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Q5VT06

- CE350_HUMAN

UniProt

Q5VT06 - CE350_HUMAN

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Protein

Centrosome-associated protein 350

Gene

CEP350

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CENPJ. Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network. Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity.5 Publications

GO - Biological processi

  1. microtubule anchoring Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Centrosome-associated protein 350
Short name:
Cep350
Alternative name(s):
Centrosome-associated protein of 350 kDa
Gene namesi
Name:CEP350
Synonyms:CAP350, KIAA0480
ORF Names:GM133
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:24238. CEP350.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Nucleus
Note: Associated with mitotic spindles. Nuclear, in discrete foci. Associated with intermediate filaments. Also present in the pericentrosomal area.

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: HPA
  3. membrane Source: UniProtKB
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi762 – 7632LL → AA: Abolishes recruitment of PPARA to specific nuclear foci. No effect on interaction with PPARA (in vitro). 1 Publication

Organism-specific databases

PharmGKBiPA143485434.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31173117Centrosome-associated protein 350PRO_0000233291Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei878 – 8781Phosphothreonine1 Publication
Modified residuei1061 – 10611Phosphoserine1 Publication
Modified residuei1253 – 12531Phosphothreonine1 Publication
Modified residuei1256 – 12561Phosphoserine1 Publication
Modified residuei1259 – 12591Phosphoserine1 Publication
Modified residuei2204 – 22041Phosphothreonine1 Publication
Modified residuei2206 – 22061Phosphoserine1 Publication
Modified residuei2460 – 24601Phosphoserine1 Publication
Modified residuei2839 – 28391Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated during mitosis.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5VT06.
PaxDbiQ5VT06.
PRIDEiQ5VT06.

PTM databases

PhosphoSiteiQ5VT06.

Expressioni

Tissue specificityi

Detected in heart, brain, skeletal muscle, testis, placenta, lung, liver, kidney and pancreas.2 Publications

Gene expression databases

BgeeiQ5VT06.
CleanExiHS_CEP350.
ExpressionAtlasiQ5VT06. baseline and differential.
GenevestigatoriQ5VT06.

Organism-specific databases

HPAiHPA028355.
HPA028357.
HPA030845.

Interactioni

Subunit structurei

Part of a ternary complex composed of SASS6, CENPJ and CEP350. Part of a ternary complex that contains CEP350, FGFR1OP and MAPRE1. Interacts directly with FGFR1OP via its C-terminus. Interacts with NR1H3, PPARA, PPARD and PPARG. Interacts directly with microtubules. Interacts with the fusion protein FGFR1OP-FGFR1, and by doing so recruits and activates PI3K and PLC-gamma.5 Publications

Protein-protein interaction databases

BioGridi115191. 14 interactions.
IntActiQ5VT06. 4 interactions.
MINTiMINT-2867672.
STRINGi9606.ENSP00000356579.

Structurei

Secondary structure

1
3117
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2483 – 24864
Beta strandi2501 – 25055
Turni2506 – 25083
Beta strandi2509 – 251810
Beta strandi2520 – 253314
Beta strandi2536 – 25383
Beta strandi2540 – 25423
Beta strandi2555 – 25584
Helixi2560 – 25623

