEKAE LQDRVTELSA LLTQSQKQNE 310 320 330 340 350 360 DYEKMIKALR ETVEILETNH TELMEHEASL SRNAQEEKLS LQQVIKDITQ VMVEEGDNIA 370 380 390 400 410 420 QGSGHENSLE LDSSIFSQFD YQDADKALTL VRSVLTRRRQ AVQDLRQQLA GCQEAVNLLQ 430 440 450 460 470 480 QQHDQWEEEG KALRQRLQKL TGERDTLAGQ TVDLQGEVDS LSKERELLQK AREELRQQLE 490 500 510 520 530 540 VLEQEAWRLR RVNVELQLQG DSAQGQKEEQ QEELHLAVRE RERLQEMLMG LEAKQSESLS 550 560 570 580 590 600 ELITLREALE SSHLEGELLR QEQTEVTAAL ARAEQSIAEL SSSENTLKTE VADLRAAAVK 610 620 630 640 650 660 LSALNEALAL DKVGLNQQLL QLEEENQSVC SRMEAAEQAR NALQVDLAEA EKRREALWEK 670 680 690 700 710 720 NTHLEAQLQK AEEAGAELQA DLRDIQEEKE EIQKKLSESR HQQEAATTQL EQLHQEAKRQ 730 740 750 760 770 780 EEVLARAVQE KEALVREKAA LEVRLQAVER DRQDLAEQLQ GLSSAKELLE SSLFEAQQQN 790 800 810 820 830 840 SVIEVTKGQL EVQIQTVTQA KEVIQGEVRC LKLELDTERS QAEQERDAAA RQLAQAEQEG 850 860 870 880 890 900 KTALEQQKAA HEKEVNQLRE KWEKERSWHQ QELAKALESL EREKMELEMR LKEQQTEMEA 910 920 930 940 950 960 IQAQREEERT QAESALCQMQ LETEKERVSL LETLLQTQKE LADASQQLER LRQDMKVQKL 970 980 990 1000 1010 1020 KEQETTGILQ TQLQEAQREL KEAARQHRDD LAALQEESSS LLQDKMDLQK QVEDLKSQLV 1030 1040 1050 1060 1070 1080 AQDDSQRLVE QEVQEKLRET QEYNRIQKEL EREKASLTLS LMEKEQRLLV LQEADSIRQQ 1090 1100 1110 1120 1130 1140 ELSALRQDMQ EAQGEQKELS AQMELLRQEV KEKEADFLAQ EAQLLEELEA SHITEQQLRA 1150 1160 1170 1180 1190 1200 SLWAQEAKAA QLQLRLRSTE SQLEALAAEQ QPGNQAQAQA QLASLYSALQ QALGSVCESR 1210 1220 1230 1240 1250 1260 PELSGGGDSA PSVWGLEPDQ NGARSLFKRG PLLTALSAEA VASALHKLHQ DLWKTQQTRD 1270 1280 1290 1300 1310 1320 VLRDQVQKLE ERLTDTEAEK SQVHTELQDL QRQLSQNQEE KSKWEGKQNS LESELMELHE 1330 1340 1350 1360 1370 1380 TMASLQSRLR RAELQRMEAQ GERELLQAAK ENLTAQVEHL QAAVVEARAQ ASAAGILEED 1390 1400 1410 1420 1430 1440 LRTARSALKL KNEEVESERE RAQALQEQGE LKVAQGKALQ ENLALLTQTL AEREEEVETL 1450 1460 1470 1480 1490 1500 RGQIQELEKQ REMQKAALEL LSLDLKKRNQ EVDLQQEQIQ ELEKCRSVLE HLPMAVQERE 1510 1520 1530 1540 1550 1560 QKLTVQREQI RELEKDRETQ RNVLEHQLLE LEKKDQMIES QRGQVQDLKK QLVTLECLAL 1570 1580 1590 1600 1610 1620 ELEENHHKME CQQKLIKELE GQRETQRVAL THLTLDLEER SQELQAQSSQ IHDLESHSTV 1630 1640 1650 1660 1670 1680 LARELQERDQ EVKSQREQIE ELQRQKEHLT QDLERRDQEL MLQKERIQVL EDQRTRQTKI 1690 1700 1710 1720 1730 1740 LEEDLEQIKL SLRERGRELT TQRQLMQERA EEGKGPSKAQ RGSLEHMKLI LRDKEKEVEC 1750 1760 1770 1780 1790 1800 QQEHIHELQE LKDQLEQQLQ GLHRKVGETS LLLSQREQEI VVLQQQLQEA REQGELKEQS 1810 1820 1830 1840 1850 1860 LQSQLDEAQR ALAQRDQELE ALQQEQQQAQ GQEERVKEKA DALQGALEQA HMTLKERHGE 1870 1880 1890 1900 1910 1920 LQDHKEQARR LEEELAVEGR RVQALEEVLG