LOCUS NP_003183 346 aa linear PRI 21-OCT-2019
DEFINITION tubulin-specific chaperone C [Homo sapiens].
ACCESSION NP_003183
VERSION NP_003183.2
DBSOURCE REFSEQ: accession NM_003192.3
KEYWORDS RefSeq; MANE Select.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 346)
AUTHORS Garcia-Mayoral MF, Castano R, Fanarraga ML, Zabala JC, Rico M and
Bruix M.
TITLE The solution structure of the N-terminal domain of human tubulin
binding cofactor C reveals a platform for tubulin interaction
JOURNAL PLoS ONE 6 (10), e25912 (2011)
PUBMED 22028797
REMARK GeneRIF: a testable model for TBCC N-terminal domain/tubulin
recognition in which the highly charged N-terminus as well as
residues from the three helices and the loops interact with the
acidic hypervariable regions of tubulin monomers
REFERENCE 2 (residues 1 to 346)
AUTHORS Hage-Sleiman R, Herveau S, Matera EL, Laurier JF and Dumontet C.
TITLE Tubulin binding cofactor C (TBCC) suppresses tumor growth and
enhances chemosensitivity in human breast cancer cells
JOURNAL BMC Cancer 10, 135 (2010)
PUBMED 20384997
REMARK GeneRIF: Microtubule dynamicity was reduced in breast cancer cells
overexpressing TBCC. Cell cycle distribution was altered in cells
containing larger amounts of TBCC. TBCC had little effect on cell
proliferation.
Publication Status: Online-Only
REFERENCE 3 (residues 1 to 346)
AUTHORS Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L,
Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel
G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD,
Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker
DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP,
Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC,
Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY,
Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman
LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M,
Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD,
Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ,
Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S,
Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL,
Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL,
Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson
CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK,
Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR,
Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M,
Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A,
Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K,
Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore
B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM,
Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith
M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G,
Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A,
Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL,
Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt
JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard
T, Sulston JE, Dunham I, Rogers J and Beck S.
TITLE The DNA sequence and analysis of human chromosome 6
JOURNAL Nature 425 (6960), 805-811 (2003)
PUBMED 14574404
REFERENCE 4 (residues 1 to 346)
AUTHORS Grayson C, Bartolini F, Chapple JP, Willison KR, Bhamidipati A,
Lewis SA, Luthert PJ, Hardcastle AJ, Cowan NJ and Cheetham ME.
TITLE Localization in the human retina of the X-linked retinitis
pigmentosa protein RP2, its homologue cofactor C and the RP2
interacting protein Arl3
JOURNAL Hum. Mol. Genet. 11 (24), 3065-3074 (2002)
PUBMED 12417528
REFERENCE 5 (residues 1 to 346)
AUTHORS Bartolini F, Bhamidipati A, Thomas S, Schwahn U, Lewis SA and Cowan
NJ.
TITLE Functional overlap between retinitis pigmentosa 2 protein and the
tubulin-specific chaperone cofactor C
JOURNAL J. Biol. Chem. 277 (17), 14629-14634 (2002)
PUBMED 11847227
REMARK GeneRIF: functional overlap with retinitis pigmenosa 2 protein
REFERENCE 6 (residues 1 to 346)
AUTHORS Tian G, Huang Y, Rommelaere H, Vandekerckhove J, Ampe C and Cowan
NJ.
TITLE Pathway leading to correctly folded beta-tubulin
JOURNAL Cell 86 (2), 287-296 (1996)
PUBMED 8706133
REFERENCE 7 (residues 1 to 346)
AUTHORS Lewis SA, Tian G, Vainberg IE and Cowan NJ.
TITLE Chaperonin-mediated folding of actin and tubulin
JOURNAL J. Cell Biol. 132 (1-2), 1-4 (1996)
PUBMED 8567715
REMARK Review article
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AL353716.18.
On May 17, 2019 this sequence version replaced NP_003183.1.
Summary: Cofactor C is one of four proteins (cofactors A, D, E, and
C) involved in the pathway leading to correctly folded beta-tubulin
from folding intermediates. Cofactors A and D are believed to play
a role in capturing and stabilizing beta-tubulin intermediates in a
quasi-native confirmation. Cofactor E binds to the cofactor
D/beta-tubulin complex; interaction with cofactor C then causes the
release of beta-tubulin polypeptides that are committed to the
native state. [provided by RefSeq, Jul 2008].
##Evidence-Data-START##
Transcript is intronless :: SRR3476690.452306.1,
SRR3476690.353594.1 [ECO:0000345]
##Evidence-Data-END##
##RefSeq-Attributes-START##
MANE Ensembl match :: ENST00000372876.2/ ENSP00000361967.1
RefSeq Select criteria :: based on single protein-coding transcript
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..346
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="6"
/map="6p21.1"
Protein 1..346
/product="tubulin-specific chaperone C"
/calculated_mol_wt=39117
Site 1
/site_type="acetylation"
/experiment="experimental evidence, no additional details
recorded"
/note="N-acetylmethionine. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}; propagated from
UniProtKB/Swiss-Prot (Q15814.2)"
Region 29..135
/region_name="TBCC_N"
/note="Tubulin-specific chaperone C N-terminal domain;
pfam16752"
/db_xref="CDD:318871"
Site 80
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/note="Phosphoserine. {ECO:0000244|PubMed:23186163};
propagated from UniProtKB/Swiss-Prot (Q15814.2)"
Site 168
/site_type="phosphorylation"
/experiment="experimental evidence, no additional details
recorded"
/note="Phosphoserine. {ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163};
propagated from UniProtKB/Swiss-Prot (Q15814.2)"
Region 204..321
/region_name="TBCC"
/note="Tubulin binding cofactor C; pfam07986"
/db_xref="CDD:311787"
CDS 1..346
/gene="TBCC"
/gene_synonym="CFC"
/coded_by="NM_003192.3:31..1071"
/db_xref="CCDS:CCDS4872.1"
/db_xref="GeneID:6903"
/db_xref="HGNC:HGNC:11580"
/db_xref="MIM:602971"
ORIGIN
1 mesvscsaaa vrtgdmesqr dlslvperlq rreqerqlev errkqkrqnq evekenshff
61 vatfvreraa veelleraes verleeaasr lqglqklind svfflaaydl rqgqealarl
121 qaalaerrrg lqpkkrfafk trgkdaasst kvdaapgipp avesiqdspl pkkaegdlgp
181 swvcgfsnle sqvlekrase lhqrdvllte lsnctvrlyg npntlrltka hsckllcgpv
241 stsvfledcs dcvlavacqq lrihstkdtr iflqvtsrai vedcsgiqfa pytwsypeid
301 kdfessgldr sknnwndvdd fnwlardmas pnwsilpeee rniqwd
//