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2COZNMR-A2473-2581[»]
ProteinModelPortaliQ5VT06.
SMRiQ5VT06. Positions 2467-2581.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5VT06.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2517 – 255943CAP-GlyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili598 – 64548Sequence AnalysisAdd
BLAST
Coiled coili1369 – 141143Sequence AnalysisAdd
BLAST
Coiled coili1707 – 180094Sequence AnalysisAdd
BLAST
Coiled coili1856 – 189944Sequence AnalysisAdd
BLAST
Coiled coili2051 – 211060Sequence AnalysisAdd
BLAST
Coiled coili2719 – 275234Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1112 – 1281170Ser-richAdd
BLAST
Compositional biasi1502 – 155655Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 CAP-Gly domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5244.
GeneTreeiENSGT00760000119173.
HOGENOMiHOG000111528.
HOVERGENiHBG095435.
InParanoidiQ5VT06.
KOiK16768.
OMAiQWEHSEE.
OrthoDBiEOG7G4QD6.
PhylomeDBiQ5VT06.
TreeFamiTF329845.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR028750. CEP350.
[Graphical view]
PANTHERiPTHR13958. PTHR13958. 1 hit.
PfamiPF01302. CAP_GLY. 1 hit.
[Graphical view]
SMARTiSM01052. CAP_GLY. 1 hit.
[Graphical view]
SUPFAMiSSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5VT06-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRSSKSKEVP LPNPRNSQSK DTVQADITTS WDALSQTKAA LRHIENKLEV
60 70 80 90 100
APTSTAVCDS VMDTKKSSTS ATRKISRKDG RYLDDSWVNA PISKSTKSRK
110 120 130 140 150
EKSRSPLRAT TLESNVKKNN RVEFREPLVS YREIHGAPSN FSSSHLESKH
160 170 180 190 200
VYCVDVNEEK TESGNWMIGS REERNIRSCD FESSQSSVIN DTVVRFLNDR
210 220 230 240 250
PAIDALQNSE CLIRMGASMR TEEEMPNRTK GSENNLKLSV NNMAHDTDPK
260 270 280 290 300
ALRLTDSSPS STSTSNSQRL DILKRRQHDV KLEKLKERIR KQWEHSEETN
310 320 330 340 350
GRGQKLGHID HPVMVVNVDN SVTAKVRKVA TAPPAPAYKG FNPSETKIRT
360 370 380 390 400
PDGKVWQEAE FQNMSRELYR DLALHFADDI SIKEKPAEKS KEKKVVKPVR
410 420 430 440 450
KVQKVAQLSS TECRTGSSHL ISTSSWRDGQ KLVKKILGPA PRMEPKEQRT
460 470 480 490 500
ASSDRGGRER TAKSGGHIGR AESDPRLDVL HRHLQRNSER SRSKSRSENN
510 520 530 540 550
IKKLASSLPD NKQEENTALN KDFLPIEIRG ILDDLQLDST AHTAKQDTVE
560 570 580 590 600
LQNQKSSAPV HAPRSHSPVK RKPDKITANE DPPVISKRRH YDTDEVRQYI
610 620 630 640 650
VRQQEERKRK QNEEKKAQKE ATEQKNKRLQ ELYRKQKEAF TKVKNVPPSE
660 670 680 690 700
PSATRRLQET YSKLLLEKTL LEEPSHQHVT QETQAKPGYQ PSGESDKENK
710 720 730 740 750
VQERPPSASS SSDMSLSEPP QPLARKDLME STWMQPERLS PQVHHSQPQP
760 770 780 790 800
FAGTAGSLLS HLLSLEHVGI LHKDFESILP TRKNHNMASR PLTFTPQPYV
810 820 830 840 850
TSPAAYTDAL LKPSASQYKS KLDRIEALKA TAASLSSRIE SEAKKLAGAS
860 870 880 890 900
INYGSAWNTE YDVQQAPQED GPWTKAVTPP VKDDNEDVFS ARIQKMLGSC
910 920 930 940 950
VSHATFDDDL PGVGNLSEFK KLPEMIRPQS AISSFRVRSP GPKPEGLLAQ
960 970 980 990 1000
LCKRQTDSSS SDMQACSQDK AKISLGSSID SVSEGPLLSE GSLSEEEGDQ
1010 1020 1030 1040 1050
DGQPLLKVAE ILKEKEFCPG ERNSYEPIKE FQKEAEKFLP LFGHIGGTQS
1060 1070 1080 1090 1100
KGPWEELAKG SPHSVINIFT KSYQLYGKGF EDKLDRGTST SRPLNATATP
1110 1120 1130 1140 1150
LSGVSYEDDF VSSPGTGTST EKKSTLEPHS TLSPQEDHSN RKSAYDPSSV
1160 1170 1180 1190 1200
DVTSQHSSGA QSAASSRSST SSKGKKGKKE KTEWLDSFTG NVQNSLLDEE
1210 1220 1230 1240 1250
KAERGSHQGK KSGTSSKLSV KDFEQTLDTD STLEDLSGHS VSVSSDKGRS
1260 1270 1280 1290 1300
QKTPTSPLSP SSQKSLQFDV AGTSSERSKS SVMPPTITGF KPNAPLTDLN
1310 1320 1330 1340 1350
PAASRTTTEN MAPIPGSKRF SPAGLHHRMA AELSYLNAIE ESVRQLSDVE
1360 1370 1380 1390 1400
RVRGISLAQQ ESVSLAQIIK AQQQRHERDL ALLKLKAEQE ALESQRQLEE
1410 1420 1430 1440 1450
TRNKAAQVHA ESLQQVVQSQ REVTEVLQEA TCKIAAQQSE TARLTTDAAR
1460 1470 1480 1490 1500
QICEMAELTR THISDAVVAS GAPLAILYDH QRQHLPDFVK QLRTRTETDR
1510 1520 1530 1540 1550
