TTC28_MOUSE
ID TTC28_MOUSE Reviewed; 2450 AA.
AC Q80XJ3; J3QM46; J3QQ36; Q6P9J6; Q80TL5; Q8BV10; Q8C0F2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Tetratricopeptide repeat protein 28;
DE Short=TPR repeat protein 28;
GN Name=Ttc28; Synonyms=Kiaa1043, Tprbk;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 746-2450.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 780-2450.
RC TISSUE=Brain;
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 [4]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1769-2450.
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Embryonic testis;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1584, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=23036704; DOI=10.1016/j.gene.2012.09.061;
RA Izumiyama T., Minoshima S., Yoshida T., Shimizu N.;
RT "A novel big protein TPRBK possessing 25 units of TPR motif is essential
RT for the progress of mitosis and cytokinesis.";
RL Gene 511:202-217(2012).
CC -!- FUNCTION: During mitosis, may be involved in the condensation of
CC spindle midzone microtubules, leading to the formation of midbody.
CC {ECO:0000250}.
CC -!- FUNCTION: Essential for the formation and integrity of the midbody. Max
CC play a critical role in the progress of mitosis and cytokinesis during
CC cell cycle (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AURKB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250}. Midbody {ECO:0000250}.
CC Note=At interphase, localizes to centrosomes. At prometaphase and
CC metaphase, associated with spindle microtubules and spindle poles. At
CC anaphase, accumulates in the spindle midzone. At telophase, condensed
CC on central spindles. During cytokinesis, condensed on the midbody where
CC it colocalizes with AURKB (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos at all stages examined. In
CC adult tissues, detected in heart and at low levels in kidney and
CC testis. {ECO:0000269|PubMed:23036704}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46779.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH60735.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65709.2; Type=Miscellaneous discrepancy; Note=Several sequencing errors and erroneous CDS prediction.; Evidence={ECO:0000305};
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DR EMBL; AC121934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC147632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046779; AAH46779.2; ALT_INIT; mRNA.
DR EMBL; BC060735; AAH60735.1; ALT_INIT; mRNA.
DR EMBL; AK122427; BAC65709.2; ALT_SEQ; mRNA.
DR EMBL; AK031458; BAC27414.1; -; mRNA.
DR EMBL; AK081382; BAC38208.1; -; mRNA.
DR CCDS; CCDS59682.1; -.
DR RefSeq; NP_001254551.1; NM_001267622.1.
DR AlphaFoldDB; Q80XJ3; -.
DR SMR; Q80XJ3; -.
DR BioGRID; 229101; 1.
DR IntAct; Q80XJ3; 2.
DR STRING; 10090.ENSMUSP00000136116; -.
DR iPTMnet; Q80XJ3; -.
DR PhosphoSitePlus; Q80XJ3; -.
DR EPD; Q80XJ3; -.
DR MaxQB; Q80XJ3; -.
DR PaxDb; Q80XJ3; -.
DR PeptideAtlas; Q80XJ3; -.
DR PRIDE; Q80XJ3; -.
DR ProteomicsDB; 297674; -.
DR Antibodypedia; 5496; 7 antibodies from 5 providers.
DR DNASU; 209683; -.
DR Ensembl; ENSMUST00000156290; ENSMUSP00000137609; ENSMUSG00000033209.
DR GeneID; 209683; -.
DR KEGG; mmu:209683; -.
DR UCSC; uc033ild.1; mouse.
DR CTD; 23331; -.
DR MGI; MGI:2140873; Ttc28.
DR VEuPathDB; HostDB:ENSMUSG00000033209; -.
DR eggNOG; KOG0548; Eukaryota.
DR GeneTree; ENSGT00940000156428; -.
DR InParanoid; Q80XJ3; -.
DR OrthoDB; 733786at2759; -.
DR TreeFam; TF328344; -.
DR BioGRID-ORCS; 209683; 6 hits in 70 CRISPR screens.
DR ChiTaRS; Ttc28; mouse.
DR PRO; PR:Q80XJ3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80XJ3; protein.
DR Bgee; ENSMUSG00000033209; Expressed in rostral migratory stream and 241 other tissues.
DR ExpressionAtlas; Q80XJ3; baseline and differential.
DR Genevisible; Q80XJ3; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:1990023; C:mitotic spindle midzone; ISO:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:MGI.
