Full text data of TBCB
TBCB
(CG22, CKAP1)
[Confidence: low (only semi-automatic identification from reviews)]
Tubulin-folding cofactor B (Cytoskeleton-associated protein 1; Cytoskeleton-associated protein CKAPI; Tubulin-specific chaperone B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tubulin-folding cofactor B (Cytoskeleton-associated protein 1; Cytoskeleton-associated protein CKAPI; Tubulin-specific chaperone B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q99426
ID TBCB_HUMAN Reviewed; 244 AA.
AC Q99426; O00111; O00674; O14728;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JUL-1998, sequence version 2.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Tubulin-folding cofactor B;
DE AltName: Full=Cytoskeleton-associated protein 1;
DE AltName: Full=Cytoskeleton-associated protein CKAPI;
DE AltName: Full=Tubulin-specific chaperone B;
GN Name=TBCB; Synonyms=CG22, CKAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9265649; DOI=10.1083/jcb.138.4.821;
RA Tian G., Lewis S.A., Feierbach B., Stearns T., Rommelaere H., Ampe C.,
RA Cowan N.J.;
RT "Tubulin subunits exist in an activated conformational state generated
RT and maintained by protein cofactors.";
RL J. Cell Biol. 138:821-832(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-244.
RC TISSUE=Fetal brain;
RX PubMed=8978778;
RA Watanabe T.K., Shimizu F., Nagata M., Kawai A., Fujiwara T.,
RA Nakamura Y., Takahashi E., Hirai Y.;
RT "Cloning, expression, and mapping of CKAPI, which encodes a putative
RT cytoskeleton-associated protein containing a CAP-Gly domain.";
RL Cytogenet. Cell Genet. 72:208-211(1996).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP INTERACTION WITH GAN.
RX PubMed=16303566; DOI=10.1016/j.cub.2005.10.052;
RA Wang W., Ding J., Allen E., Zhu P., Zhang L., Vogel H., Yang Y.;
RT "Gigaxonin interacts with tubulin folding cofactor B and controls its
RT degradation through the ubiquitin-proteasome pathway.";
RL Curr. Biol. 15:2050-2055(2005).
RN [8]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-65 AND SER-128, AND
RP MUTAGENESIS OF SER-65 AND SER-128.
RX PubMed=15831477; DOI=10.1128/MCB.25.9.3726-3736.2005;
RA Vadlamudi R.K., Barnes C.J., Rayala S., Li F., Balasenthil S.,
RA Marcus S., Goodson H.V., Sahin A.A., Kumar R.;
RT "p21-activated kinase 1 regulates microtubule dynamics by
RT phosphorylating tubulin cofactor B.";
RL Mol. Cell. Biol. 25:3726-3736(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Binds to alpha-tubulin folding intermediates after their
CC interaction with cytosolic chaperonin in the pathway leading from
CC newly synthesized tubulin to properly folded heterodimer. Involved
CC in regulation of tubulin heterodimer dissociation. May function as
CC a negative regulator of axonal growth.
CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC function by capturing and stabilizing tubulin in a quasi-native
CC conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC interaction with cofactor C then causes the release of tubulin
CC polypeptides that are committed to the native state. Cofactors B
CC and E can form a heterodimer which binds to alpha-tubulin and
CC enhances their ability to dissociate tubulin heterodimers. Binds
CC to GAN.
CC -!- INTERACTION:
CC Q9H2C0:GAN; NbExp=3; IntAct=EBI-764356, EBI-764342;
CC Q93009:USP7; NbExp=2; IntAct=EBI-764356, EBI-302474;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC Note=Colocalizes with microtubules. In differentiated neurons,
CC located in the cytoplasm. In differentiating neurons, accumulates
CC at the growth cone.
CC -!- TISSUE SPECIFICITY: Found in most tissues.
CC -!- PTM: Phosphorylation by PAK1 is required for normal function.
CC -!- PTM: Ubiquitinated in the presence of GAN which targets it for
CC degradation by the proteasome (By similarity).
CC -!- SIMILARITY: Belongs to the TBCB family.
CC -!- SIMILARITY: Contains 1 CAP-Gly domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51182.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF013488; AAB67716.1; -; mRNA.
DR EMBL; BT007424; AAP36092.1; -; mRNA.
DR EMBL; AD001527; AAB51182.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC005969; AAH05969.1; -; mRNA.
DR EMBL; BC052812; AAH52812.1; -; mRNA.
DR EMBL; D49738; BAA08572.1; -; mRNA.
DR RefSeq; NP_001272.2; NM_001281.2.
DR UniGene; Hs.31053; -.
DR ProteinModelPortal; Q99426; -.
DR SMR; Q99426; 11-93, 134-233.
DR IntAct; Q99426; 3.
DR MINT; MINT-2855745; -.