KSPSVSLSQS KEGTLDSKHQ KYSASYDSYS ESSGYKNHDR RSSSGSSRQE
1560 1570 1580 1590 1600
SPSVPSCKEN EKKLNGEKIE SSIDEQVQTA ADDSLRSDSV PSLPDEKDST
1610 1620 1630 1640 1650
SIATEYSLKF DESMTEDEIE EQSFRSLLPS ESHRRFNMEK RRGHHDDSDE
1660 1670 1680 1690 1700
EASPEKTTLS TAKELNMPFS GGQDSFSKFT MEMVRQYMKE EEMRAAHQSS
1710 1720 1730 1740 1750
LLRLREKALK EKTKAELAWL EHQKKHLRDK GEDDKMPPLR KKQRGLLLRL
1760 1770 1780 1790 1800
QQEKAEIKRL QEANKAARKE RQLILKQQEE IEKIRQTTIK LQEKLKSAGE
1810 1820 1830 1840 1850
SKLDSHSDDD TKDNKATSPG PTDLETRSPS PISISSSETS SIMQKLKKMR
1860 1870 1880 1890 1900
SRMDEKFLTK REQKLMQRRQ HAEELLEWKR RLDAEEAEIR QMEKQALAAW
1910 1920 1930 1940 1950
DKELIKPKTP KKELEDQRTE QKEIASEEES PVPLYSHLNS ESSIPEELGS
1960 1970 1980 1990 2000
PAVEYVPSES IGQEQPGSPD HSILTEEMIC SQELESSTSP SKHSLPKSCT
2010 2020 2030 2040 2050
SVSKQESSKG SHRTGGQCHL PIKSHQHCYS WSDESLSMTQ SETTSDQSDI
2060 2070 2080 2090 2100
EGRIRALKDE LRKRKSVVNQ LKKEQKKRQK ERLKAQEASL IKQLESYDEF
2110 2120 2130 2140 2150
IKKTEAELSQ DLETSPTAKP QIKTLSSASE KPKIKPLTPL HRSETAKNWK
2160 2170 2180 2190 2200
SLTESERSRG SLESIAEHVD ASLSGSERSV SERSLSAYAK RVNEWDSRTE
2210 2220 2230 2240 2250
DFQTPSPVLR SSRKIREESG DSLENVPALH LLKELNATSR ILDMSDGKVG
2260 2270 2280 2290 2300
ESSKKSEIKE IEYTKLKKSK IEDAFSKEGK SDVLLKLVLE QGDSSEILSK
2310 2320 2330 2340 2350
KDLPLDSENV QKDLVGLAIE NLHKSEEMLK ERQSDQDMNH SPNIQSGKDI
2360 2370 2380 2390 2400
HEQKNTKEKD LSWSEHLFAP KEIPYSEDFE VSSFKKEISA ELYKDDFEVS
2410 2420 2430 2440 2450
SLLSLRKDSQ SCRDKPQPMR SSTSGATSFG SNEEISECLS EKSLSIHSNV
2460 2470 2480 2490 2500
HSDRLLELKS PTELMKSKER SDVEHEQQVT ESPSLASVPT ADELFDFHIG
2510 2520 2530 2540 2550
DRVLIGNVQP GILRFKGETS FAKGFWAGVE LDKPEGNNNG TYDGIAYFEC
2560 2570 2580 2590 2600
KEKHGIFAPP QKISHIPENF DDYVDINEDE DCYSDERYQC YNQEQNDTEG
2610 2620 2630 2640 2650
PKDREKDVSE YFYEKSLPSV NDIEASVNRS RSLKIETDNV QDISGVLEAH
2660 2670 2680 2690 2700
VHQQSSVDSQ ISSKENKDLI SDATEKVSIA AEDDTLDNTF SEELEKQQQF
2710 2720 2730 2740 2750
TEEEDNLYAE ASEKLCTPLL DLLTREKNQL EAQLKSSLNE EKKSKQQLEK
2760 2770 2780 2790 2800
ISLLTDSLLK VFVKDTVNQL QQIKKTRDEK IQLSNQELLG DDQKKVTPQD
2810 2820 2830 2840 2850
LSQNVEEQSP SISGCFLSSE LEDEKEEISS PDMCPRPESP VFGASGQEEL
2860 2870 2880 2890 2900
AKRLAELELS REFLSALGDD QDWFDEDFGL SSSHKIQKNK AEETIVPLMA
2910 2920 2930 2940 2950
EPKRVTQQPC ETLLAVPHTA EEVEILVHNA AEELWKWKEL GHDLHSISIP
2960 2970 2980 2990 3000
TKLLGCASKG LDIESTSKRV YKQAVFDLTK EIFEEIFAED PNLNQPVWMK
3010 3020 3030 3040 3050
PCRINSSYFR RVKNPNNLDE IKSFIASEVL KLFSLKKEPN HKTDWQKMMK
3060 3070 3080 3090 3100
FGRKKRDRVD HILVQELHEE EAQWVNYDED ELCVKMQLAD GIFETLIKDT
3110
IDVLNQISEK QGRMLLV
Length:3,117
Mass (Da):350,930
Last modified:December 7, 2004 - v1
Checksum:iDD0E03EA96DA319E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251Missing in AAL91355. (PubMed:11891061)Curated
Sequence conflicti114 – 1141S → G in AAL55733. 1 PublicationCurated
Sequence conflicti459 – 4591E → R in AAL55733. 1 PublicationCurated
Sequence conflicti2164 – 21641S → P in AAL55733. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti892 – 8921R → T.
Corresponds to variant rs6692219 [ dbSNP | Ensembl ].
VAR_059202
Natural varianti945 – 9451E → Q.1 Publication
Corresponds to variant rs2477120 [ dbSNP | Ensembl ].
VAR_026126
Natural varianti1213 – 12131G → V.
Corresponds to variant rs12125245 [ dbSNP | Ensembl ].
VAR_059203
Natural varianti1445 – 14451T → A.
Corresponds to variant rs16855164 [ dbSNP | Ensembl ].
VAR_048671
Natural varianti1446 – 14461T → A.
Corresponds to variant rs16855164 [ dbSNP | Ensembl ].
VAR_059204
Natural varianti1517 – 15171S → A.
Corresponds to variant rs12124336 [ dbSNP | Ensembl ].
VAR_059205
Natural varianti2044 – 20441T → P.
Corresponds to variant rs56173179 [ dbSNP | Ensembl ].
VAR_061092