DLRAESREQE KALLALQQQC AEQAQEHEVE 1930 1940 1950 1960 1970 1980 TRALQDSWLQ AQAVLKERDQ ELEALRAESQ SSRHQEEAAR ARAEALQEAL GKAHAALQGK 1990 2000 2010 2020 2030 2040 EQHLLEQAEL SRSLEASTAT LQASLDACQA HSRQLEEALR IQEGEIQDQD LRYQEDVQQL 2050 2060 2070 2080 2090 2100 QQALAQRDEE LRHQQEREQL LEKSLAQRVQ ENMIQEKQNL GQEREEEEIR GLHQSVRELQ 2110 2120 2130 2140 2150 2160 LTLAQKEQEI LELRETQQRN NLEALPHSHK TSPMEEQSLK LDSLEPRLQR ELERLQAALR 2170 2180 2190 2200 2210 2220 QTEAREIEWR EKAQDLALSL AQTKASVSSL QEVAMFLQAS VLERDSEQQR LQDELELTRR 2230 2240 2250 2260 2270 2280 ALEKERLHSP GATSTAELGS RGEQGVQLGE VSGVEAEPSP DGMEKQSWRQ RLEHLQQAVA 2290 2300 2310 2320 2330 2340 RLEIDRSRLQ RHNVQLRSTL EQVERERRKL KREAMRAAQA GSLEISKATA SSPTQQDGRG 2350 2360 2370 2380 2390 2400 QKNSDAKCVA ELQKEVVLLQ AQLTLERKQK QDYITRSAQT SRELAGLHHS LSHSLLAVAQ 2410 2420 2430 2440 APEATVLEAE TRRLDESLTQ SLTSPGPVLL HPSPSTTQAA SR
	Isoform 2. Checksum: CE22E600206C2CE8	FASTA	2,386	274,380
	10 20 30 40 50 60 METRSPGLNN MKPQSLQLVL EEQVLALQQQ MAENQAASWR KLKNSQEAQQ RQATLVRKLQ 70 80 90 100 110 120 AKVLQYRSWC QELEKRLEAT GGPIPQRWEN VEEPNLDELL VRLEEEQQRC ESLAEVNTQL 130 140 150 160 170 180 RLHMEKADVV NKALREDVEK LTVDWSRARD ELMRKESQWQ MEQEFFKGYL KGEHGRLLSL 190 200 210 220 230 240 WREVVTFRRH FLEMKSATDR DLMELKAEHV RLSGSLLTCC LRLTVGAQSR EPNGSGRMDG 250 260 270 280 290 300 REPAQLLLLL AKTQELEKEA HERSQELIQL KSQGDLEKAE LQDRVTELSA LLTQSQKQNE 310 320 330 340 350 360 DYEKMIKALR ETVEILETNH TELMEHEASL SRNAQEEKLS LQQVIKDITQ VMVEEGDNIA 370 380 390 400 410 420 QGSGHENSLE LDSSIFSQFD YQDADKALTL VRSVLTRRRQ AVQDLRQQLA GCQEAVNLLQ 430 440 450 460 470 480 QQHDQWEEEG KALRQRLQKL TGERDTLAGQ TVDLQGEVDS LSKERELLQK AREELRQQLE 490 500 510 520 530 540 VLEQEAWRLR RVNVELQLQG DSAQGQKEEQ QEELHLAVRE RERLQEMLMG LEAKQSESLS 550 560 570 580 590 600 ELITLREALE SSHLEGELLR QEQTEVTAAL ARAEQSIAEL SSSENTLKTE VADLRAAAVK 610 620 630 640 650 660 LSALNEALAL DKVGLNQQLL QLEEENQSVC SRMEAAEQAR NALQVDLAEA EKRREALWEK 670 680 690 700 710 720 NTHLEAQLQK AEEAGAELQA DLRDIQEEKE EIQKKLSESR HQQEAATTQL EQLHQEAKRQ 730 740 750 760 770 780 EEVLARAVQE KEALVREKAA LEVRLQAVER DRQDLAEQLQ GLSSAKELLE SSLFEAQQQN 790 800 810 820 830 840 SVIEVTKGQL EVQIQTVTQA KEVIQGEVRC LKLELDTERS QAEQERDAAA RQLAQAEQEG 850 860 870 880 890 900 KTALEQQKAA HEKEVNQLRE KWMQLETEKE RVSLLETLLQ TQKELADASQ QLERLRQDMK 910 920 930 940 950 960 VQKLKEQETT GILQTQLQEA QRELKEAARQ HRDDLAALQE ESSSLLQDKM DLQKQVEDLK 970 980 990 1000 1010 1020 SQLVAQDDSQ RLVEQEVQEK LRETQEYNRI QKELEREKAS LTLSLMEKEQ RLLVLQEADS 1030 1040 1050 1060 1070 1080 IRQQELSALR QDMQEAQGEQ KELSAQMELL