DR STRING; 9606.ENSP00000221855; -.
DR PhosphoSite; Q99426; -.
DR DMDM; 3023518; -.
DR OGP; Q99426; -.
DR PaxDb; Q99426; -.
DR PeptideAtlas; Q99426; -.
DR PRIDE; Q99426; -.
DR DNASU; 1155; -.
DR Ensembl; ENST00000221855; ENSP00000221855; ENSG00000105254.
DR GeneID; 1155; -.
DR KEGG; hsa:1155; -.
DR UCSC; uc002odg.1; human.
DR CTD; 1155; -.
DR GeneCards; GC19P036605; -.
DR HGNC; HGNC:1989; TBCB.
DR HPA; HPA041428; -.
DR HPA; HPA041722; -.
DR MIM; 601303; gene.
DR neXtProt; NX_Q99426; -.
DR PharmGKB; PA162405357; -.
DR eggNOG; COG5244; -.
DR HOGENOM; HOG000209180; -.
DR HOVERGEN; HBG003239; -.
DR InParanoid; Q99426; -.
DR KO; K17262; -.
DR OMA; KLEPITG; -.
DR OrthoDB; EOG7C2R2R; -.
DR PhylomeDB; Q99426; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; TBCB; human.
DR GeneWiki; TBCB; -.
DR GenomeRNAi; 1155; -.
DR NextBio; 4796; -.
DR PRO; PR:Q99426; -.
DR ArrayExpress; Q99426; -.
DR Bgee; Q99426; -.
DR CleanEx; HS_TBCB; -.
DR Genevestigator; Q99426; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; TAS:ProtInc.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR027933; Ubiquitin-like_dom.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Microtubule; Neurogenesis;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1 244 Tubulin-folding cofactor B.
FT /FTId=PRO_0000083534.
FT DOMAIN 183 225 CAP-Gly.
FT MOD_RES 65 65 Phosphoserine; by PAK1.
FT MOD_RES 98 98 Phosphotyrosine.
FT MOD_RES 110 110 Phosphoserine.
FT MOD_RES 128 128 Phosphoserine; by PAK1.
FT MOD_RES 219 219 N6-acetyllysine.
FT MUTAGEN 65 65 S->A: Reduced phosphorylation by PAK1.
FT Reduced microtubule polymerization and
FT loss of phosphorylation by PAK1; when
FT associated with A-128.
FT MUTAGEN 128 128 S->A: Reduced phosphorylation by PAK1.
FT Reduced microtubule polymerization and
FT loss of phosphorylation by PAK1; when
FT associated with A-65.
FT CONFLICT 128 128 S -> R (in Ref. 1; AAB67716).
SQ SEQUENCE 244 AA; 27326 MW; E984C7C74A105384 CRC64;
MEVTGVSAPT VTVFISSSLN TFRSEKRYSR SLTIAEFKCK LELLVGSPAS CMELELYGVD
DKFYSKLDQE DALLGSYPVD DGCRIHVIDH SGARLGEYED VSRVEKYTIS QEAYDQRQDT
VRSFLKRSKL GRYNEEERAQ QEAEAAQRLA EEKAQASSIP VGSRCEVRAA GQSPRRGTVM
YVGLTDFKPG YWIGVRYDEP LGKNDGSVNG KRYFECQAKY GAFVKPAVVT VGDFPEEDYG
LDEI
//
ID TBCB_HUMAN Reviewed; 244 AA.
AC Q99426; O00111; O00674; O14728;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JUL-1998, sequence version 2.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Tubulin-folding cofactor B;
DE AltName: Full=Cytoskeleton-associated protein 1;
DE AltName: Full=Cytoskeleton-associated protein CKAPI;
DE AltName: Full=Tubulin-specific chaperone B;
GN Name=TBCB; Synonyms=CG22, CKAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9265649; DOI=10.1083/jcb.138.4.821;
RA Tian G., Lewis S.A., Feierbach B., Stearns T., Rommelaere H., Ampe C.,
RA Cowan N.J.;
RT "Tubulin subunits exist in an activated conformational state generated
RT and maintained by protein cofactors.";
RL J. Cell Biol. 138:821-832(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-244.
RC TISSUE=Fetal brain;
RX PubMed=8978778;
RA Watanabe T.K., Shimizu F., Nagata M., Kawai A., Fujiwara T.,
RA Nakamura Y., Takahashi E., Hirai Y.;
RT "Cloning, expression, and mapping of CKAPI, which encodes a putative
RT cytoskeleton-associated protein containing a CAP-Gly domain.";
RL Cytogenet. Cell Genet. 72:208-211(1996).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP INTERACTION WITH GAN.
