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Q5SW79 (CE170_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centrosomal protein of 170 kDa
Short name=Cep170
Alternative name(s):
KARP-1-binding protein
Short name=KARP1-binding protein
Gene names
Name:CEP170
Synonyms:FAM68A, KAB, KIAA0470
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length1584 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in microtubule organization. Ref.6

Subunit structure

Interacts with PLK1. Ref.6

Subcellular location

Cytoplasm › cytoskeleton › centrosome › centriole. Cytoplasm › cytoskeleton › spindle. Note: Associated with the mature mother centriole. Associated with spindle microtubules during mitosis. Ref.6

Post-translational modification

Phosphorylated; probably by PLK1. Ref.6

Sequence similarities

Belongs to the CEP170 family.

Contains 1 FHA domain.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcentriole

Inferred from electronic annotation. Source: UniProtKB-SubCell

centrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

vprP125204EBI-1104799,EBI-6164519From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5SW79-1)

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.
Isoform 2 (identifier: Q5SW79-2)

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
Isoform 3 (identifier: Q5SW79-3)

Also known as: Beta; KAB2;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15841584Centrosomal protein of 170 kDa
PRO_0000282887

Regions

Domain23 – 7351FHA
Region853 – 1584732Targeting to microtubules
Region1113 – 1584472Targeting to centrosomes
Coiled coil1467 – 149529 Potential

Amino acid modifications

Modified residue3561Phosphoserine Ref.7 Ref.10 Ref.13 Ref.15
Modified residue3591Phosphoserine Ref.7 Ref.10 Ref.13 Ref.15
Modified residue3641Phosphotyrosine Ref.13
Modified residue4461Phosphoserine Ref.15
Modified residue4971Phosphoserine Ref.15
Modified residue5011Phosphothreonine Ref.10
Modified residue6331Phosphoserine Ref.9 Ref.10
Modified residue6361Phosphoserine Ref.8 Ref.9 Ref.10
Modified residue8381Phosphoserine Ref.10 Ref.15
Modified residue9301Phosphoserine Ref.10
Modified residue9331Phosphoserine Ref.7
Modified residue9581Phosphoserine Ref.10
Modified residue11121Phosphoserine Ref.10 Ref.12 Ref.13
Modified residue11141Phosphoserine Ref.13
Modified residue11601Phosphoserine Ref.12
Modified residue11651Phosphoserine Ref.10
Modified residue11981Phosphoserine By similarity
Modified residue12511Phosphoserine Ref.10

Natural variations

Alternative sequence425 – 52298Missing in isoform 2 and isoform 3.
VSP_024240
Alternative sequence1226 – 126136Missing in isoform 2.
VSP_024241
Alternative sequence13531E → EVGDLHGEMHK in isoform 2.
VSP_024242
Natural variant2131G → S. Ref.1 Ref.2 Ref.5
Corresponds to variant rs2631092 [ dbSNP | Ensembl ].
VAR_031437

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 50E981650D21B2E6

FASTA1,584175,293
        10         20         30         40         50         60 
MSLTSWFLVS SGGTRHRLPR EMIFVGRDDC ELMLQSRSVD KQHAVINYDA STDEHLVKDL 

        70         80         90        100        110        120 
GSLNGTFVND VRIPEQTYIT LKLEDKLRFG YDTNLFTVVQ GEMRVPEEAL KHEKFTIQLQ 

       130        140        150        160        170        180 
LSQKSSESEL SKSASAKSID SKVADAATEV QHKTTEALKS EEKAMDISAM PRGTPLYGQP 

       190        200        210        220        230        240 
SWWGDDEVDE KRAFKTNGKP EEKNHEAGTS GCGIDAKQVE EQSAAANEEV LFPFCREPSY 

       250        260        270        280        290        300 
FEIPTKEFQQ PSQITESTIH EIPTKDTPSS HITGAGHASF TIEFDDSTPG KVTIRDHVTK 

       310        320        330        340        350        360 
FTSDQRHKSK KSSPGTQDLL GIQTGMMAPE NKVADWLAQN NPPQMLWERT EEDSKSIKSD 

       370        380        390        400        410        420 
VPVYLKRLKG NKHDDGTQSD SENAGAHRRC SKRATLEEHL RRHHSEHKKL QKVQATEKHQ 

       430        440        450        460        470        480 
DQAVTSSAHH RGGHGVPHGK LLKQKSEEPS VSIPFLQTAL LRSSGSLGHR PSQEMDKMLK 

       490        500        510        520        530        540 
NQATSATSEK DNDDDQSDKG TYTIELENPN SEEVEARKMI DKVFGVDDNQ DYNRPVINEK 

       550        560        570        580        590        600 
HKDLIKDWAL SSAAAVMEER KPLTTSGFHH SEEGTSSSGS KRWVSQWASL AANHTRHDQE 

       610        620        630        640        650        660 
ERIMEFSAPL PLENETEISE SGMTVRSTGS ATSLASQGER RRRTLPQLPN EEKSLESHRA 

       670        680        690        700        710        720 
KVVTQRSEIG EKQDTELQEK ETPTQVYQKD KQDADRPLSK MNRAVNGETL KTGGDNKTLL 

       730        740        750        760        770        780 
HLGSSAPGKE KSETDKETSL VKQTLAKLQQ QEQREEAQWT PTKLSSKNVS GQTDKCREET 