RQEVKEKEAD FLAQEAQLLE ELEASHITEQ 1090 1100 1110 1120 1130 1140 QLRASLWAQE AKAAQLQLRL RSTESQLEAL AAEQQPGNQA QAQAQLASLY SALQQALGSV 1150 1160 1170 1180 1190 1200 CESRPELSGG GDSAPSVWGL EPDQNGARSL FKRGPLLTAL SAEAVASALH KLHQDLWKTQ 1210 1220 1230 1240 1250 1260 QTRDVLRDQV QKLEERLTDT EAEKSQVHTE LQDLQRQLSQ NQEEKSKWEG KQNSLESELM 1270 1280 1290 1300 1310 1320 ELHETMASLQ SRLRRAELQR MEAQGERELL QAAKENLTAQ VEHLQAAVVE ARAQASAAGI 1330 1340 1350 1360 1370 1380 LEEDLRTARS ALKLKNEEVE SERERAQALQ EQGELKVAQG KALQENLALL TQTLAEREEE 1390 1400 1410 1420 1430 1440 VETLRGQIQE LEKQREMQKA ALELLSLDLK KRNQEVDLQQ EQIQELEKCR SVLEHLPMAV 1450 1460 1470 1480 1490 1500 QEREQKLTVQ REQIRELEKD RETQRNVLEH QLLELEKKDQ MIESQRGQVQ DLKKQLVTLE 1510 1520 1530 1540 1550 1560 CLALELEENH HKMECQQKLI KELEGQRETQ RVALTHLTLD LEERSQELQA QSSQIHDLES 1570 1580 1590 1600 1610 1620 HSTVLARELQ ERDQEVKSQR EQIEELQRQK EHLTQDLERR DQELMLQKER IQVLEDQRTR 1630 1640 1650 1660 1670 1680 QTKILEEDLE QIKLSLRERG RELTTQRQLM QERAEEGKGP SKAQRGSLEH MKLILRDKEK 1690 1700 1710 1720 1730 1740 EVECQQEHIH ELQELKDQLE QQLQGLHRKV GETSLLLSQR EQEIVVLQQQ LQEAREQGEL 1750 1760 1770 1780 1790 1800 KEQSLQSQLD EAQRALAQRD QELEALQQEQ QQAQGQEERV KEKADALQGA LEQAHMTLKE 1810 1820 1830 1840 1850 1860 RHGELQDHKE QARRLEEELA VEGRRVQALE EVLGDLRAES REQEKALLAL QQQCAEQAQE 1870 1880 1890 1900 1910 1920 HEVETRALQD SWLQAQAVLK ERDQELEALR AESQSSRHQE EAARARAEAL QEALGKAHAA 1930 1940 1950 1960 1970 1980 LQGKEQHLLE QAELSRSLEA STATLQASLD ACQAHSRQLE EALRIQEGEI QDQDLRYQED 1990 2000 2010 2020 2030 2040 VQQLQQALAQ RDEELRHQQE REQLLEKSLA QRVQENMIQE KQNLGQEREE EEIRGLHQSV 2050 2060 2070 2080 2090 2100 RELQLTLAQK EQEILELRET QQRNNLEALP HSHKTSPMEE QSLKLDSLEP RLQRELERLQ 2110 2120 2130 2140 2150 2160 AALRQTEARE IEWREKAQDL ALSLAQTKAS VSSLQEVAMF LQASVLERDS EQQRLQDELE 2170 2180 2190 2200 2210 2220 LTRRALEKER LHSPGATSTA ELGSRGEQGV QLGEVSGVEA EPSPDGMEKQ SWRQRLEHLQ 2230 2240 2250 2260 2270 2280 QAVARLEIDR SRLQRHNVQL RSTLEQVERE RRKLKREAMR AAQAGSLEIS KATASSPTQQ 2290 2300 2310 2320 2330 2340 DGRGQKNSDA KCVAELQKEV VLLQAQLTLE RKQKQDYITR SAQTSRELAG LHHSLSHSLL 2350 2360 2370 2380 AVAQAPEATV LEAETRRLDE SLTQSLTSPG PVLLHPSPST TQAASR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Autoantibodies to a group of centrosomal proteins in human autoimmune sera reactive with the centrosome." Mack G.J., Rees J., Sandblom O., Balczon R., Fritzler M.J., Rattner J.B. Arthritis Rheum. 41:551-558(1998) [PubMed: 9506584] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS AUTOANTIGEN IN AUTOIMMUNE DISEASES. Tissue: Cervix carcinoma.
