TBCEL_HUMAN
ID TBCEL_HUMAN Reviewed; 424 AA.
AC Q5QJ74; Q0VAN6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tubulin-specific chaperone cofactor E-like protein;
DE Short=EL;
DE AltName: Full=Leucine-rich repeat-containing protein 35;
GN Name=TBCEL; Synonyms=LRRC35;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15728251; DOI=10.1242/jcs.01719;
RA Bartolini F., Tian G., Piehl M., Cassimeris L., Lewis S.A., Cowan N.J.;
RT "Identification of a novel tubulin-destabilizing protein related to the
RT chaperone cofactor E.";
RL J. Cell Sci. 118:1197-1207(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Acts as a regulator of tubulin stability.
CC {ECO:0000269|PubMed:15728251}.
CC -!- INTERACTION:
CC Q5QJ74; P52954: LBX1; NbExp=3; IntAct=EBI-10244795, EBI-20141748;
CC Q5QJ74; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10244795, EBI-739832;
CC Q5QJ74; P50222: MEOX2; NbExp=3; IntAct=EBI-10244795, EBI-748397;
CC Q5QJ74; P32243-2: OTX2; NbExp=3; IntAct=EBI-10244795, EBI-9087860;
CC Q5QJ74; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-10244795, EBI-742388;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in testis, but is also present
CC in several tissues at a much lower level.
CC {ECO:0000269|PubMed:15728251}.
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DR EMBL; AY398644; AAR27875.1; -; mRNA.
DR EMBL; AK295673; BAG58531.1; -; mRNA.
DR EMBL; CH471065; EAW67514.1; -; Genomic_DNA.
DR EMBL; BC120988; AAI20989.1; -; mRNA.
DR CCDS; CCDS31692.1; -.
DR RefSeq; NP_001123519.1; NM_001130047.1.
DR RefSeq; NP_689928.3; NM_152715.3.
DR RefSeq; XP_016872815.1; XM_017017326.1.
DR AlphaFoldDB; Q5QJ74; -.
DR BioGRID; 128592; 9.
DR IntAct; Q5QJ74; 6.
DR STRING; 9606.ENSP00000403925; -.
DR GlyGen; Q5QJ74; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5QJ74; -.
DR PhosphoSitePlus; Q5QJ74; -.
DR BioMuta; TBCEL; -.
DR DMDM; 215273924; -.
DR EPD; Q5QJ74; -.
DR jPOST; Q5QJ74; -.
DR MassIVE; Q5QJ74; -.
DR MaxQB; Q5QJ74; -.
DR PaxDb; Q5QJ74; -.
DR PeptideAtlas; Q5QJ74; -.
DR PRIDE; Q5QJ74; -.
DR ProteomicsDB; 63619; -.
DR Antibodypedia; 49450; 171 antibodies from 21 providers.
DR DNASU; 219899; -.
DR Ensembl; ENST00000422003.6; ENSP00000403925.2; ENSG00000154114.13.
DR Ensembl; ENST00000529397.5; ENSP00000437184.1; ENSG00000154114.13.
DR Ensembl; ENST00000683345.1; ENSP00000507873.1; ENSG00000154114.13.
DR GeneID; 219899; -.
DR KEGG; hsa:219899; -.
DR MANE-Select; ENST00000683345.1; ENSP00000507873.1; NM_001363644.2; NP_001350573.1.
DR UCSC; uc001pxo.4; human.
DR CTD; 219899; -.
DR DisGeNET; 219899; -.
DR GeneCards; TBCEL; -.
DR HGNC; HGNC:28115; TBCEL.
DR HPA; ENSG00000154114; Low tissue specificity.
DR MIM; 610451; gene.
DR neXtProt; NX_Q5QJ74; -.
DR OpenTargets; ENSG00000154114; -.
DR PharmGKB; PA162405374; -.
DR VEuPathDB; HostDB:ENSG00000154114; -.
DR eggNOG; KOG2982; Eukaryota.
DR GeneTree; ENSGT00530000063405; -.
DR HOGENOM; CLU_017716_1_1_1; -.
DR InParanoid; Q5QJ74; -.
DR OMA; TYLDWAC; -.
DR OrthoDB; 1495296at2759; -.
DR PhylomeDB; Q5QJ74; -.
DR TreeFam; TF320819; -.
DR PathwayCommons; Q5QJ74; -.
DR SignaLink; Q5QJ74; -.
DR BioGRID-ORCS; 219899; 7 hits in 1076 CRISPR screens.
DR ChiTaRS; TBCEL; human.
DR GenomeRNAi; 219899; -.
DR Pharos; Q5QJ74; Tdark.
DR PRO; PR:Q5QJ74; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q5QJ74; protein.
DR Bgee; ENSG00000154114; Expressed in secondary oocyte and 185 other tissues.
DR ExpressionAtlas; Q5QJ74; baseline and differential.
DR Genevisible; Q5QJ74; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044994; TBCE.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR15140; PTHR15140; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Leucine-rich repeat; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..424
FT /note="Tubulin-specific chaperone cofactor E-like protein"
FT /id="PRO_0000239668"
FT REPEAT 73..98
FT /note="LRR 1"
FT REPEAT 99..123
FT /note="LRR 2"
FT REPEAT 124..147
FT /note="LRR 3"
FT REPEAT 150..172
FT /note="LRR 4"
FT REPEAT 173..197
FT /note="LRR 5"
FT REPEAT 199..224
FT /note="LRR 6"
FT REPEAT 226..250
FT /note="LRR 7"
FT DOMAIN 262..303
FT /note="LRRCT"
FT DOMAIN 334..424
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT COILED 349..375
FT /evidence="ECO:0000255"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C5W3"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 226
FT /note="F -> V (in Ref. 1; AAR27875)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="K -> R (in Ref. 1; AAR27875)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="A -> T (in Ref. 1; AAR27875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 48195 MW; F9057405EB096A9E CRC64;
MDQPSGRSFM QVLCEKYSPE NFPYRRGPGM GVHVPATPQG SPMKDRLNLP SVLVLNSCGI
TCAGDEKEIA AFCAHVSELD LSDNKLEDWH EVSKIVSNVP QLEFLNLSSN PLNLSVLERT
CAGSFSGVRK LVLNNSKASW ETVHMILQEL PDLEELFLCL NDYETVSCPS ICCHSLKLLH
ITDNNLQDWT EIRKLGVMFP SLDTLVLANN HLNAIEEPDD SLARLFPNLR SISLHKSGLQ
SWEDIDKLNS FPKLEEVRLL GIPLLQPYTT EERRKLVIAR LPSVSKLNGS VVTDGEREDS
ERFFIRYYVD VPQEEVPFRY HELITKYGKL EPLAEVDLRP QSSAKVEVHF NDQVEEMSIR
LDQTVAELKK QLKTLVQLPT SNMLLYYFDH EAPFGPEEMK YSSRALHSFG IRDGDKIYVE
SKTK
