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Protein

Centrosomal protein of 170 kDa

Gene

CEP170

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

Functioni

Plays a role in microtubule organization.1 Publication

Names & Taxonomyi

Protein namesi
Recommended name:
Centrosomal protein of 170 kDa
Short name:
Cep170
Alternative name(s):
KARP-1-binding protein
Short name:
KARP1-binding protein
Gene namesi
Name:CEP170
Synonyms:FAM68A, KAB, KIAA0470
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:28920. CEP170.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: MGI
  • centrosome Source: UniProtKB
  • cytoplasm Source: HPA
  • microtubule Source: UniProtKB-KW
  • nuclear membrane Source: HPA
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128395757.

Polymorphism and mutation databases

BioMutaiCEP170.
DMDMi74743919.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15841584Centrosomal protein of 170 kDaPRO_0000282887Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei356 – 3561Phosphoserine4 Publications
Modified residuei359 – 3591Phosphoserine4 Publications
Modified residuei364 – 3641Phosphotyrosine1 Publication
Modified residuei446 – 4461Phosphoserine1 Publication
Modified residuei497 – 4971Phosphoserine1 Publication
Modified residuei501 – 5011Phosphothreonine1 Publication
Modified residuei633 – 6331Phosphoserine2 Publications
Modified residuei636 – 6361Phosphoserine3 Publications
Modified residuei838 – 8381Phosphoserine1 Publication
Modified residuei930 – 9301Phosphoserine1 Publication
Modified residuei933 – 9331Phosphoserine1 Publication
Modified residuei958 – 9581Phosphoserine1 Publication
Modified residuei1112 – 11121Phosphoserine3 Publications
Modified residuei1114 – 11141Phosphoserine1 Publication
Modified residuei1160 – 11601Phosphoserine1 Publication
Modified residuei1165 – 11651Phosphoserine1 Publication
Modified residuei1251 – 12511Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated; probably by PLK1.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5SW79.
PaxDbiQ5SW79.
PRIDEiQ5SW79.

PTM databases

PhosphoSiteiQ5SW79.

Miscellaneous databases

PMAP-CutDBQ5SW79.

Expressioni

Gene expression databases

BgeeiQ5SW79.
CleanExiHS_CEP170.
ExpressionAtlasiQ5SW79. baseline and differential.
GenevisibleiQ5SW79. HS.

Organism-specific databases

HPAiHPA042151.
HPA045787.

Interactioni

Subunit structurei

Interacts with PLK1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
vprP125204EBI-1104799,EBI-6164519From a different organism.

Protein-protein interaction databases

BioGridi115193. 58 interactions.
DIPiDIP-37594N.
IntActiQ5SW79. 15 interactions.
MINTiMINT-1790395.
STRINGi9606.ENSP00000355500.

Structurei

Secondary structure

1
1584
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Beta strandi15 – 173Combined sources
Beta strandi23 – 297Combined sources
Beta strandi31 – 333Combined sources
Beta strandi44 – 496Combined sources
Turni50 – 534Combined sources
Beta strandi54 – 596Combined sources
Beta strandi66 – 683Combined sources
Beta strandi86 – 894Combined sources
Beta strandi96 – 1049Combined sources
Helixi107 – 1115Combined sources
Helixi113 – 1208Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JONX-ray2.15A/B/C/D/E1-126[»]
ProteinModelPortaliQ5SW79.
SMRiQ5SW79. Positions 1-123.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 7351FHAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni853 – 1584732Targeting to microtubulesAdd
BLAST
Regioni1113 – 1584472Targeting to centrosomesAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1467 – 149529Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the CEP170 family.Curated
Contains 1 FHA domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG18196.
GeneTreeiENSGT00640000091476.
HOVERGENiHBG058059.
InParanoidiQ5SW79.
KOiK16463.
OMAiHGEMHKL.
OrthoDBiEOG741Z19.
PhylomeDBiQ5SW79.
TreeFamiTF328469.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR026644. CEP170.
IPR029300. CEP170_C.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR15715:SF17. PTHR15715:SF17. 1 hit.
PfamiPF15308. CEP170_C. 1 hit.
PF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5SW79-1) [UniParc]FASTAAdd to basket

Also known as: Alpha

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.