[2]	"C-Nap1, a novel centrosomal coiled-coil protein and candidate substrate of the cell cycle-regulated protein kinase Nek2." Fry A.M., Mayor T., Meraldi P., Stierhof Y.-D., Tanaka K., Nigg E.A. J. Cell Biol. 141:1563-1574(1998) [PubMed: 9647649] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH NEK2, SUBCELLULAR LOCATION DURING THE CELL CYCLE. Tissue: Placenta.
[3]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1." Helps N.R., Luo X., Barker H.M., Cohen P.T.W. Biochem. J. 349:509-518(2000) [PubMed: 10880350] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH NEK2 AND PPP1CA.
[5]	"The mechanism regulating the dissociation of the centrosomal protein C-Nap1 from mitotic spindle poles." Mayor T., Hacker U., Stierhof Y.-D., Nigg E.A. J. Cell Sci. 115:3275-3284(2002) [PubMed: 12140259] [Abstract] Cited for: PHOSPHORYLATION DURING CELL CYCLE.
[6]	"A novel function of CEP135 as a platform protein of C-NAP1 for its centriolar localization." Kim K., Lee S., Chang J., Rhee K. Exp. Cell Res. 314:3692-3700(2008) [PubMed: 18851962] [Abstract] Cited for: INTERACTION WITH CEP135.
[7]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2229 AND SER-2259, MASS SPECTROMETRY. Tissue: T-cell.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1048, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF022655 mRNA. Translation: AAC06349.1. AF049105 mRNA. Translation: AAC07988.1. AL121586 Genomic DNA. Translation: CAB89415.1.
IPI	IPI00160622. IPI00292871.
PIR	T08621.
RefSeq	NP_009117.2.
UniGene	Hs.443976
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BV73. 3 interactions.
STRING	Q9BV73.
PTM databases
PhosphoSite	Q9BV73.
Proteomic databases
PRIDE	Q9BV73.
Genome annotation databases
Ensembl	ENST00000356095; ENSP00000348401; ENSG00000126001; Homo sapiens. [Genome view] ENST00000397527; ENSP00000380661; ENSG00000126001; Homo sapiens. [Genome view]
GeneID	11190.
KEGG	hsa:11190.
UCSC	uc002xcm.1. human. uc002xcn.1. human.
Organism-specific databases
CTD	11190.
GeneCards	GC20P033507.
HGNC	HGNC:1859. CEP250.
MIM	609689. gene.
PharmGKB	PA26415.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16155.
HOGENOM	HBG402917.
HOVERGEN	HBG081320.
InParanoid	Q9BV73.
OMA	RDSMRAS.
OrthoDB	EOG970X2J.
PhylomeDB	Q9BV73.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic.
Gene expression databases
ArrayExpress	Q9BV73.
Bgee	Q9BV73.
CleanEx	HS_CEP250.
Genevestigator	Q9BV73.
GermOnline	ENSG00000126001. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	42595.
SOURCE	Search...

Entry information

Entry name

CP250_HUMAN

Accession

Primary (citable) accession number: Q9BV73
Secondary accession number(s): O14812, O60588, Q9H450

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	May 9, 2003
Last modified:	March 2, 2010
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.