Full text data of TUBA1B
TUBA1B
[Confidence: low (only semi-automatic identification from reviews)]
Tubulin alpha-1B chain (Alpha-tubulin ubiquitous; Tubulin K-alpha-1; Tubulin alpha-ubiquitous chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tubulin alpha-1B chain (Alpha-tubulin ubiquitous; Tubulin K-alpha-1; Tubulin alpha-ubiquitous chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P68363
ID TBA1B_HUMAN Reviewed; 451 AA.
AC P68363; P04687; P05209; Q27I68;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-1987, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Tubulin alpha-1B chain;
DE AltName: Full=Alpha-tubulin ubiquitous;
DE AltName: Full=Tubulin K-alpha-1;
DE AltName: Full=Tubulin alpha-ubiquitous chain;
GN Name=TUBA1B;
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].
RC TISSUE=Keratinocyte;
RX PubMed=6646120;
RA Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W.;
RT "Expression of human alpha-tubulin genes: interspecies conservation of
RT 3' untranslated regions.";
RL Mol. Cell. Biol. 3:1738-1745(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA de Hostos E.L.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li Q., Liu L., Ma S.;
RT "Gene response of gangliocytes stimulated by Herpes simplex virus type
RT 1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, Eye, Kidney, Lung, Muscle, Placenta, Prostate,
RC Skin, 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 PROTEIN SEQUENCE OF 41-60; 65-79; 113-121; 230-280; 312-320; 327-336;
RP 340-370; 374-390; 395-401 AND 403-422, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 41-79; 65-79; 85-121; 125-164; 216-304; 312-370
RP AND 374-451, PHOSPHORYLATION AT SER-48 AND SER-232, METHYLATION AT
RP ARG-339, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 353-370 AND 395-401.
RC TISSUE=Brain;
RX PubMed=8619814; DOI=10.1006/bbrc.1996.0211;
RA Baumann M.H., Wisniewski T., Levy E., Plant G.T., Ghiso J.;
RT "C-terminal fragments of alpha- and beta-tubulin form amyloid fibrils
RT in vitro and associate with amyloid deposits of familial cerebral
RT amyloid angiopathy, British type.";
RL Biochem. Biophys. Res. Commun. 219:238-242(1996).
RN [8]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC binds two moles of GTP, one at an exchangeable site on the beta
CC chain and one at a non-exchangeable site on the alpha chain.
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is
CC a hollow water-filled tube with an outer diameter of 25 nm and an
CC inner diameter of 15 nM. Alpha-beta heterodimers associate head-
CC to-tail to form protofilaments running lengthwise along the
CC microtubule wall with the beta-tubulin subunit facing the
CC microtubule plus end conferring a structural polarity.
CC Microtubules usually have 13 protofilaments but different
CC protofilament numbers can be found in some organisms and
CC specialized cells.
CC -!- INTERACTION:
CC Q13509:TUBB3; NbExp=3; IntAct=EBI-487083, EBI-350989;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic
CC removal and re-addition of a C-terminal tyrosine residue by the
CC enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin
CC tyrosine ligase (TTL), respectively (By similarity).
CC -!- PTM: Some glutamate residues at the C-terminus are
CC polyglutamylated. This modification occurs exclusively on
CC glutamate residues and results in polyglutamate chains on the
CC gamma-carboxyl group. Also monoglycylated but not polyglycylated
CC due to the absence of functional TTLL10 in human. Monoglycylation
CC is mainly limited to tubulin incorporated into axonemes (cilia and
CC flagella) whereas glutamylation is prevalent in neuronal cells,
CC centrioles, axonemes, and the mitotic spindle. Both modifications
CC can coexist on the same protein on adjacent residues, and lowering
CC glycylation levels increases polyglutamylation, and reciprocally.
CC The precise function of such modifications is still unclear but
CC they regulate the assembly and dynamics of axonemal microtubules
CC (Probable).
CC -!- PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules
CC and affects affinity and processivity of microtubule motors. This
CC modification has a role in multiple cellular functions, ranging
CC from cell motility, cell cycle progression or cell differentiation
CC to intracellular trafficking and signaling (By similarity).
CC -!- SIMILARITY: Belongs to the tubulin family.
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; K00558; AAA91576.1; -; mRNA.
DR EMBL; AF081484; AAC31959.1; -; mRNA.
DR EMBL; DQ400107; ABD60581.1; -; mRNA.
DR EMBL; BC000696; AAH00696.1; -; mRNA.
DR EMBL; BC001128; AAH01128.1; -; mRNA.
DR EMBL; BC006379; AAH06379.1; -; mRNA.
DR EMBL; BC006481; AAH06481.1; -; mRNA.
DR EMBL; BC008659; AAH08659.1; -; mRNA.
DR EMBL; BC009314; AAH09314.1; -; mRNA.
DR EMBL; BC009509; AAH09509.1; -; mRNA.
DR EMBL; BC009512; AAH09512.1; -; mRNA.
DR EMBL; BC009513; AAH09513.1; -; mRNA.
