LOCUS NP_003183 346 aa linear PRI 28-APR-2025
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 Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
TITLE Interactome Mapping Provides a Network of Neurodegenerative Disease
Proteins and Uncovers Widespread Protein Aggregation in Affected
Brains
JOURNAL Cell Rep 32 (7), 108050 (2020)
PUBMED 32814053
REFERENCE 2 (residues 1 to 346)
AUTHORS Garcia-Mayoral,M.F., Castano,R., Fanarraga,M.L., Zabala,J.C.,
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 3 (residues 1 to 346)
AUTHORS Hage-Sleiman,R., Herveau,S., Matera,E.L., Laurier,J.F. 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 4 (residues 1 to 346)
AUTHORS Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
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 5 (residues 1 to 346)
AUTHORS Grayson,C., Bartolini,F., Chapple,J.P., Willison,K.R.,
Bhamidipati,A., Lewis,S.A., Luthert,P.J., Hardcastle,A.J.,
Cowan,N.J. and Cheetham,M.E.
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 6 (residues 1 to 346)
AUTHORS Bartolini,F., Bhamidipati,A., Thomas,S., Schwahn,U., Lewis,S.A. and
Cowan,N.J.
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 7 (residues 1 to 346)
AUTHORS Tian,G., Huang,Y., Rommelaere,H., Vandekerckhove,J., Ampe,C. and
Cowan,N.J.
TITLE Pathway leading to correctly folded beta-tubulin
JOURNAL Cell 86 (2), 287-296 (1996)
PUBMED 8706133
REFERENCE 8 (residues 1 to 346)
AUTHORS Lewis,S.A., Tian,G., Vainberg,I.E. and Cowan,N.J.
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
Region 1..26
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15814.2)"
Site 1
/site_type="acetylation"
/note="N-acetylmethionine.
/evidence=ECO:0007744|PubMed:22223895,
ECO:0007744|PubMed:22814378; propagated from
UniProtKB/Swiss-Prot (Q15814.2)"
Region 27..135
/region_name="TBCC_N"
/note="Tubulin-specific chaperone C N-terminal domain;
pfam16752"
/db_xref="CDD:465258"
Site 80
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:23186163; propagated from
UniProtKB/Swiss-Prot (Q15814.2)"
Region 140..171
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q15814.2)"
Site 168
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
propagated from UniProtKB/Swiss-Prot (Q15814.2)"
Region 204..321
/region_name="TBCC"
/note="Tubulin binding cofactor C; pfam07986"
/db_xref="CDD:462331"
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
//