« Hide

        10         20         30         40         50
MSLTSWFLVS SGGTRHRLPR EMIFVGRDDC ELMLQSRSVD KQHAVINYDA
60 70 80 90 100
STDEHLVKDL GSLNGTFVND VRIPEQTYIT LKLEDKLRFG YDTNLFTVVQ
110 120 130 140 150
GEMRVPEEAL KHEKFTIQLQ LSQKSSESEL SKSASAKSID SKVADAATEV
160 170 180 190 200
QHKTTEALKS EEKAMDISAM PRGTPLYGQP SWWGDDEVDE KRAFKTNGKP
210 220 230 240 250
EEKNHEAGTS GCGIDAKQVE EQSAAANEEV LFPFCREPSY FEIPTKEFQQ
260 270 280 290 300
PSQITESTIH EIPTKDTPSS HITGAGHASF TIEFDDSTPG KVTIRDHVTK
310 320 330 340 350
FTSDQRHKSK KSSPGTQDLL GIQTGMMAPE NKVADWLAQN NPPQMLWERT
360 370 380 390 400
EEDSKSIKSD VPVYLKRLKG NKHDDGTQSD SENAGAHRRC SKRATLEEHL
410 420 430 440 450
RRHHSEHKKL QKVQATEKHQ DQAVTSSAHH RGGHGVPHGK LLKQKSEEPS
460 470 480 490 500
VSIPFLQTAL LRSSGSLGHR PSQEMDKMLK NQATSATSEK DNDDDQSDKG
510 520 530 540 550
TYTIELENPN SEEVEARKMI DKVFGVDDNQ DYNRPVINEK HKDLIKDWAL
560 570 580 590 600
SSAAAVMEER KPLTTSGFHH SEEGTSSSGS KRWVSQWASL AANHTRHDQE
610 620 630 640 650
ERIMEFSAPL PLENETEISE SGMTVRSTGS ATSLASQGER RRRTLPQLPN
660 670 680 690 700
EEKSLESHRA KVVTQRSEIG EKQDTELQEK ETPTQVYQKD KQDADRPLSK
710 720 730 740 750
MNRAVNGETL KTGGDNKTLL HLGSSAPGKE KSETDKETSL VKQTLAKLQQ
760 770 780 790 800
QEQREEAQWT PTKLSSKNVS GQTDKCREET FKQESQPPEK NSGHSTSKGD
810 820 830 840 850
RVAQSESKRR KAEEILKSQT PKGGDKKESS KSLVRQGSFT IEKPSPNIPI
860 870 880 890 900
ELIPHINKQT SSTPSSLALT SASRIRERSE SLDPDSSMDT TLILKDTEAV
910 920 930 940 950
MAFLEAKLRE DNKTDEGPDT PSYNRDNSIS PESDVDTAST ISLVTGETER
960 970 980 990 1000
KSTQKRKSFT SLYKDRCSTG SPSKDVTKSS SSGAREKMEK KTKSRSTDVG
1010 1020 1030 1040 1050
SRADGRKFVQ SSGRIRQPSV DLTDDDQTSS VPHSAISDIM SSDQETYSCK
1060 1070 1080 1090 1100
PHGRTPLTSA DEHVHSKLEG SKVTKSKTSP VVSGSSSKST TLPRPRPTRT
1110 1120 1130 1140 1150
SLLRRARLGE ASDSELADAD KASVASEVST TSSTSKPPTG RRNISRIDLL
1160 1170 1180 1190 1200
AQPRRTRLGS LSARSDSEAT ISRSSASSRT AEAIIRSGAR LVPSDKFSPR
1210 1220 1230 1240 1250
IRANSISRLS DSKVKSMTSA HGSASVNSRW RRFPTDYAST SEDEFGSNRN
1260 1270 1280 1290 1300
SPKHTRLRTS PALKTTRLQS AGSAMPTSSS FKHRIKEQED YIRDWTAHRE
1310 1320 1330 1340 1350
EIARISQDLA LIAREINDVA GEIDSVTSSG TAPSTTVSTA ATTPGSAIDT
1360 1370 1380 1390 1400
REELVDRVFD ESLNFRKIPP LVHSKTPEGN NGRSGDPRPQ AAEPPDHLTI
1410 1420 1430 1440 1450
TRRRTWSRDE VMGDNLLLSS VFQFSKKIRQ SIDKTAGKIR ILFKDKDRNW
1460 1470 1480 1490 1500
DDIESKLRAE SEVPIVKTSS MEISSILQEL KRVEKQLQAI NAMIDPDGTL
1510 1520 1530 1540 1550
EALNNMGFPS AMLPSPPKQK SSPVNNHHSP GQTPTLGQPE ARALHPAAVS
1560 1570 1580
AAAEFENAES EADFSIHFNR FNPDGEEEDV TVQE
Length:1,584
Mass (Da):175,293
Last modified:December 21, 2004 - v1
Checksum:i50E981650D21B2E6
GO
Isoform 2 (identifier: Q5SW79-2) [UniParc]FASTAAdd to basket