DR EMBL; BC010494; AAH10494.1; -; mRNA.
DR EMBL; BC011572; AAH11572.1; -; mRNA.
DR EMBL; BC015883; AAH15883.1; -; mRNA.
DR EMBL; BC017004; AAH17004.1; -; mRNA.
DR EMBL; BC030820; AAH30820.1; -; mRNA.
DR EMBL; BC071904; AAH71904.1; -; mRNA.
DR PIR; I77403; I77403.
DR RefSeq; NP_006073.2; NM_006082.2.
DR UniGene; Hs.524390; -.
DR PDB; 2E4H; NMR; -; B=416-451.
DR PDBsum; 2E4H; -.
DR ProteinModelPortal; P68363; -.
DR SMR; P68363; 1-440.
DR IntAct; P68363; 18.
DR MINT; MINT-4998849; -.
DR STRING; 9606.ENSP00000336799; -.
DR ChEMBL; CHEMBL2095182; -.
DR PhosphoSite; P68363; -.
DR DMDM; 55977474; -.
DR OGP; P68363; -.
DR SWISS-2DPAGE; P68363; -.
DR PaxDb; P68363; -.
DR PRIDE; P68363; -.
DR DNASU; 10376; -.
DR Ensembl; ENST00000336023; ENSP00000336799; ENSG00000123416.
DR GeneID; 10376; -.
DR KEGG; hsa:10376; -.
DR UCSC; uc001rtl.3; human.
DR CTD; 10376; -.
DR GeneCards; GC12M049523; -.
DR H-InvDB; HIX0079488; -.
DR HGNC; HGNC:18809; TUBA1B.
DR HPA; CAB011513; -.
DR HPA; HPA039247; -.
DR HPA; HPA043684; -.
DR MIM; 602530; gene.
DR neXtProt; NX_P68363; -.
DR PharmGKB; PA162407332; -.
DR eggNOG; COG5023; -.
DR HOGENOM; HOG000165711; -.
DR HOVERGEN; HBG000089; -.
DR InParanoid; P68363; -.
DR KO; K07374; -.
DR OMA; KRATHES; -.
DR OrthoDB; EOG7TBC1W; -.
DR PhylomeDB; P68363; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; TUBA1B; human.
DR EvolutionaryTrace; P68363; -.
DR GeneWiki; TUBA1B; -.
DR GenomeRNAi; 10376; -.
DR NextBio; 39315; -.
DR PRO; PR:P68363; -.
DR ArrayExpress; P68363; -.
DR Bgee; P68363; -.
DR CleanEx; HS_TUBA1B; -.
DR Genevestigator; P68363; -.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; TAS:BHF-UCL.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0051301; P:cell division; TAS:BHF-UCL.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0007017; P:microtubule-based process; TAS:BHF-UCL.
DR GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002452; Alpha_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation;
KW Microtubule; Nitration; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1 451 Tubulin alpha-1B chain.
FT /FTId=PRO_0000048108.
FT NP_BIND 142 148 GTP (Potential).
FT SITE 451 451 Involved in polymerization.
FT MOD_RES 48 48 Phosphoserine.
FT MOD_RES 83 83 Nitrated tyrosine (By similarity).
FT MOD_RES 232 232 Phosphoserine.
FT MOD_RES 282 282 Nitrated tyrosine (By similarity).
FT MOD_RES 339 339 Omega-N-methylarginine.
FT MOD_RES 432 432 Phosphotyrosine (By similarity).
FT MOD_RES 439 439 Phosphoserine (By similarity).
FT CROSSLNK 326 326 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 370 370 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CONFLICT 131 131 G -> R (in Ref. 1; AAA91576).
FT CONFLICT 290 290 E -> D (in Ref. 1; AAA91576).
FT CONFLICT 308 308 R -> G (in Ref. 1; AAA91576).
FT CONFLICT 340 340 S -> T (in Ref. 1; AAA91576).
SQ SEQUENCE 451 AA; 50152 MW; 94355B4EC2086429 CRC64;
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y
//
ID TBA1B_HUMAN Reviewed; 451 AA.
AC P68363; P04687; P05209; Q27I68;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-AUG-1987, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Tubulin alpha-1B chain;
DE AltName: Full=Alpha-tubulin ubiquitous;
DE AltName: Full=Tubulin K-alpha-1;
DE AltName: Full=Tubulin alpha-ubiquitous chain;
GN Name=TUBA1B;
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].
RC TISSUE=Keratinocyte;
RX PubMed=6646120;
RA Cowan N.J., Dobner P., Fuchs E.V., Cleveland D.W.;
RT "Expression of human alpha-tubulin genes: interspecies conservation of
RT 3' untranslated regions.";
RL Mol. Cell. Biol. 3:1738-1745(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA de Hostos E.L.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li Q., Liu L., Ma S.;
RT "Gene response of gangliocytes stimulated by Herpes simplex virus type
RT 1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, Eye, Kidney, Lung, Muscle, Placenta, Prostate,
RC Skin, 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 PROTEIN SEQUENCE OF 41-60; 65-79; 113-121; 230-280; 312-320; 327-336;
RP 340-370; 374-390; 395-401 AND 403-422, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 41-79; 65-79; 85-121; 125-164; 216-304; 312-370
RP AND 374-451, PHOSPHORYLATION AT SER-48 AND SER-232, METHYLATION AT
RP ARG-339, AND MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 353-370 AND 395-401.
