NCK5L_MOUSE
ID NCK5L_MOUSE Reviewed; 1323 AA.
AC Q6GQX2; Q8BX75; Q8R364;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Nck-associated protein 5-like;
DE AltName: Full=Centrosomal protein of 169 kDa {ECO:0000250|UniProtKB:Q9HCH0};
DE Short=Cep169 {ECO:0000250|UniProtKB:Q9HCH0};
GN Name=Nckap5l; Synonyms=Cep169 {ECO:0000250|UniProtKB:Q9HCH0};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 752-1323.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulates microtubule organization and stabilization.
CC Promotes microtubule growth and bundling formation and stabilizes
CC microtubules by increasing intense acetylation of microtubules. Both
CC tubulin-binding and homodimer formation are required for NCKAP5L-
CC mediated microtubule bundle formation. {ECO:0000250|UniProtKB:Q9HCH0}.
CC -!- SUBUNIT: Homodimer. Interacts with CDK5RAP2. Interacts with MAPRE1.
CC Interacts with beta-tubulin. {ECO:0000250|UniProtKB:Q9HCH0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q9HCH0}. Note=Localizes to
CC microtubule plus ends. Associates with centrosomes during interphase,
CC but dissociates from these structures from the onset of mitosis.
CC {ECO:0000250|UniProtKB:Q9HCH0}.
CC -!- PTM: CDK1/Cyclin B-dependent phosphorylation mediates its dissociation
CC from centrosomes during mitosis. {ECO:0000250|UniProtKB:Q9HCH0}.
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DR EMBL; BC026468; AAH26468.1; -; mRNA.
DR EMBL; BC072572; AAH72572.1; -; mRNA.
DR EMBL; AK048721; BAC33433.1; -; mRNA.
DR CCDS; CCDS27820.1; -.
DR RefSeq; NP_001001884.1; NM_001001884.1.
DR RefSeq; XP_006521186.1; XM_006521123.3.
DR AlphaFoldDB; Q6GQX2; -.
DR SMR; Q6GQX2; -.
DR BioGRID; 237726; 4.
DR STRING; 10090.ENSMUSP00000023747; -.
DR iPTMnet; Q6GQX2; -.
DR PhosphoSitePlus; Q6GQX2; -.
DR EPD; Q6GQX2; -.
DR jPOST; Q6GQX2; -.
DR MaxQB; Q6GQX2; -.
DR PaxDb; Q6GQX2; -.
DR PeptideAtlas; Q6GQX2; -.
DR PRIDE; Q6GQX2; -.
DR ProteomicsDB; 293531; -.
DR Antibodypedia; 49270; 23 antibodies from 13 providers.
DR Ensembl; ENSMUST00000023747; ENSMUSP00000023747; ENSMUSG00000023009.
DR GeneID; 380969; -.
DR KEGG; mmu:380969; -.
DR UCSC; uc007xpn.1; mouse.
DR CTD; 57701; -.
DR MGI; MGI:3609653; Nckap5l.
DR VEuPathDB; HostDB:ENSMUSG00000023009; -.
DR eggNOG; ENOG502RB0P; Eukaryota.
DR GeneTree; ENSGT00530000063607; -.
DR HOGENOM; CLU_007601_0_0_1; -.
DR InParanoid; Q6GQX2; -.
DR OMA; EGTGRPW; -.
DR OrthoDB; 29694at2759; -.
DR PhylomeDB; Q6GQX2; -.
DR TreeFam; TF331208; -.
DR BioGRID-ORCS; 380969; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Nckap5l; mouse.
DR PRO; PR:Q6GQX2; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6GQX2; protein.
DR Bgee; ENSMUSG00000023009; Expressed in embryonic post-anal tail and 104 other tissues.
DR ExpressionAtlas; Q6GQX2; baseline and differential.
DR Genevisible; Q6GQX2; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; ISS:UniProtKB.
DR InterPro; IPR032769; NCKAP5_C.
DR InterPro; IPR026163; Nckap5l.
DR PANTHER; PTHR21740; PTHR21740; 1.