RX PubMed=16303566; DOI=10.1016/j.cub.2005.10.052;
RA Wang W., Ding J., Allen E., Zhu P., Zhang L., Vogel H., Yang Y.;
RT "Gigaxonin interacts with tubulin folding cofactor B and controls its
RT degradation through the ubiquitin-proteasome pathway.";
RL Curr. Biol. 15:2050-2055(2005).
RN [8]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-65 AND SER-128, AND
RP MUTAGENESIS OF SER-65 AND SER-128.
RX PubMed=15831477; DOI=10.1128/MCB.25.9.3726-3736.2005;
RA Vadlamudi R.K., Barnes C.J., Rayala S., Li F., Balasenthil S.,
RA Marcus S., Goodson H.V., Sahin A.A., Kumar R.;
RT "p21-activated kinase 1 regulates microtubule dynamics by
RT phosphorylating tubulin cofactor B.";
RL Mol. Cell. Biol. 25:3726-3736(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Binds to alpha-tubulin folding intermediates after their
CC interaction with cytosolic chaperonin in the pathway leading from
CC newly synthesized tubulin to properly folded heterodimer. Involved
CC in regulation of tubulin heterodimer dissociation. May function as
CC a negative regulator of axonal growth.
CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC function by capturing and stabilizing tubulin in a quasi-native
CC conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC interaction with cofactor C then causes the release of tubulin
CC polypeptides that are committed to the native state. Cofactors B
CC and E can form a heterodimer which binds to alpha-tubulin and
CC enhances their ability to dissociate tubulin heterodimers. Binds
CC to GAN.
CC -!- INTERACTION:
CC Q9H2C0:GAN; NbExp=3; IntAct=EBI-764356, EBI-764342;
CC Q93009:USP7; NbExp=2; IntAct=EBI-764356, EBI-302474;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC Note=Colocalizes with microtubules. In differentiated neurons,
CC located in the cytoplasm. In differentiating neurons, accumulates
CC at the growth cone.
CC -!- TISSUE SPECIFICITY: Found in most tissues.
CC -!- PTM: Phosphorylation by PAK1 is required for normal function.
CC -!- PTM: Ubiquitinated in the presence of GAN which targets it for
CC degradation by the proteasome (By similarity).
CC -!- SIMILARITY: Belongs to the TBCB family.
CC -!- SIMILARITY: Contains 1 CAP-Gly domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51182.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF013488; AAB67716.1; -; mRNA.
DR EMBL; BT007424; AAP36092.1; -; mRNA.
DR EMBL; AD001527; AAB51182.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC005969; AAH05969.1; -; mRNA.
DR EMBL; BC052812; AAH52812.1; -; mRNA.
DR EMBL; D49738; BAA08572.1; -; mRNA.
DR RefSeq; NP_001272.2; NM_001281.2.
DR UniGene; Hs.31053; -.
DR ProteinModelPortal; Q99426; -.
DR SMR; Q99426; 11-93, 134-233.
DR IntAct; Q99426; 3.
DR MINT; MINT-2855745; -.
DR STRING; 9606.ENSP00000221855; -.
DR PhosphoSite; Q99426; -.
DR DMDM; 3023518; -.
DR OGP; Q99426; -.
DR PaxDb; Q99426; -.
DR PeptideAtlas; Q99426; -.
DR PRIDE; Q99426; -.
DR DNASU; 1155; -.
DR Ensembl; ENST00000221855; ENSP00000221855; ENSG00000105254.
DR GeneID; 1155; -.
DR KEGG; hsa:1155; -.
DR UCSC; uc002odg.1; human.
DR CTD; 1155; -.
DR GeneCards; GC19P036605; -.
DR HGNC; HGNC:1989; TBCB.
DR HPA; HPA041428; -.
DR HPA; HPA041722; -.
DR MIM; 601303; gene.
DR neXtProt; NX_Q99426; -.
DR PharmGKB; PA162405357; -.
DR eggNOG; COG5244; -.
DR HOGENOM; HOG000209180; -.
DR HOVERGEN; HBG003239; -.
DR InParanoid; Q99426; -.
DR KO; K17262; -.
DR OMA; KLEPITG; -.
DR OrthoDB; EOG7C2R2R; -.
DR PhylomeDB; Q99426; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; TBCB; human.
DR GeneWiki; TBCB; -.
DR GenomeRNAi; 1155; -.
DR NextBio; 4796; -.
DR PRO; PR:Q99426; -.
DR ArrayExpress; Q99426; -.
DR Bgee; Q99426; -.
DR CleanEx; HS_TBCB; -.
DR Genevestigator; Q99426; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; TAS:ProtInc.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR027933; Ubiquitin-like_dom.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Microtubule; Neurogenesis;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1 244 Tubulin-folding cofactor B.
FT /FTId=PRO_0000083534.
FT DOMAIN 183 225 CAP-Gly.
