Database: RefSeq
Entry: NP_003183
LinkDB: NP_003183
Original site: NP_003183 
LOCUS       NP_003183                346 aa            linear   PRI 21-OCT-2019
DEFINITION  tubulin-specific chaperone C [Homo sapiens].
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
            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
  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
  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].
            Transcript is intronless :: SRR3476690.452306.1,
                                        SRR3476690.353594.1 [ECO:0000345]
            MANE Ensembl match     :: ENST00000372876.2/ ENSP00000361967.1
            RefSeq Select criteria :: based on single protein-coding transcript
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
     Protein         1..346
                     /product="tubulin-specific chaperone C"
     Site            1
                     /experiment="experimental evidence, no additional details
                     /note="N-acetylmethionine. {ECO:0000244|PubMed:22223895,
                     ECO:0000244|PubMed:22814378}; propagated from
                     UniProtKB/Swiss-Prot (Q15814.2)"
     Region          29..135
                     /note="Tubulin-specific chaperone C N-terminal domain;
     Site            80
                     /experiment="experimental evidence, no additional details
                     /note="Phosphoserine. {ECO:0000244|PubMed:23186163};
                     propagated from UniProtKB/Swiss-Prot (Q15814.2)"
     Site            168
                     /experiment="experimental evidence, no additional details
                     /note="Phosphoserine. {ECO:0000244|PubMed:18669648,
                     ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163};
                     propagated from UniProtKB/Swiss-Prot (Q15814.2)"
     Region          204..321
                     /note="Tubulin binding cofactor C; pfam07986"
     CDS             1..346
        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
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