Also known as: Gamma, 3

The sequence of this isoform differs from the canonical sequence as follows:
     425-522: Missing.
     1226-1261: Missing.
     1353-1353: E → EVGDLHGEMHK

Show »
Length:1,460
Mass (Da):161,408
Checksum:i4EEECA047C7B0EFA
GO
Isoform 3 (identifier: Q5SW79-3) [UniParc]FASTAAdd to basket

Also known as: Beta, KAB2

The sequence of this isoform differs from the canonical sequence as follows:
     425-522: Missing.

Show »
Length:1,486
Mass (Da):164,539
Checksum:i376DEE4949EC24D1
GO

Sequence cautioni

The sequence BAA32315.2 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti213 – 2131G → S.3 Publications
Corresponds to variant rs2631092 [ dbSNP | Ensembl ].
VAR_031437

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei425 – 52298Missing in isoform 2 and isoform 3. 3 PublicationsVSP_024240Add
BLAST
Alternative sequencei1226 – 126136Missing in isoform 2. 3 PublicationsVSP_024241Add
BLAST
Alternative sequencei1353 – 13531E → EVGDLHGEMHK in isoform 2. 3 PublicationsVSP_024242

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022657 mRNA. Translation: BAA83378.1.
AB022658 mRNA. Translation: BAA83379.1.
AB022659 mRNA. Translation: BAA83380.1.
AB007939 mRNA. Translation: BAA32315.2. Different initiation.
AL606534, AC092782 Genomic DNA. Translation: CAI12943.1.
AL606534, AC092782 Genomic DNA. Translation: CAI12944.1.
AL606534, AC092782 Genomic DNA. Translation: CAI12945.1.
BC050722 mRNA. Translation: AAH50722.1. Different termination.
CCDSiCCDS44337.1. [Q5SW79-3]
CCDS44338.1. [Q5SW79-2]
CCDS44339.1. [Q5SW79-1]
PIRiT00095.
RefSeqiNP_001035863.1. NM_001042404.1. [Q5SW79-3]
NP_001035864.1. NM_001042405.1. [Q5SW79-2]
NP_055627.2. NM_014812.2. [Q5SW79-1]
UniGeneiHs.533635.

Genome annotation databases

EnsembliENST00000366542; ENSP00000355500; ENSG00000143702.
ENST00000366543; ENSP00000355501; ENSG00000143702. [Q5SW79-2]
ENST00000366544; ENSP00000355502; ENSG00000143702. [Q5SW79-3]
ENST00000450306; ENSP00000482707; ENSG00000276725. [Q5SW79-3]
ENST00000612450; ENSP00000483344; ENSG00000276725.
ENST00000621831; ENSP00000484359; ENSG00000276725. [Q5SW79-2]
GeneIDi9859.
KEGGihsa:9859.
UCSCiuc021plo.1. human. [Q5SW79-1]
uc021plp.1. human. [Q5SW79-2]
uc021plq.1. human. [Q5SW79-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022657 mRNA. Translation: BAA83378.1.
AB022658 mRNA. Translation: BAA83379.1.
AB022659 mRNA. Translation: BAA83380.1.
AB007939 mRNA. Translation: BAA32315.2. Different initiation.
AL606534, AC092782 Genomic DNA. Translation: CAI12943.1.
AL606534, AC092782 Genomic DNA. Translation: CAI12944.1.
AL606534, AC092782 Genomic DNA. Translation: CAI12945.1.
BC050722 mRNA. Translation: AAH50722.1. Different termination.
CCDSiCCDS44337.1. [Q5SW79-3]
CCDS44338.1. [Q5SW79-2]
CCDS44339.1. [Q5SW79-1]
PIRiT00095.
RefSeqiNP_001035863.1. NM_001042404.1. [Q5SW79-3]
NP_001035864.1. NM_001042405.1. [Q5SW79-2]
NP_055627.2. NM_014812.2. [Q5SW79-1]
UniGeneiHs.533635.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JONX-ray2.15A/B/C/D/E1-126[»]
ProteinModelPortaliQ5SW79.
SMRiQ5SW79. Positions 1-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115193. 58 interactions.
DIPiDIP-37594N.
IntActiQ5SW79. 15 interactions.
MINTiMINT-1790395.
STRINGi9606.ENSP00000355500.

