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Protein

Nck-associated protein 5-like

Gene

NCKAP5L

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

Functioni

Regulates microtubule organization and stabilization. Promotes microtubule growth and bundling formation and stabilizes microtubules by increasing intense acetylation of microtubules (PubMed:26482847, PubMed:26485573). Both tubulin-binding and homodimer formation are required for NCKAP5L-mediated microtubule bundle formation (PubMed:26485573).2 Publications

GO - Biological processi

  • microtubule bundle formation Source: UniProtKB
  • microtubule depolymerization Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Nck-associated protein 5-like
Short name:
NCKAP5-like
Alternative name(s):
Centrosomal protein of 169 kDa1 Publication
Short name:
Cep1691 Publication
Gene namesi
Name:NCKAP5L
Synonyms:CEP1691 Publication, KIAA1602
ORF Names:FP1193
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:29321. NCKAP5L.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • microtubule plus-end Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi482 – 4832IP → AA: No decrease in localization to microtubule plus ends. Loss of interaction with MAPRE1 and localization to microtubule plus ends; when associated with 814-A-A-815 and 924-A-A-925. 2 Publications
Mutagenesisi814 – 8152LP → AA: No decrease in localization to microtubule plus ends. Loss of interaction with MAPRE1 and localization to microtubule plus ends; when associated with 482-A-A-483 and 924-A-A-925. 2 Publications
Mutagenesisi924 – 9252LP → AA: Loss of interaction with MAPRE1 and significantly reduced localization to microtubule plus ends. Loss of interaction with MAPRE1 and localization to microtubule plus ends; when associated with 482-A-A-483 and 814-A-A-815. 2 Publications

Organism-specific databases

PharmGKBiPA165513124.

Polymorphism and mutation databases

BioMutaiNCKAP5L.
DMDMi156630840.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13301330Nck-associated protein 5-likePRO_0000288447Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei436 – 4361Phosphoserine; by CDK1Combined sources1 Publication
Modified residuei447 – 4471Phosphoserine; by CDK1Combined sources1 Publication
Modified residuei466 – 4661Phosphoserine; by CDK11 Publication
Modified residuei473 – 4731Phosphoserine; by CDK1Combined sources1 Publication
Modified residuei489 – 4891PhosphoserineCombined sources
Modified residuei492 – 4921PhosphoserineCombined sources
Modified residuei494 – 4941PhosphoserineCombined sources
Modified residuei567 – 5671Phosphoserine; by CDK1Combined sources1 Publication
Modified residuei573 – 5731Phosphoserine; by CDK11 Publication
Modified residuei655 – 6551PhosphothreonineCombined sources
Modified residuei763 – 7631Phosphoserine; by CDK1Combined sources1 Publication
Modified residuei1190 – 11901PhosphoserineCombined sources

Post-translational modificationi

CDK1/Cyclin B-dependent phosphorylation mediates its dissociation from centrosomes during mitosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9HCH0.
MaxQBiQ9HCH0.
PaxDbiQ9HCH0.
PeptideAtlasiQ9HCH0.
PRIDEiQ9HCH0.

PTM databases

iPTMnetiQ9HCH0.
PhosphoSiteiQ9HCH0.

Expressioni

Gene expression databases

BgeeiQ9HCH0.
CleanExiHS_KIAA1602.
ExpressionAtlasiQ9HCH0. baseline and differential.
GenevisibleiQ9HCH0. HS.

Organism-specific databases

HPAiHPA041034.