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF287356 mRNA. Translation: AAL55733.1.
AL645487, AL390718, AL590632 Genomic DNA. Translation: CAH72345.1.
AL590632, AL390718, AL645487 Genomic DNA. Translation: CAI15177.1.
AL390718, AL590632, AL645487 Genomic DNA. Translation: CAI14833.1.
AF387614 mRNA. Translation: AAL91355.1.
CCDSiCCDS1336.1.
PIRiT00263.
RefSeqiNP_055625.4. NM_014810.4.
UniGeneiHs.413045.

Genome annotation databases

EnsembliENST00000367607; ENSP00000356579; ENSG00000135837.
GeneIDi9857.
KEGGihsa:9857.
UCSCiuc001gnt.3. human.

Polymorphism databases

DMDMi74746869.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF287356 mRNA. Translation: AAL55733.1 .
AL645487 , AL390718 , AL590632 Genomic DNA. Translation: CAH72345.1 .
AL590632 , AL390718 , AL645487 Genomic DNA. Translation: CAI15177.1 .
AL390718 , AL590632 , AL645487 Genomic DNA. Translation: CAI14833.1 .
AF387614 mRNA. Translation: AAL91355.1 .
CCDSi CCDS1336.1.
PIRi T00263.
RefSeqi NP_055625.4. NM_014810.4.
UniGenei Hs.413045.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2COZ NMR - A 2473-2581 [» ]
ProteinModelPortali Q5VT06.
SMRi Q5VT06. Positions 2467-2581.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115191. 14 interactions.
IntActi Q5VT06. 4 interactions.
MINTi MINT-2867672.
STRINGi 9606.ENSP00000356579.

PTM databases

PhosphoSitei Q5VT06.

Polymorphism databases

DMDMi 74746869.