       790        800        810        820        830        840 
FKQESQPPEK NSGHSTSKGD RVAQSESKRR KAEEILKSQT PKGGDKKESS KSLVRQGSFT 

       850        860        870        880        890        900 
IEKPSPNIPI ELIPHINKQT SSTPSSLALT SASRIRERSE SLDPDSSMDT TLILKDTEAV 

       910        920        930        940        950        960 
MAFLEAKLRE DNKTDEGPDT PSYNRDNSIS PESDVDTAST ISLVTGETER KSTQKRKSFT 

       970        980        990       1000       1010       1020 
SLYKDRCSTG SPSKDVTKSS SSGAREKMEK KTKSRSTDVG SRADGRKFVQ SSGRIRQPSV 

      1030       1040       1050       1060       1070       1080 
DLTDDDQTSS VPHSAISDIM SSDQETYSCK PHGRTPLTSA DEHVHSKLEG SKVTKSKTSP 

      1090       1100       1110       1120       1130       1140 
VVSGSSSKST TLPRPRPTRT SLLRRARLGE ASDSELADAD KASVASEVST TSSTSKPPTG 

      1150       1160       1170       1180       1190       1200 
RRNISRIDLL AQPRRTRLGS LSARSDSEAT ISRSSASSRT AEAIIRSGAR LVPSDKFSPR 

      1210       1220       1230       1240       1250       1260 
IRANSISRLS DSKVKSMTSA HGSASVNSRW RRFPTDYAST SEDEFGSNRN SPKHTRLRTS 

      1270       1280       1290       1300       1310       1320 
PALKTTRLQS AGSAMPTSSS FKHRIKEQED YIRDWTAHRE EIARISQDLA LIAREINDVA 

      1330       1340       1350       1360       1370       1380 
GEIDSVTSSG TAPSTTVSTA ATTPGSAIDT REELVDRVFD ESLNFRKIPP LVHSKTPEGN 

      1390       1400       1410       1420       1430       1440 
NGRSGDPRPQ AAEPPDHLTI TRRRTWSRDE VMGDNLLLSS VFQFSKKIRQ SIDKTAGKIR 

      1450       1460       1470       1480       1490       1500 
ILFKDKDRNW DDIESKLRAE SEVPIVKTSS MEISSILQEL KRVEKQLQAI NAMIDPDGTL 

      1510       1520       1530       1540       1550       1560 
EALNNMGFPS AMLPSPPKQK SSPVNNHHSP GQTPTLGQPE ARALHPAAVS AAAEFENAES 

      1570       1580 
EADFSIHFNR FNPDGEEEDV TVQE

« Hide

Isoform 2 (Gamma) (3) [UniParc].

Checksum: 4EEECA047C7B0EFA
Show »

FASTA1,460161,408
Isoform 3 (Beta) (KAB2) [UniParc].

Checksum: 376DEE4949EC24D1
Show »

FASTA1,486164,539

References

« Hide 'large scale' references
[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. expand/collapse author list , 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, MASS SPECTROMETRY.
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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633 AND SER-636, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[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-356; SER-359; TYR-364; SER-1112 AND SER-1114, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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; SER-497 AND SER-838, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00186194.
IPI00477477.
IPI00871460.
PIRT00095.
RefSeqNP_001035863.1. NM_001042404.1.
NP_001035864.1. NM_001042405.1.
NP_055627.2. NM_014812.2.
UniGeneHs.533635.

3D structure databases

ProteinModelPortalQ5SW79.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-37594N.
IntActQ5SW79. 12 interactions.
MINTMINT-1790395.
STRING9606.ENSP00000415575.

PTM databases

PhosphoSiteQ5SW79.

Polymorphism databases

DMDM74743919.

Proteomic databases

PaxDbQ5SW79.
PRIDEQ5SW79.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366542; ENSP00000355500; ENSG00000143702.
ENST00000366543; ENSP00000355501; ENSG00000143702.
ENST00000366544; ENSP00000355502; ENSG00000143702.
GeneID9859.
KEGGhsa:9859.
UCSCuc021plo.1. human.
uc021plp.1. human.
uc021plq.1. human.

Organism-specific databases

CTD9859.
GeneCardsGC01M243287.
H-InvDBHIX0004456.
HGNCHGNC:28920. CEP170.
MIM613023. gene.
neXtProtNX_Q5SW79.
PharmGKBPA128395757.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG18196.
HOVERGENHBG058059.
KOK16463.
OMARHHSEQK.
OrthoDBEOG4BCDMF.

Gene expression databases

ArrayExpressQ5SW79.
BgeeQ5SW79.
CleanExHS_CEP170.
GenevestigatorQ5SW79.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
InterProIPR026644. CEP170.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERPTHR15715:SF2. PTHR15715:SF2. 1 hit.
PfamPF00498. FHA. 1 hit.
[Graphical view]
SMARTSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMSSF49879. SMAD_FHA. 1 hit.
PROSITEPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi9859.
NextBio37158.
PMAP-CutDBQ5SW79.
SOURCESearch...

Entry information

Entry nameCE170_HUMAN
AccessionPrimary (citable) accession number: Q5SW79
Secondary accession number(s): O75058 expand/collapse secondary AC list , Q5SW77, Q5SW78, Q7LGA9, Q86W31, Q9UQ08, Q9UQ09
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 21, 2004
Last modified: May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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