Interactioni

Subunit structurei

Homodimer (PubMed:26482847). Interacts with CDK5RAP2 (PubMed:26485573). Interacts with MAPRE1 (PubMed:26485573). Interacts with beta-tubulin (PubMed:26482847).2 Publications

Protein-protein interaction databases

BioGridi121726. 24 interactions.
IntActiQ9HCH0. 21 interactions.
STRINGi9606.ENSP00000337998.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 135135Mediates interaction with CDK5RAP2 and is required for homodimerization and microtubule bundle formation2 PublicationsAdd
BLAST
Regioni746 – 1142397Mediates interaction with beta-tubulin and is required for microtubule bundle formation1 PublicationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili24 – 10279Sequence analysisAdd
BLAST
Coiled coili952 – 99039Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi480 – 4834(S/T)X(I/L)P motif 12 Publications
Motifi812 – 8154(S/T)X(I/L)P motif 22 Publications
Motifi922 – 9254(S/T)X(I/L)P motif 3; required for interaction with MAPRE12 Publications

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi112 – 614503Pro-richAdd
BLAST
Compositional biasi784 – 87592Pro-richAdd
BLAST
Compositional biasi1042 – 1283242Pro-richAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IHBY. Eukaryota.
ENOG410XSUM. LUCA.
HOGENOMiHOG000113170.
HOVERGENiHBG080689.
InParanoidiQ9HCH0.
PhylomeDBiQ9HCH0.
TreeFamiTF331208.

Family and domain databases

InterProiIPR032769. NCKAP5_C.
IPR026163. Nckap5l.
[Graphical view]
PANTHERiPTHR21740. PTHR21740. 1 hit.
PfamiPF15246. NCKAP5. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HCH0-1) [UniParc]FASTAAdd to basket

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
MDQPAGGPGN PRPGEGDDGS MEPGTCQELL HRLRELEAEN SALAQANENQ
60 70 80 90 100
RETYERCLDE VANHVVQALL NQKDLREECI KLKKRVFDLE RQNQMLSALF
110 120 130 140 150
QQKLQLTTGS LPQIPLTPLQ PPSEPPASPS LSSTEGPAAP LPLGHCAGQR
160 170 180 190 200
EVCWEQQLRP GGPGPPAAPP PALDALSPFL RKKAQILEVL RALEETDPLL
210 220 230 240 250
LCSPATPWRP PGQGPGSPEP INGELCGPPQ PEPSPWAPCL LLGPGNLGGL
260 270 280 290 300
LHWERLLGGL GGEEDTGRPW GPSRGPPQAQ GTSSGPNCAP GSSSSSSSDE
310 320 330 340 350
AGDPNEAPSP DTLLGALARR QLNLGQLLED TESYLQAFLA GAAGPLNGDH
360 370 380 390 400
PGPGQSSSPD QAPPQLSKSK GLPKSAWGGG TPEAHRPGFG ATSEGQGPLP
410 420 430 440 450
FLSMFMGAGD APLGSRPGHP HSSSQVKSKL QIGPPSPGEA QGPLLPSPAR
460 470 480 490 500
GLKFLKLPPT SEKSPSPGGP QLSPQLPRNS RIPCRNSGSD GSPSPLLARR
510 520 530 540 550
GLGGGELSPE GAQGLPTSPS PCYTTPDSTQ LRPPQSALST TLSPGPVVSP
560 570 580 590 600
CYENILDLSR STFRGPSPEP PPSPLQVPTY PQLTLEVPQA PEVLRSPGVP
610 620 630 640 650
PSPCLPESYP YGSPQEKSLD KAGSESPHPG RRTPGNSSKK PSQGSGRRPG
660 670 680 690 700
DPGSTPLRDR LAALGKLKTG PEGALGSEKN GVPARPGTEK TRGPGKSGES
710 720 730 740 750
AGDMVPSIHR PLEQLEAKGG IRGAVALGTN SLKQQEPGLM GDPGARVYSS
760 770 780 790 800
HSMGARVDLE PVSPRSCLTK VELAKSRLAG ALCPQVPRTP AKVPTSAPSL
810 820 830 840 850
GKPNKSPHSS PTKLPSKSPT KVVPRPGAPL VTKESPKPDK GKGPPWADCG
860 870 880 890 900
STTAQSTPLV PGPTDPSQGP EGLAPHSAIE EKVMKGIEEN VLRLQGQERA
910 920 930 940 950
PGAEVKHRNT SSIASWFGLK KSKLPALNRR TEATKNKEGA GGGSPLRREV
960 970 980 990 1000
KMEARKLEAE SLNISKLMAK AEDLRRALEE EKAYLSSRAR PRPGGPAPGP
1010 1020 1030 1040 1050
NTGLGQVQGQ LAGMYQGADT FMQQLLNRVD GKELPSKSWR EPKPEYGDFQ
1060 1070 1080 1090 1100
PVSSDPKSPW PACGPRNGLV GPLQGCGKPP GKPSSEPGRR EETPSEDSLA
1110 1120 1130 1140 1150
EPVPTSHFTA CGSLTRTLDS GIGTFPPPDH GSSGTPSKNL PKTKPPRLDP
1160 1170 1180 1190 1200
PPGVPPARPP PLTKVPRRAH TLEREVPGIE ELLVSGRHPS MPAFPALLPA
1210 1220 1230 1240 1250
APGHRGHETC PDDPCEDPGP TPPVQLAKNW TFPNTRAAGS SSDPLMCPPR
1260 1270 1280 1290 1300
QLEGLPRTPM ALPVDRKRSQ EPSRPSPTPQ GPPFGGSRTP STSDMAEEGR
1310 1320 1330
VASGGPPGLE TSESLSDSLY DSLSSCGSQG
Length:1,330
Mass (Da):139,013
Last modified:May 29, 2007 - v2
Checksum:iF1BF45DF48445342
GO
Isoform 2 (identifier: Q9HCH0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1261-1330: ALPVDRKRSQ...DSLSSCGSQG → VRIAAEERERTREQEGVMWGDQFLQ