Proteomic databases

MaxQBi Q5VT06.
PaxDbi Q5VT06.
PRIDEi Q5VT06.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367607 ; ENSP00000356579 ; ENSG00000135837 .
GeneIDi 9857.
KEGGi hsa:9857.
UCSCi uc001gnt.3. human.

Organism-specific databases

CTDi 9857.
GeneCardsi GC01P179923.
H-InvDB HIX0001384.
HGNCi HGNC:24238. CEP350.
HPAi HPA028355.
HPA028357.
HPA030845.
neXtProti NX_Q5VT06.
PharmGKBi PA143485434.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5244.
GeneTreei ENSGT00760000119173.
HOGENOMi HOG000111528.
HOVERGENi HBG095435.
InParanoidi Q5VT06.
KOi K16768.
OMAi QWEHSEE.
OrthoDBi EOG7G4QD6.
PhylomeDBi Q5VT06.
TreeFami TF329845.

Miscellaneous databases

ChiTaRSi CEP350. human.
EvolutionaryTracei Q5VT06.
GeneWikii CEP350.
GenomeRNAii 9857.
NextBioi 37150.
PROi Q5VT06.

Gene expression databases

Bgeei Q5VT06.
CleanExi HS_CEP350.
ExpressionAtlasi Q5VT06. baseline and differential.
Genevestigatori Q5VT06.

Family and domain databases

Gene3Di 2.30.30.190. 1 hit.
InterProi IPR000938. CAP-Gly_domain.
IPR028750. CEP350.
[Graphical view ]
PANTHERi PTHR13958. PTHR13958. 1 hit.
Pfami PF01302. CAP_GLY. 1 hit.
[Graphical view ]
SMARTi SM01052. CAP_GLY. 1 hit.
[Graphical view ]
SUPFAMi SSF74924. SSF74924. 1 hit.
PROSITEi PS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a cDNA encoding a protein of 350 kDa (CAP350) associated with centrosomes."
    Klein-Hitpass L., Esser F., Michels D., Schwerk C., Vassen L.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-945.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Identification of six novel genes by experimental validation of GeneMachine predicted genes."
    Makalowska I., Sood R., Faruque M.U., Hu P., Robbins C.M., Eddings E.M., Mestre J.D., Baxevanis A.D., Carpten J.D.
    Gene 284:203-213(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-131, IDENTIFICATION, TISSUE SPECIFICITY.
  4. "Proteomic characterization of the human centrosome by protein correlation profiling."
    Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.
    Nature 426:570-574(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Lymphoblast.
  5. "Activity and subcellular compartmentalization of peroxisome proliferator-activated receptor alpha are altered by the centrosome-associated protein CAP350."
    Patel H., Truant R., Rachubinski R.A., Capone J.P.
    J. Cell Sci. 118:175-186(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 762-LEU-LEU-763, INTERACTION WITH NR1H3; PPARA; PPARD AND PPARG.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2839, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "A complex of two centrosomal proteins, CAP350 and FOP, cooperates with EB1 in microtubule anchoring."
    Yan X., Habedanck R., Nigg E.A.
    Mol. Biol. Cell 17:634-644(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH FGFR1OP.
  8. "Centrosomal CAP350 protein stabilises microtubules associated with the Golgi complex."
    Hoppeler-Lebel A., Celati C., Bellett G., Mogensen M.M., Klein-Hitpass L., Bornens M., Tassin A.-M.
    J. Cell Sci. 120:3299-3308(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MICROTUBULE.
  9. "Myeloproliferative disorder FOP-FGFR1 fusion kinase recruits phosphoinositide-3 kinase and phospholipase Cgamma at the centrosome."
    Lelievre H., Chevrier V., Tassin A.-M., Birnbaum D.
    Mol. Cancer 7:30-30(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FGFR1OP-FGFR1 FUSION PROTEIN.
  10. "Role of CAP350 in centriolar tubule stability and centriole assembly."
    Le Clech M.
    PLoS ONE 3:E3855-E3855(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH SASS6 AND CENPJ.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-878; THR-1253; SER-1256; SER-1259; THR-2204; SER-2206 AND SER-2460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Solution structure of the CAP-Gly domain in human centrosome-associated protein CAP350."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 2473-2581.

Entry informationi

Entry nameiCE350_HUMAN
AccessioniPrimary (citable) accession number: Q5VT06
Secondary accession number(s): O75068, Q8TDK3, Q8WY20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: December 7, 2004
Last modified: October 29, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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