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Q5SW79

- CE170_HUMAN

UniProt

Q5SW79 - CE170_HUMAN

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Protein
Centrosomal protein of 170 kDa
Gene
CEP170, FAM68A, KAB, KIAA0470
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a role in microtubule organization.1 Publication

GO - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

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: Chromosome 1

Organism-specific databases

HGNCiHGNC:28920. CEP170.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Cytoplasmcytoskeletonspindle
Note: Associated with the mature mother centriole. Associated with spindle microtubules during mitosis.1 Publication

GO - Cellular componenti

  1. centriole Source: MGI
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: HPA
  4. microtubule Source: UniProtKB-KW
  5. nuclear membrane Source: HPA
  6. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128395757.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15841584Centrosomal protein of 170 kDa
PRO_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 – 8381Phosphoserine2 Publications
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

ArrayExpressiQ5SW79.
BgeeiQ5SW79.
CleanExiHS_CEP170.
GenevestigatoriQ5SW79.

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. 19 interactions.
DIPiDIP-37594N.
IntActiQ5SW79. 15 interactions.
MINTiMINT-1790395.
STRINGi9606.ENSP00000415575.

Structurei

Secondary structure

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

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 7351FHA
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni853 – 1584732Targeting to microtubules
Add
BLAST
Regioni1113 – 1584472Targeting to centrosomes
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1467 – 149529 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Belongs to the CEP170 family.
Contains 1 FHA domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG18196.
HOVERGENiHBG058059.
KOiK16463.
OMAiQSSGRMR.
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. Align

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

MSLTSWFLVS SGGTRHRLPR EMIFVGRDDC ELMLQSRSVD KQHAVINYDA     50
STDEHLVKDL GSLNGTFVND VRIPEQTYIT LKLEDKLRFG YDTNLFTVVQ 100
GEMRVPEEAL KHEKFTIQLQ LSQKSSESEL SKSASAKSID SKVADAATEV 150
QHKTTEALKS EEKAMDISAM PRGTPLYGQP SWWGDDEVDE KRAFKTNGKP 200
EEKNHEAGTS GCGIDAKQVE EQSAAANEEV LFPFCREPSY FEIPTKEFQQ 250
PSQITESTIH EIPTKDTPSS HITGAGHASF TIEFDDSTPG KVTIRDHVTK 300
FTSDQRHKSK KSSPGTQDLL GIQTGMMAPE NKVADWLAQN NPPQMLWERT 350
EEDSKSIKSD VPVYLKRLKG NKHDDGTQSD SENAGAHRRC SKRATLEEHL 400
RRHHSEHKKL QKVQATEKHQ DQAVTSSAHH RGGHGVPHGK LLKQKSEEPS 450
VSIPFLQTAL LRSSGSLGHR PSQEMDKMLK NQATSATSEK DNDDDQSDKG 500
TYTIELENPN SEEVEARKMI DKVFGVDDNQ DYNRPVINEK HKDLIKDWAL 550
SSAAAVMEER KPLTTSGFHH SEEGTSSSGS KRWVSQWASL AANHTRHDQE 600
ERIMEFSAPL PLENETEISE SGMTVRSTGS ATSLASQGER RRRTLPQLPN 650
EEKSLESHRA KVVTQRSEIG EKQDTELQEK ETPTQVYQKD KQDADRPLSK 700
MNRAVNGETL KTGGDNKTLL HLGSSAPGKE KSETDKETSL VKQTLAKLQQ 750
QEQREEAQWT PTKLSSKNVS GQTDKCREET FKQESQPPEK NSGHSTSKGD 800
RVAQSESKRR KAEEILKSQT PKGGDKKESS KSLVRQGSFT IEKPSPNIPI 850
ELIPHINKQT SSTPSSLALT SASRIRERSE SLDPDSSMDT TLILKDTEAV 900
MAFLEAKLRE DNKTDEGPDT PSYNRDNSIS PESDVDTAST ISLVTGETER 950
KSTQKRKSFT SLYKDRCSTG SPSKDVTKSS SSGAREKMEK KTKSRSTDVG 1000
SRADGRKFVQ SSGRIRQPSV DLTDDDQTSS VPHSAISDIM SSDQETYSCK 1050
PHGRTPLTSA DEHVHSKLEG SKVTKSKTSP VVSGSSSKST TLPRPRPTRT 1100
SLLRRARLGE ASDSELADAD KASVASEVST TSSTSKPPTG RRNISRIDLL 1150
AQPRRTRLGS LSARSDSEAT ISRSSASSRT AEAIIRSGAR LVPSDKFSPR 1200
IRANSISRLS DSKVKSMTSA HGSASVNSRW RRFPTDYAST SEDEFGSNRN 1250
SPKHTRLRTS PALKTTRLQS AGSAMPTSSS FKHRIKEQED YIRDWTAHRE 1300
EIARISQDLA LIAREINDVA GEIDSVTSSG TAPSTTVSTA ATTPGSAIDT 1350
REELVDRVFD ESLNFRKIPP LVHSKTPEGN NGRSGDPRPQ AAEPPDHLTI 1400
TRRRTWSRDE VMGDNLLLSS VFQFSKKIRQ SIDKTAGKIR ILFKDKDRNW 1450
DDIESKLRAE SEVPIVKTSS MEISSILQEL KRVEKQLQAI NAMIDPDGTL 1500
EALNNMGFPS AMLPSPPKQK SSPVNNHHSP GQTPTLGQPE ARALHPAAVS 1550
AAAEFENAES EADFSIHFNR FNPDGEEEDV TVQE 1584
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.

