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Q5VT06

- CE350_HUMAN

UniProt

Q5VT06 - CE350_HUMAN

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Protein

Centrosome-associated protein 350

Gene
CEP350, CAP350, KIAA0480, GM133
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.5 Publications

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: HPA
  3. nucleus Source: HPA
  4. spindle Source: UniProtKB-SubCell
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.1 Publication

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

ArrayExpressiQ5VT06.
BgeeiQ5VT06.
CleanExiHS_CEP350.
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. 12 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.

Miscellaneous databases

EvolutionaryTraceiQ5VT06.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2517 – 255943CAP-GlyAdd
BLAST

Coiled coil

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5244.
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

MRSSKSKEVP LPNPRNSQSK DTVQADITTS WDALSQTKAA LRHIENKLEV     50
APTSTAVCDS VMDTKKSSTS ATRKISRKDG RYLDDSWVNA PISKSTKSRK 100
EKSRSPLRAT TLESNVKKNN RVEFREPLVS YREIHGAPSN FSSSHLESKH 150
VYCVDVNEEK TESGNWMIGS REERNIRSCD FESSQSSVIN DTVVRFLNDR 200
PAIDALQNSE CLIRMGASMR TEEEMPNRTK GSENNLKLSV NNMAHDTDPK 250
ALRLTDSSPS STSTSNSQRL DILKRRQHDV KLEKLKERIR KQWEHSEETN 300
GRGQKLGHID HPVMVVNVDN SVTAKVRKVA TAPPAPAYKG FNPSETKIRT 350
PDGKVWQEAE FQNMSRELYR DLALHFADDI SIKEKPAEKS KEKKVVKPVR 400
KVQKVAQLSS TECRTGSSHL ISTSSWRDGQ KLVKKILGPA PRMEPKEQRT 450
ASSDRGGRER TAKSGGHIGR AESDPRLDVL HRHLQRNSER SRSKSRSENN 500
IKKLASSLPD NKQEENTALN KDFLPIEIRG ILDDLQLDST AHTAKQDTVE 550
LQNQKSSAPV HAPRSHSPVK RKPDKITANE DPPVISKRRH YDTDEVRQYI 600
VRQQEERKRK QNEEKKAQKE ATEQKNKRLQ ELYRKQKEAF TKVKNVPPSE 650
PSATRRLQET YSKLLLEKTL LEEPSHQHVT QETQAKPGYQ PSGESDKENK 700
VQERPPSASS SSDMSLSEPP QPLARKDLME STWMQPERLS PQVHHSQPQP 750
FAGTAGSLLS HLLSLEHVGI LHKDFESILP TRKNHNMASR PLTFTPQPYV 800
TSPAAYTDAL LKPSASQYKS KLDRIEALKA TAASLSSRIE SEAKKLAGAS 850
INYGSAWNTE YDVQQAPQED GPWTKAVTPP VKDDNEDVFS ARIQKMLGSC 900
VSHATFDDDL PGVGNLSEFK KLPEMIRPQS AISSFRVRSP GPKPEGLLAQ 950
LCKRQTDSSS SDMQACSQDK AKISLGSSID SVSEGPLLSE GSLSEEEGDQ 1000
DGQPLLKVAE ILKEKEFCPG ERNSYEPIKE FQKEAEKFLP LFGHIGGTQS 1050
KGPWEELAKG SPHSVINIFT KSYQLYGKGF EDKLDRGTST SRPLNATATP 1100
LSGVSYEDDF VSSPGTGTST EKKSTLEPHS TLSPQEDHSN RKSAYDPSSV 1150
DVTSQHSSGA QSAASSRSST SSKGKKGKKE KTEWLDSFTG NVQNSLLDEE 1200
KAERGSHQGK KSGTSSKLSV KDFEQTLDTD STLEDLSGHS VSVSSDKGRS 1250
QKTPTSPLSP SSQKSLQFDV AGTSSERSKS SVMPPTITGF KPNAPLTDLN 1300
PAASRTTTEN MAPIPGSKRF SPAGLHHRMA AELSYLNAIE ESVRQLSDVE 1350
RVRGISLAQQ ESVSLAQIIK AQQQRHERDL ALLKLKAEQE ALESQRQLEE 1400
TRNKAAQVHA ESLQQVVQSQ REVTEVLQEA TCKIAAQQSE TARLTTDAAR 1450