Note: No experimental confirmation available.
Show »
Length:1,285
Mass (Da):134,913
Checksum:i9BD104E362412201
GO
Isoform 4 (identifier: Q9HCH0-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     62-108: ANHVVQALLN...LFQQKLQLTT → CGSVVGLGGC...GTGVAEPEGE
     109-1330: Missing.

Note: No experimental confirmation available.
Show »
Length:108
Mass (Da):11,186
Checksum:i4C26FEC3CB3F5D90
GO
Isoform 3 (identifier: Q9HCH0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     771-792: Missing.

Note: No experimental confirmation available.
Show »
Length:1,308
Mass (Da):136,726
Checksum:i14CCB310858BB187
GO

Sequence cautioni

The sequence AAQ15202.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1093 – 10931T → M in AAH07998 (PubMed:15489334).Curated
Sequence conflicti1093 – 10931T → M in AAH33253 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei62 – 10847ANHVV…LQLTT → CGSVVGLGGCGSSAPGRSWG QLMALPRGFLSPGCQPCGTG VAEPEGE in isoform 4. 1 PublicationVSP_033818Add
BLAST
Alternative sequencei109 – 13301222Missing in isoform 4. 1 PublicationVSP_033819Add
BLAST
Alternative sequencei771 – 79222Missing in isoform 3. 1 PublicationVSP_025677Add
BLAST
Alternative sequencei1261 – 133070ALPVD…CGSQG → VRIAAEERERTREQEGVMWG DQFLQ in isoform 2. 1 PublicationVSP_025678Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC131157 Genomic DNA. No translation available.
BC007998 mRNA. Translation: AAH07998.1.
BC033253 mRNA. Translation: AAH33253.1.
BC110599 mRNA. Translation: AAI10600.1.
AB046822 mRNA. Translation: BAB13428.1.
AF370366 mRNA. Translation: AAQ15202.1. Frameshift.
RefSeqiNP_001032895.2. NM_001037806.3.
UniGeneiHs.143067.

Genome annotation databases

EnsembliENST00000335999; ENSP00000337998; ENSG00000167566.
GeneIDi57701.
KEGGihsa:57701.
UCSCiuc009zlk.2. human. [Q9HCH0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC131157 Genomic DNA. No translation available.
BC007998 mRNA. Translation: AAH07998.1.
BC033253 mRNA. Translation: AAH33253.1.
BC110599 mRNA. Translation: AAI10600.1.
AB046822 mRNA. Translation: BAB13428.1.
AF370366 mRNA. Translation: AAQ15202.1. Frameshift.
RefSeqiNP_001032895.2. NM_001037806.3.
UniGeneiHs.143067.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121726. 24 interactions.
IntActiQ9HCH0. 21 interactions.
STRINGi9606.ENSP00000337998.