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.
VSP_024240Add
BLAST
Alternative sequencei1226 – 126136Missing in isoform 2.
VSP_024241Add
BLAST
Alternative sequencei1353 – 13531E → EVGDLHGEMHK in isoform 2.
VSP_024242

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
XP_006711912.1. XM_006711849.1. [Q5SW79-1]
XP_006711914.1. XM_006711851.1. [Q5SW79-3]
XP_006711915.1. XM_006711852.1. [Q5SW79-2]
XP_006725044.1. XM_006724981.1. [Q5SW79-1]
XP_006725046.1. XM_006724983.1. [Q5SW79-3]
XP_006725047.1. XM_006724984.1. [Q5SW79-2]
UniGeneiHs.533635.

Genome annotation databases

EnsembliENST00000366542; ENSP00000355500; ENSG00000143702. [Q5SW79-1]
ENST00000366543; ENSP00000355501; ENSG00000143702. [Q5SW79-2]
ENST00000366544; ENSP00000355502; ENSG00000143702. [Q5SW79-3]
GeneIDi9859.
KEGGihsa:9859.
UCSCiuc021plo.1. human. [Q5SW79-1]
uc021plp.1. human. [Q5SW79-2]
uc021plq.1. human. [Q5SW79-3]

Polymorphism databases

DMDMi74743919.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS44337.1. [Q5SW79-3 ]
CCDS44338.1. [Q5SW79-2 ]
CCDS44339.1. [Q5SW79-1 ]
PIRi T00095.
RefSeqi NP_001035863.1. NM_001042404.1. [Q5SW79-3 ]
NP_001035864.1. NM_001042405.1. [Q5SW79-2 ]
NP_055627.2. NM_014812.2. [Q5SW79-1 ]
XP_006711912.1. XM_006711849.1. [Q5SW79-1 ]
XP_006711914.1. XM_006711851.1. [Q5SW79-3 ]
XP_006711915.1. XM_006711852.1. [Q5SW79-2 ]
XP_006725044.1. XM_006724981.1. [Q5SW79-1 ]
XP_006725046.1. XM_006724983.1. [Q5SW79-3 ]
XP_006725047.1. XM_006724984.1. [Q5SW79-2 ]
UniGenei Hs.533635.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4JON X-ray 2.15 A/B/C/D/E 1-126 [» ]
ProteinModelPortali Q5SW79.
SMRi Q5SW79. Positions 1-123.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115193. 19 interactions.
DIPi DIP-37594N.
IntActi Q5SW79. 15 interactions.
MINTi MINT-1790395.
STRINGi 9606.ENSP00000415575.

PTM databases

PhosphoSitei Q5SW79.

Polymorphism databases

DMDMi 74743919.

Proteomic databases

MaxQBi Q5SW79.
PaxDbi Q5SW79.
PRIDEi Q5SW79.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366542 ; ENSP00000355500 ; ENSG00000143702 . [Q5SW79-1 ]
ENST00000366543 ; ENSP00000355501 ; ENSG00000143702 . [Q5SW79-2 ]
ENST00000366544 ; ENSP00000355502 ; ENSG00000143702 . [Q5SW79-3 ]
GeneIDi 9859.
KEGGi hsa:9859.
UCSCi uc021plo.1. human. [Q5SW79-1 ]
uc021plp.1. human. [Q5SW79-2 ]
uc021plq.1. human. [Q5SW79-3 ]

Organism-specific databases

CTDi 9859.
GeneCardsi GC01M243287.
H-InvDB HIX0004456.
HGNCi HGNC:28920. CEP170.
HPAi HPA042151.
HPA045787.
MIMi 613023. gene.
neXtProti NX_Q5SW79.
PharmGKBi PA128395757.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG18196.
HOVERGENi HBG058059.
KOi K16463.
OMAi QSSGRMR.
OrthoDBi EOG741Z19.
PhylomeDBi Q5SW79.
TreeFami TF328469.

Miscellaneous databases

GeneWikii CEP170.
GenomeRNAii 9859.
NextBioi 37158.
PMAP-CutDB Q5SW79.
PROi Q5SW79.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q5SW79.
Bgeei Q5SW79.
CleanExi HS_CEP170.
Genevestigatori Q5SW79.

Family and domain databases

Gene3Di 2.60.200.20. 1 hit.
InterProi IPR026644. CEP170.
IPR029300. CEP170_C.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view ]
PANTHERi PTHR15715:SF17. PTHR15715:SF17. 1 hit.
Pfami PF15308. CEP170_C. 1 hit.
PF00498. FHA. 1 hit.
[Graphical view ]
SMARTi SM00240. FHA. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
PROSITEi PS50006. FHA_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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; SER-497 AND SER-838, 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: September 3, 2014
This is version 94 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

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