DR Pfam; PF15246; NCKAP5; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1323
FT /note="Nck-associated protein 5-like"
FT /id="PRO_0000288448"
FT REGION 1..135
FT /note="Mediates interaction with CDK5RAP2 and is required
FT for homodimerization and microtubule bundle formation"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..1136
FT /note="Mediates interaction with beta-tubulin and is
FT required for microtubule bundle formation"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT REGION 778..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..109
FT /evidence="ECO:0000255"
FT COILED 942..985
FT /evidence="ECO:0000255"
FT MOTIF 480..483
FT /note="(S/T)X(I/L)P motif 1"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOTIF 808..811
FT /note="(S/T)X(I/L)P motif 2"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOTIF 918..921
FT /note="(S/T)X(I/L)P motif 3; required for interaction with
FT MAPRE1"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT COMPBIAS 221..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 436
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOD_RES 447
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOD_RES 466
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOD_RES 473
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOD_RES 573
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOD_RES 654
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOD_RES 760
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT MOD_RES 1184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCH0"
FT CONFLICT 752
FT /note="A -> S (in Ref. 2; BAC33433)"
FT /evidence="ECO:0000305"
FT CONFLICT 1100
FT /note="T -> A (in Ref. 1; AAH26468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1323 AA; 138170 MW; 944DCC62EB77EEF7 CRC64;
MDQPAGGTGK LRASAGEDDS MELSTCQELL HRLRELEAEN SALAQANENQ RETYERCLDE
VANHVVQALL NQKDLREECI KLKKRVFDLE RQNQVLSALL QQKLQLTANS LPQIPLTPLQ
PPSERPTSPA PNVSEGPATS LPSGLCAGQR EVCWEQQLRP GGPGPPATPP PALDALSPFL
RKKAQILEVL RALEETDPLL LCSPATPWRP TGQGPGSPEP INGEPCGPPQ PEPSPWAPYL
LLGPGSLGAL LHWERVLGGP GEEEGIRQPW ASSRAPPSAQ GPSSGPHCAP GSSSSSSSDE
AGDPNEAPSP DTLLGALARK QLNLGQLLGD TETYLQAFLA GATGPLSGDQ PGPGKPNSPD
PGPPQVSKSK GLPKSAWGAS TPEATRLGFG ATSEGQGPLP FLSMFMGAGD APLGSRPGHP
HSSSQVKSKL QIGPPSPGDA QGPLLPSPAR GLKFLKLPPA SEKVPSPGGP QLSPQLPRSS
RIPCRNSGSD GSPSPLLARR GLGGGELSPE GAQGLPGSPL PCSAMPDSAQ LRPSQSTVST
ALSPGPVVSP CFENILDLSR STFRGSPPEP PPSPLQVPTY PQLTLEVPQT PEVLRSPGAP
SPGLPESCPY SGPQEKSMDR AGSESPHASR RTPGGSSKKP GQGSGRRPGD PSHTPLRDRL
AALGKLKTGP EGPLGPEKNG VPARSSAEKA RALVRSGECA GDVPPSARPL EQPEAKGIFR
GAVALGTSSL KQQEPGLTDP GARVYSSHSM GARVDLEPIS PRSCLTKVEL AKSRLAGALC
PQMPRTPAKV PTSAPSLGKP KSPHSSPTKL PSKSPTKVVP RPVVPLGTKE PPKPDKVKGP
PWADCGSTVG QPTSPVAGPA DPSQGSEGPA PHSAIEEKVM KGIEENVLRL QGQERTPGSE
AKHRNTSSIA SWFGLKKSKL PALNRRTEAT KNKDGAGGGS PLRKEVKTEA RKLEAESLNI
SKLMAKAEDL RRALEEEKAY LSRARPRPGG PATVPSPGLG QAQGQLAGMY QGADTFMQQL
LNRVDGKELP PKSWREPKPE YGDFQPVSTD PKSPWPACGP RNGLVGPLQG CGKPGKPSSE
PGRREEMPSE DSLAEPVSTT HFTACGSLTR TLDSGIGTFP PPDHSSSGTP SKNLPKTKSL
RLDPPPGAPP ARPPGLTKVP RRAHTLEREV PGIEELLVSG RHPSMPAFPG LLTAPPGHRS
HQTCPDDPCE DPGPPPPVQL AKNWTFPNTR TAGSSSDPFL CPPRQLEGLP RTPMALPVDR
KQSVDPSRTS TPQGPAFGGS RTPSTSDMGE EGRVASGGAP GLETSESLSD SLYDSLSSCG
SQG