PTM databases

iPTMnetiQ9HCH0.
PhosphoSiteiQ9HCH0.

Polymorphism and mutation databases

BioMutaiNCKAP5L.
DMDMi156630840.

Proteomic databases

EPDiQ9HCH0.
MaxQBiQ9HCH0.
PaxDbiQ9HCH0.
PeptideAtlasiQ9HCH0.
PRIDEiQ9HCH0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335999; ENSP00000337998; ENSG00000167566.
GeneIDi57701.
KEGGihsa:57701.
UCSCiuc009zlk.2. human. [Q9HCH0-1]

Organism-specific databases

CTDi57701.
GeneCardsiNCKAP5L.
H-InvDBHIX0010612.
HGNCiHGNC:29321. NCKAP5L.
HPAiHPA041034.
MIMi615104. gene.
neXtProtiNX_Q9HCH0.
PharmGKBiPA165513124.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHBY. Eukaryota.
ENOG410XSUM. LUCA.
HOGENOMiHOG000113170.
HOVERGENiHBG080689.
InParanoidiQ9HCH0.
PhylomeDBiQ9HCH0.
TreeFamiTF331208.

Miscellaneous databases

ChiTaRSiNCKAP5L. human.
GenomeRNAii57701.
PROiQ9HCH0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HCH0.
CleanExiHS_KIAA1602.
ExpressionAtlasiQ9HCH0. baseline and differential.
GenevisibleiQ9HCH0. HS.

Family and domain databases

InterProiIPR032769. NCKAP5_C.
IPR026163. Nckap5l.
[Graphical view]
PANTHERiPTHR21740. PTHR21740. 1 hit.
PfamiPF15246. NCKAP5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-1330 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-1330 (ISOFORM 3).
    Tissue: Eye and Skin.
  3. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 283-1330 (ISOFORM 2).
    Tissue: Brain.
  4. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 827-1330 (ISOFORM 1).
  5. "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-436 AND SER-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473; SER-492; SER-494 AND SER-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "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-436; SER-447; SER-489; SER-492 AND SER-494, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; SER-447; SER-473; SER-489; SER-494; THR-655; SER-763 AND SER-1190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  10. "Phosphorylation of the centrosomal protein, Cep169, by Cdk1 promotes its dissociation from centrosomes in mitosis."
    Mori Y., Inoue Y., Taniyama Y., Tanaka S., Terada Y.
    Biochem. Biophys. Res. Commun. 468:642-646(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-436; SER-447; SER-466; SER-473; SER-567; SER-573 AND SER-763, SUBCELLULAR LOCATION.
  11. "Microtubule-bundling activity of the centrosomal protein, Cep169, and its binding to microtubules."
    Mori Y., Taniyama Y., Tanaka S., Fukuchi H., Terada Y.
    Biochem. Biophys. Res. Commun. 467:754-759(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH BETA-TUBULIN, MUTAGENESIS OF 482-ILE-PRO-483; 814-LEU-PRO-815 AND 924-PRO-LEU-925, DOMAIN (S/T)X(I/L)P MOTIF.
  12. "Cep169, a novel microtubule plus-end-tracking centrosomal protein, binds to CDK5RAP2 and regulates microtubule stability."
    Mori Y., Inoue Y., Tanaka S., Doda S., Yamanaka S., Fukuchi H., Terada Y.
    PLoS ONE 10:E0140968-E0140968(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDK5RAP2 AND MAPRE1, MUTAGENESIS OF 482-ILE-PRO-483; 814-LEU-PRO-815 AND 924-PRO-LEU-925, DOMAIN (S/T)X(I/L)P MOTIF.

Entry informationi

Entry nameiNCK5L_HUMAN
AccessioniPrimary (citable) accession number: Q9HCH0
Secondary accession number(s): Q2TB26
, Q71RH1, Q8N4W1, Q96HX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: July 6, 2016
This is version 97 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 one 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.