C170B_MOUSE
ID C170B_MOUSE Reviewed; 1574 AA.
AC Q80U49; Q3UH33; Q3UHG1; Q80UM2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Centrosomal protein of 170 kDa protein B;
DE AltName: Full=Centrosomal protein 170B;
DE Short=Cep170B;
GN Name=Cep170b; Synonyms=Kiaa0284;
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] (ISOFORM 1).
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trophoblast stem cell;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-709; SER-1122 AND
RP SER-1186, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-478; SER-534;
RP THR-541; SER-709; SER-947; SER-965; SER-981; SER-1122; SER-1166; THR-1289;
RP THR-1345 AND SER-1347, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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: Plays a role in microtubule organization.
CC {ECO:0000250|UniProtKB:Q5SW79}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q498L0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80U49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U49-2; Sequence=VSP_024249;
CC -!- SIMILARITY: Belongs to the CEP170 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65518.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122236; BAC65518.1; ALT_INIT; mRNA.
DR EMBL; AK147410; BAE27896.1; -; mRNA.
DR EMBL; AK147612; BAE28024.1; -; mRNA.
DR EMBL; BC050077; AAH50077.1; -; mRNA.
DR CCDS; CCDS56867.1; -. [Q80U49-1]
DR RefSeq; NP_001019773.2; NM_001024602.3. [Q80U49-1]
DR RefSeq; XP_006515829.1; XM_006515766.3. [Q80U49-1]
DR AlphaFoldDB; Q80U49; -.
DR SMR; Q80U49; -.
DR BioGRID; 229975; 18.
DR IntAct; Q80U49; 6.
DR MINT; Q80U49; -.
DR STRING; 10090.ENSMUSP00000098580; -.
DR iPTMnet; Q80U49; -.
DR PhosphoSitePlus; Q80U49; -.
DR EPD; Q80U49; -.
DR MaxQB; Q80U49; -.
DR PaxDb; Q80U49; -.
DR PeptideAtlas; Q80U49; -.
DR PRIDE; Q80U49; -.
DR ProteomicsDB; 273719; -. [Q80U49-1]
DR ProteomicsDB; 273720; -. [Q80U49-2]
DR Antibodypedia; 54848; 41 antibodies from 13 providers.
DR DNASU; 217882; -.
DR Ensembl; ENSMUST00000092279; ENSMUSP00000089930; ENSMUSG00000072825. [Q80U49-2]
DR Ensembl; ENSMUST00000101018; ENSMUSP00000098580; ENSMUSG00000072825. [Q80U49-1]
DR Ensembl; ENSMUST00000179041; ENSMUSP00000137331; ENSMUSG00000072825. [Q80U49-1]
DR Ensembl; ENSMUST00000222711; ENSMUSP00000152451; ENSMUSG00000072825. [Q80U49-1]
DR GeneID; 217882; -.
DR KEGG; mmu:217882; -.
DR UCSC; uc007pfb.1; mouse. [Q80U49-1]
DR CTD; 283638; -.
DR MGI; MGI:2145043; Cep170b.
DR VEuPathDB; HostDB:ENSMUSG00000072825; -.
DR eggNOG; ENOG502QSH8; Eukaryota.
DR GeneTree; ENSGT00940000157058; -.
DR HOGENOM; CLU_003940_1_0_1; -.
DR InParanoid; Q80U49; -.
DR OMA; LKHHHED; -.
DR OrthoDB; 83451at2759; -.
DR PhylomeDB; Q80U49; -.
DR TreeFam; TF328469; -.
DR BioGRID-ORCS; 217882; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cep170b; mouse.
DR PRO; PR:Q80U49; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q80U49; protein.
DR Bgee; ENSMUSG00000072825; Expressed in primary visual cortex and 83 other tissues.
DR ExpressionAtlas; Q80U49; baseline and differential.