FT MOD_RES 65 65 Phosphoserine; by PAK1.
FT MOD_RES 98 98 Phosphotyrosine.
FT MOD_RES 110 110 Phosphoserine.
FT MOD_RES 128 128 Phosphoserine; by PAK1.
FT MOD_RES 219 219 N6-acetyllysine.
FT MUTAGEN 65 65 S->A: Reduced phosphorylation by PAK1.
FT Reduced microtubule polymerization and
FT loss of phosphorylation by PAK1; when
FT associated with A-128.
FT MUTAGEN 128 128 S->A: Reduced phosphorylation by PAK1.
FT Reduced microtubule polymerization and
FT loss of phosphorylation by PAK1; when
FT associated with A-65.
FT CONFLICT 128 128 S -> R (in Ref. 1; AAB67716).
SQ SEQUENCE 244 AA; 27326 MW; E984C7C74A105384 CRC64;
MEVTGVSAPT VTVFISSSLN TFRSEKRYSR SLTIAEFKCK LELLVGSPAS CMELELYGVD
DKFYSKLDQE DALLGSYPVD DGCRIHVIDH SGARLGEYED VSRVEKYTIS QEAYDQRQDT
VRSFLKRSKL GRYNEEERAQ QEAEAAQRLA EEKAQASSIP VGSRCEVRAA GQSPRRGTVM
YVGLTDFKPG YWIGVRYDEP LGKNDGSVNG KRYFECQAKY GAFVKPAVVT VGDFPEEDYG
LDEI
//
MIM
601303
*RECORD*
*FIELD* NO
601303
*FIELD* TI
*601303 CYTOSKELETON-ASSOCIATED PROTEIN 1; CKAP1
;;CKAPI
*FIELD* TX
The cytoskeleton is composed of 3 structural elements: actin filaments,
read moremicrotubules, and intermediate filaments. Cytoskeletal activity is
modulated by many cytoskeleton-associated proteins (CAPs). One group of
CAPs is characterized by a highly conserved glycine motif, the CAP-GLY
domain, which may contribute to its association with microtubules.
Members of the group of CAPs include dynactin (601143), the
dynein-associated protein. Watanabe et al. (1996) isolated a novel
member of this family, which they called CKAPI (for
cytoskeleton-associated protein I, glycine motif). The cDNA was isolated
from a human fetal-brain cDNA library and found to contain an open
reading frame of 579 nucleotides encoding a 193-amino acid polypeptide.
Three transcripts of different sizes were expressed in all tissues
examined. By fluorescence in situ hybridization, Watanabe et al. (1996)
assigned the gene to 19q13.11-q13.12.
*FIELD* RF
1. Watanabe, T. K.; Shimizu, F.; Nagata, M.; Kawai, A.; Fujiwara,
T.; Nakamura, Y.; Takahashi, E.; Hirai, Y.: Cloning, expression,
and mapping of CKAP1, which encodes a putative cytoskeleton-associated
protein containing a CAP-GLY domain. Cytogenet. Cell Genet. 72:
208-211, 1996.
*FIELD* CD
Victor A. McKusick: 6/11/1996
*FIELD* ED
mark: 06/11/1996
*RECORD*
*FIELD* NO
601303
*FIELD* TI
*601303 CYTOSKELETON-ASSOCIATED PROTEIN 1; CKAP1
;;CKAPI
*FIELD* TX
The cytoskeleton is composed of 3 structural elements: actin filaments,
read moremicrotubules, and intermediate filaments. Cytoskeletal activity is
modulated by many cytoskeleton-associated proteins (CAPs). One group of
CAPs is characterized by a highly conserved glycine motif, the CAP-GLY
domain, which may contribute to its association with microtubules.
Members of the group of CAPs include dynactin (601143), the
dynein-associated protein. Watanabe et al. (1996) isolated a novel
member of this family, which they called CKAPI (for
cytoskeleton-associated protein I, glycine motif). The cDNA was isolated
from a human fetal-brain cDNA library and found to contain an open
reading frame of 579 nucleotides encoding a 193-amino acid polypeptide.
Three transcripts of different sizes were expressed in all tissues
examined. By fluorescence in situ hybridization, Watanabe et al. (1996)
assigned the gene to 19q13.11-q13.12.
*FIELD* RF
1. Watanabe, T. K.; Shimizu, F.; Nagata, M.; Kawai, A.; Fujiwara,
T.; Nakamura, Y.; Takahashi, E.; Hirai, Y.: Cloning, expression,
and mapping of CKAP1, which encodes a putative cytoskeleton-associated
protein containing a CAP-GLY domain. Cytogenet. Cell Genet. 72:
208-211, 1996.
*FIELD* CD
Victor A. McKusick: 6/11/1996
*FIELD* ED
mark: 06/11/1996