DR Gene3D; 1.25.40.10; -; 6.
DR InterPro; IPR024983; CHAT_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF12770; CHAT; 1.
DR Pfam; PF13176; TPR_7; 1.
DR SMART; SM00028; TPR; 25.
DR SUPFAM; SSF48452; SSF48452; 7.
DR PROSITE; PS50005; TPR; 25.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..2450
FT /note="Tetratricopeptide repeat protein 28"
FT /id="PRO_0000106428"
FT REPEAT 52..85
FT /note="TPR 1"
FT REPEAT 87..119
FT /note="TPR 2"
FT REPEAT 120..153
FT /note="TPR 3"
FT REPEAT 190..223
FT /note="TPR 4"
FT REPEAT 228..261
FT /note="TPR 5"
FT REPEAT 268..301
FT /note="TPR 6"
FT REPEAT 308..341
FT /note="TPR 7"
FT REPEAT 348..381
FT /note="TPR 8"
FT REPEAT 388..421
FT /note="TPR 9"
FT REPEAT 428..461
FT /note="TPR 10"
FT REPEAT 468..501
FT /note="TPR 11"
FT REPEAT 508..541
FT /note="TPR 12"
FT REPEAT 548..581
FT /note="TPR 13"
FT REPEAT 588..621
FT /note="TPR 14"
FT REPEAT 628..661
FT /note="TPR 15"
FT REPEAT 668..701
FT /note="TPR 16"
FT REPEAT 708..741
FT /note="TPR 17"
FT REPEAT 748..781
FT /note="TPR 18"
FT REPEAT 788..821
FT /note="TPR 19"
FT REPEAT 828..861
FT /note="TPR 20"
FT REPEAT 871..904
FT /note="TPR 21"
FT REPEAT 911..944
FT /note="TPR 22"
FT REPEAT 951..984
FT /note="TPR 23"
FT REPEAT 991..1024
FT /note="TPR 24"
FT REPEAT 1031..1064
FT /note="TPR 25"
FT REPEAT 1071..1104
FT /note="TPR 26"
FT REPEAT 1111..1144
FT /note="TPR 27"
FT REPEAT 1163..1196
FT /note="TPR 28"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2001..2364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2091..2142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2156..2170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2189..2250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2284..2316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY4"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY4"
FT MOD_RES 1584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2098
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY4"
FT MOD_RES 2216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY4"
FT MOD_RES 2365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY4"
FT MOD_RES 2370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AY4"
FT CONFLICT 1769
FT /note="V -> L (in Ref. 5; BAC27414)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2450 AA; 267459 MW; 5E1B47053C61AC99 CRC64;
MEQPPPLAPE PASARSRRRR EPESPPAPIP LFGARTVVQR SPDEPALSKA EFVEKVRQSN
QACHDGDFHT AIVLYNEALA VDPQNCILYS NRSAAYMKTQ QYHKALDDAI KARLLNPKWP
KAYFRQGVAL QYLGRHADAL AAFASGLAQD PKSLQLLVGM VEAAMKSPMR DTLEPTYQQL