DR Genevisible; Q80U49; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR029300; CEP170_C.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF15308; CEP170_C; 1.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1574
FT /note="Centrosomal protein of 170 kDa protein B"
FT /id="PRO_0000282890"
FT DOMAIN 23..73
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 121..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1333..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..549
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..989
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 540
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 541
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 1289
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 1345
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT MOD_RES 1533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F5"
FT VAR_SEQ 259..1174
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024249"
FT CONFLICT 54
FT /note="E -> V (in Ref. 2; BAE28024)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="P -> L (in Ref. 3; AAH50077)"
FT /evidence="ECO:0000305"
FT CONFLICT 1365
FT /note="E -> G (in Ref. 2; BAE27896)"
FT /evidence="ECO:0000305"
FT CONFLICT 1428
FT /note="L -> P (in Ref. 3; AAH50077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1574 AA; 170821 MW; 9CB9DB93413B3B1F CRC64;
MSVTSWFLVS SSGTRHRLPR ELIFVGRDEC ELMLQSRSVD KQHAVINYDQ DRDEHWVKDL
GSLNGTFVND VRIPDQKYIT LKLNDVIRFG YDSNMYVLER VQHRVPEEAL KHEKYTSQLQ
VSVKVSAPKR GDALPDHTPY CESSQPRPEK GDRRHGAEAV AYRTPLYGQP SWWGEDDSGA
PSEDRHQEEP YSERPKDLAQ QNGELDSCRA PAEPPDYSFR REPSYFEIPT KETPQPPRLP
EVPTQEVPTK DQEAGVGGTA PVVQSHASFT IEFDDCSPGK VKIKDHITKF SLRQRRAPSK
ETTPVETVSA ETKVADWLVQ NDPSLLRRDG PGDDRHSTKS DLPVHTRTLK GHKHEDGTQS
DSEDPLAKTA SVSGASAEAS GEQVRLQRQI KRDPQELLHN QQAFVIEFFD GDTPRKKRSQ
SFTHTPPADP KADKRRGPGT SDRDRPGVSV RATGSSSGPQ RASSLKREKT EERLGNTSPV
PRASTRSFGS VGRRSRLAQD FMAQCMRDSS PATRPAPEKT PPVLPAPLTP RGASPVTPST
TPPPPTDPQL TKARKQEEDD SLSDAGTYTI ETEAQDQEVE EARRMIDQVF GVFESPELSR
VSSATFRPVI RGDKDESSDG GMAQRMALLQ EFASRAPGMA PQMEQQSLLV PGSPGGQKWV
SRWASLADSY SDAGLPEDGP GRRTGEPEGP LPVRTRRLLP QLPSGRADSP AGLEAARRNG
PGPPELGSEP ANCLIGQEDL DPDSLSDASG SDGGRGPEPG TERQEDLAWV RGRRSPRAPG
ELVPTSFFIG DQNGEATFPK KSFVGPGEVD GPGRVVQTSP SARDGLYVSS NGRMVIQLRS
GRSPEPDPAP PKETLTFARQ ESFTKEPTSG PPAPGKLPHI SSHPLLQDLA AARASRLDFH
AQDTHLILKE TETALAALEA RLRSKSADEC DGGSTPRPPE DSLSGDSDVD TASTISLLSG
KNGPSPTTPQ TPGPQKESPL SPPTVPDPGG ATPGSARERM SERQHRPTPA DLGPGDTSRR
AAMRRGHGSR GSLDWPEEER GSGLAHLPSS NHETPEATLA GRQGPRRKPA APPPSPAARE
EQSRSSATAQ KVQQALTRSN SLSTPRPTRA SRLRRARLGD ASDTEAVDGE RGTAANPEPA
NRAAPEQAKK LTRLDILAMP RKRAGSFTGP SDSETAPART GFSGRSAELY STSRKPTIAE
ARAAAKKAAA TAANTGPRQP FSRARPGSAR YSSNTRRRQQ GSDYTSTSEE EYGSHHSSPK
HTRSHASTAT QTPRGSSSTR ARSQGPRDTD DDEEEPDPYG FIVQTAEIAE IARLSQTLVK
DVAILAREIH DVAGDGDSLG SPGPTRSPSL GNVPNTPAST ISAREELVQR IPEASLNFQK
VPPGSMNSHN LDQNMNDSRD DALTNKTRPR NREEVIFDNL MLNPVSQLSH AIRENTEHLA
EKMKVLFQNT GRAWEDLEAR INSENEVPIL KTSNKEISSI LKELRRVQKQ LEVINAIVDP
SLNLDLLMGN RAPSGSGQPG LGKARPAAQS STSPASVDTL LPALPLRSFP QRANCGPPGL
PEPAFLPDAE RFLI