PTM databases

PhosphoSiteiQ5SW79.

Polymorphism and mutation databases

BioMutaiCEP170.
DMDMi74743919.

Proteomic databases

MaxQBiQ5SW79.
PaxDbiQ5SW79.
PRIDEiQ5SW79.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366542; ENSP00000355500; ENSG00000143702.
ENST00000366543; ENSP00000355501; ENSG00000143702. [Q5SW79-2]
ENST00000366544; ENSP00000355502; ENSG00000143702. [Q5SW79-3]
ENST00000450306; ENSP00000482707; ENSG00000276725. [Q5SW79-3]
ENST00000612450; ENSP00000483344; ENSG00000276725.
ENST00000621831; ENSP00000484359; ENSG00000276725. [Q5SW79-2]
GeneIDi9859.
KEGGihsa:9859.
UCSCiuc021plo.1. human. [Q5SW79-1]
uc021plp.1. human. [Q5SW79-2]
uc021plq.1. human. [Q5SW79-3]

Organism-specific databases

CTDi9859.
GeneCardsiGC01M243287.
H-InvDBHIX0004456.
HGNCiHGNC:28920. CEP170.
HPAiHPA042151.
HPA045787.
MIMi613023. gene.
neXtProtiNX_Q5SW79.
PharmGKBiPA128395757.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG18196.
GeneTreeiENSGT00640000091476.
HOVERGENiHBG058059.
InParanoidiQ5SW79.
KOiK16463.
OMAiHGEMHKL.
OrthoDBiEOG741Z19.
PhylomeDBiQ5SW79.
TreeFamiTF328469.

Miscellaneous databases

GeneWikiiCEP170.
GenomeRNAii9859.
NextBioi37158.
PMAP-CutDBQ5SW79.
PROiQ5SW79.
SOURCEiSearch...

Gene expression databases

BgeeiQ5SW79.
CleanExiHS_CEP170.
ExpressionAtlasiQ5SW79. baseline and differential.
GenevisibleiQ5SW79. HS.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR026644. CEP170.
IPR029300. CEP170_C.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR15715:SF17. PTHR15715:SF17. 1 hit.
PfamiPF15308. CEP170_C. 1 hit.
PF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and initial characterization of KAB."
    Hara Y., Adachi Y.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT SER-213.
    Tissue: Brain and Cervix carcinoma.
  2. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
    Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
    DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT SER-213.
    Tissue: Brain.
  3. Ohara O.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "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].
  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 1-543 (ISOFORM 2), VARIANT SER-213.
    Tissue: Testis.
  6. "The forkhead-associated domain protein Cep170 interacts with Polo-like kinase 1 and serves as a marker for mature centrioles."
    Guarguaglini G., Duncan P.I., Stierhof Y.D., Holmstroem T., Duensing S., Nigg E.A.
    Mol. Biol. Cell 16:1095-1107(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLK1, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  7. "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-356; SER-359 AND SER-933, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633 AND SER-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-359; THR-501; SER-633; SER-636; SER-838; SER-930; SER-958; SER-1112; SER-1165 AND SER-1251, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1112 AND SER-1160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-356; SER-359; TYR-364; SER-1112 AND SER-1114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-359; SER-446 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Crystal structure of a centrosomal protein 170kDA, transcript variant beta (CEP170) from Homo sapiens at 2.15 A resolution (PSI community target, Sundstrom)."
    Joint center for structural genomics (JCSG)
    Submitted (APR-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-126.

Entry informationi

Entry nameiCE170_HUMAN
AccessioniPrimary (citable) accession number: Q5SW79
Secondary accession number(s): O75058
, Q5SW77, Q5SW78, Q7LGA9, Q86W31, Q9UQ08, Q9UQ09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 21, 2004
Last modified: July 22, 2015
This is version 103 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.