QKMKLDKSPF VVVSVVGQEL LTAGHHGASV VVLEAALKIG TCSLKLRGSV FSALSSAHWS
LGNTEKSTGY MQQDLDVAKT LGDQTGECRA HGNLGSAFFS KGNYREALTN HRHQLVLAMK
LKDREAASSA LSSLGHVYTA IGDYPNALAS HKQCVLLAKQ SKDDLSEARE LGNMGAVYIA
MGDFENAVQC HEQHLRIAKD LGSKREEARA YSNLGSAYHY RRNFDKAMSY HNCVLELAQE
LMEKPIEMRA YAGLGHAARC MQDLERAKQY HEQQLGIAED LKDRAAEGRA SSNLGIIHQM
KGDYDTALKL HKTHLCIAQE LSDYAAQGRA YGNMGNAYNA LGMYDQAVKY HRQELQISME
VNDRASQAST HGNLAVAYQA LGAHDRALQH YQNHLNIARE LRDIQSEARA LSNLGNFHCS
RGEYVQAAPY YEQYLRLAPD LQDMEGEGKV CHNLGYAHYC LGNYQEAVKY YEQDLALAKD
LHDKLSQAKA YCNLGLAFKA LLNFAKAEEC QKYLLSLAQS LDNSQAKFRA LGNLGDIFIC
KKDINGAIKF YEQQLGLSHH VKDRRLEASA YAALGTAYRM VQKYDKALGY HTQELEVYQE
LSDLPGECRA HGHLAAVYMA LGKYTMAFKC YQEQLELGRK LKEPSLEAQV YGNMGITKMN
MNVMEDAIGY FEQQLAMLQQ LSGNESVLDR GRAYGNLGDC YEALGDYEEA IKYYEQYLSV
AQSLNRMQDQ AKAYRGLGNG HRATGSLQQA LVCFEKRLVV AHELGEASNK AQAYGELGSL
HSQLGNYEQA ISCLERQLNI ARDMKDRALE SDAACGLGGV YQQMGEYDTA LQYHQLDLQI
AEETDNPTCQ GRAYGNLGLT YESLGTFERA VVYQEQHLSI AAQMNDLVAK TVSYSSLGRT
HHALQNYSQA VMYLQEGLRL AEQLGRREDE AKIRHGLGLS LWASGNLEEA QHQLYRASAL
FETIRHEAQL STDYKLSLFD LQTSSYQALQ RVLVSLGHHD EALAVAERGR TRAFADLLVE
RQTGQQDSDP YSPITIDQIL EMVNAQRGLV LYYSLAAGYL YSWLLAPGAG ILKFHEHYLG
DNSVESSSDF QAGSSAALPV ATNSTLEQHI ASVREALGVE SYYSRACASS ETESEAGDIM
EQQLEEMNKQ LNSVTDPTGF LRMVRHNNLL HRSCQSMTSL FSGTVSPSKD GTSSLPRRQN
SLAKPPLRAL YDLLIAPMEG GLMHSSGPVG RHRQLVLVLE GELYFVPFAL LKGSASNEYL
YERFTLIAVP AVRSLGPHSK CHLRKTPPTY SSSTTMAAVI GNPKLPSAVM DRWLWGPMPS
AEEEAFMVSE LLGCQPLVGS MATKERVMSA LTQAECVHFA THVSWKLSAL VLTPNTEGNP
AGSKSSFGHP YTIPESLRVQ DDASDVESIS DCPPLRELLL TAADLLDLRL SVKLVVLSSS
QEANGRVTAD GLVALTRAFL AAGAQCVLVA LWPVPVAASK MFVHAFYSSL LNGLKASASL
GEAMKVVQSS KAFSHPSNWA GFTLIGSDVK LNSPSSLIGQ ALTEILQHPE RARDALRVLL
HLVEKSLQRI QNGQRNAMYT SQQSVENKVG GIPGWQALLT AVGFRLDPAA SGLPAAVFFP
TSDPGDRLQQ CSSTLQALLG LPNPALQALC KLITASETGE QLISRAVKNM VGMLHQVLVQ
LQACEKEQDF ASAPIPVSLS VQLWRLPGCH EFLAALGFDL CEVGQEEVIL KTGKQASRRT
THFALQSLLS LFDSTELPKR LSLDSSSSLE SLASAQSVSN ALPLGYQHPP FSPTGADSIA
SDAISVYSLS SIASSMSFVS KPEGGLEGGG PRGRQDYDRS KSTHPQRATL PRRQTSPQAR
RGASKEEEEY EGFSIISMEP LATYQGEGKT RFSPDPKQPC VKAPGGVRLS VSSKGSVSTP
NSPVKMTLIP SPNSPFQKVG KLASSDTGES DQSSTETDST VKSQEESTPK LDPQELAQRI
LEETKSHLLA VERLQRSGGP AGPDREDSVV APSSTTVFRA SETSAFSKPI LSHQRSQLSP
LTVKPQPPAR SSSLPKVSSP ATSEVSGKDG LSPPGSSHPS PGRDTPVSPA DPPLFRLKYP
SSPYSAHISK SPRNTSPACS APSPALSYSS AGSARSSPAD APDEKVQAVH SLKMLWQSTP
QPPRGPRKTC RGAPGTLTSK RDVLSLLNLS PRHGKEEGGA DRLELKELSV QRHDEVPPKV
PTNGHWCTDT ATLTTAGGRS TTAAPRPLRL PLANGYKFLS PGRLFPSSKC