QICEMAELTR THISDAVVAS GAPLAILYDH QRQHLPDFVK QLRTRTETDR 1500
KSPSVSLSQS KEGTLDSKHQ KYSASYDSYS ESSGYKNHDR RSSSGSSRQE 1550
SPSVPSCKEN EKKLNGEKIE SSIDEQVQTA ADDSLRSDSV PSLPDEKDST 1600
SIATEYSLKF DESMTEDEIE EQSFRSLLPS ESHRRFNMEK RRGHHDDSDE 1650
EASPEKTTLS TAKELNMPFS GGQDSFSKFT MEMVRQYMKE EEMRAAHQSS 1700
LLRLREKALK EKTKAELAWL EHQKKHLRDK GEDDKMPPLR KKQRGLLLRL 1750
QQEKAEIKRL QEANKAARKE RQLILKQQEE IEKIRQTTIK LQEKLKSAGE 1800
SKLDSHSDDD TKDNKATSPG PTDLETRSPS PISISSSETS SIMQKLKKMR 1850
SRMDEKFLTK REQKLMQRRQ HAEELLEWKR RLDAEEAEIR QMEKQALAAW 1900
DKELIKPKTP KKELEDQRTE QKEIASEEES PVPLYSHLNS ESSIPEELGS 1950
PAVEYVPSES IGQEQPGSPD HSILTEEMIC SQELESSTSP SKHSLPKSCT 2000
SVSKQESSKG SHRTGGQCHL PIKSHQHCYS WSDESLSMTQ SETTSDQSDI 2050
EGRIRALKDE LRKRKSVVNQ LKKEQKKRQK ERLKAQEASL IKQLESYDEF 2100
IKKTEAELSQ DLETSPTAKP QIKTLSSASE KPKIKPLTPL HRSETAKNWK 2150
SLTESERSRG SLESIAEHVD ASLSGSERSV SERSLSAYAK RVNEWDSRTE 2200
DFQTPSPVLR SSRKIREESG DSLENVPALH LLKELNATSR ILDMSDGKVG 2250
ESSKKSEIKE IEYTKLKKSK IEDAFSKEGK SDVLLKLVLE QGDSSEILSK 2300
KDLPLDSENV QKDLVGLAIE NLHKSEEMLK ERQSDQDMNH SPNIQSGKDI 2350
HEQKNTKEKD LSWSEHLFAP KEIPYSEDFE VSSFKKEISA ELYKDDFEVS 2400
SLLSLRKDSQ SCRDKPQPMR SSTSGATSFG SNEEISECLS EKSLSIHSNV 2450
HSDRLLELKS PTELMKSKER SDVEHEQQVT ESPSLASVPT ADELFDFHIG 2500
DRVLIGNVQP GILRFKGETS FAKGFWAGVE LDKPEGNNNG TYDGIAYFEC 2550
KEKHGIFAPP QKISHIPENF DDYVDINEDE DCYSDERYQC YNQEQNDTEG 2600
PKDREKDVSE YFYEKSLPSV NDIEASVNRS RSLKIETDNV QDISGVLEAH 2650
VHQQSSVDSQ ISSKENKDLI SDATEKVSIA AEDDTLDNTF SEELEKQQQF 2700
TEEEDNLYAE ASEKLCTPLL DLLTREKNQL EAQLKSSLNE EKKSKQQLEK 2750
ISLLTDSLLK VFVKDTVNQL QQIKKTRDEK IQLSNQELLG DDQKKVTPQD 2800
LSQNVEEQSP SISGCFLSSE LEDEKEEISS PDMCPRPESP VFGASGQEEL 2850
AKRLAELELS REFLSALGDD QDWFDEDFGL SSSHKIQKNK AEETIVPLMA 2900
EPKRVTQQPC ETLLAVPHTA EEVEILVHNA AEELWKWKEL GHDLHSISIP 2950
TKLLGCASKG LDIESTSKRV YKQAVFDLTK EIFEEIFAED PNLNQPVWMK 3000
PCRINSSYFR RVKNPNNLDE IKSFIASEVL KLFSLKKEPN HKTDWQKMMK 3050
FGRKKRDRVD HILVQELHEE EAQWVNYDED ELCVKMQLAD GIFETLIKDT 3100
IDVLNQISEK QGRMLLV 3117
Length:3,117
Mass (Da):350,930
Last modified:December 7, 2004 - v1
Checksum:iDD0E03EA96DA319E
GO

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 conflict

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

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. 12 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.
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

ArrayExpressi Q5VT06.
Bgeei Q5VT06.
CleanExi HS_CEP350.
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: September 3, 2014
This is version 102 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

Dasty 3

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