RC TISSUE=Brain;
RX PubMed=8619814; DOI=10.1006/bbrc.1996.0211;
RA Baumann M.H., Wisniewski T., Levy E., Plant G.T., Ghiso J.;
RT "C-terminal fragments of alpha- and beta-tubulin form amyloid fibrils
RT in vitro and associate with amyloid deposits of familial cerebral
RT amyloid angiopathy, British type.";
RL Biochem. Biophys. Res. Commun. 219:238-242(1996).
RN [8]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC binds two moles of GTP, one at an exchangeable site on the beta
CC chain and one at a non-exchangeable site on the alpha chain.
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is
CC a hollow water-filled tube with an outer diameter of 25 nm and an
CC inner diameter of 15 nM. Alpha-beta heterodimers associate head-
CC to-tail to form protofilaments running lengthwise along the
CC microtubule wall with the beta-tubulin subunit facing the
CC microtubule plus end conferring a structural polarity.
CC Microtubules usually have 13 protofilaments but different
CC protofilament numbers can be found in some organisms and
CC specialized cells.
CC -!- INTERACTION:
CC Q13509:TUBB3; NbExp=3; IntAct=EBI-487083, EBI-350989;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic
CC removal and re-addition of a C-terminal tyrosine residue by the
CC enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin
CC tyrosine ligase (TTL), respectively (By similarity).
CC -!- PTM: Some glutamate residues at the C-terminus are
CC polyglutamylated. This modification occurs exclusively on
CC glutamate residues and results in polyglutamate chains on the
CC gamma-carboxyl group. Also monoglycylated but not polyglycylated
CC due to the absence of functional TTLL10 in human. Monoglycylation
CC is mainly limited to tubulin incorporated into axonemes (cilia and
CC flagella) whereas glutamylation is prevalent in neuronal cells,
CC centrioles, axonemes, and the mitotic spindle. Both modifications
CC can coexist on the same protein on adjacent residues, and lowering
CC glycylation levels increases polyglutamylation, and reciprocally.
CC The precise function of such modifications is still unclear but
CC they regulate the assembly and dynamics of axonemal microtubules
CC (Probable).
CC -!- PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules
CC and affects affinity and processivity of microtubule motors. This
CC modification has a role in multiple cellular functions, ranging
CC from cell motility, cell cycle progression or cell differentiation
CC to intracellular trafficking and signaling (By similarity).
CC -!- SIMILARITY: Belongs to the tubulin family.
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; K00558; AAA91576.1; -; mRNA.
DR EMBL; AF081484; AAC31959.1; -; mRNA.
DR EMBL; DQ400107; ABD60581.1; -; mRNA.
DR EMBL; BC000696; AAH00696.1; -; mRNA.
DR EMBL; BC001128; AAH01128.1; -; mRNA.
DR EMBL; BC006379; AAH06379.1; -; mRNA.
DR EMBL; BC006481; AAH06481.1; -; mRNA.
DR EMBL; BC008659; AAH08659.1; -; mRNA.
DR EMBL; BC009314; AAH09314.1; -; mRNA.
DR EMBL; BC009509; AAH09509.1; -; mRNA.
DR EMBL; BC009512; AAH09512.1; -; mRNA.
DR EMBL; BC009513; AAH09513.1; -; mRNA.
DR EMBL; BC010494; AAH10494.1; -; mRNA.
DR EMBL; BC011572; AAH11572.1; -; mRNA.
DR EMBL; BC015883; AAH15883.1; -; mRNA.
DR EMBL; BC017004; AAH17004.1; -; mRNA.
DR EMBL; BC030820; AAH30820.1; -; mRNA.
DR EMBL; BC071904; AAH71904.1; -; mRNA.
DR PIR; I77403; I77403.
DR RefSeq; NP_006073.2; NM_006082.2.
DR UniGene; Hs.524390; -.
DR PDB; 2E4H; NMR; -; B=416-451.
DR PDBsum; 2E4H; -.
DR ProteinModelPortal; P68363; -.
DR SMR; P68363; 1-440.
DR IntAct; P68363; 18.
DR MINT; MINT-4998849; -.
DR STRING; 9606.ENSP00000336799; -.
DR ChEMBL; CHEMBL2095182; -.
DR PhosphoSite; P68363; -.
DR DMDM; 55977474; -.
DR OGP; P68363; -.
DR SWISS-2DPAGE; P68363; -.
DR PaxDb; P68363; -.
DR PRIDE; P68363; -.
DR DNASU; 10376; -.
DR Ensembl; ENST00000336023; ENSP00000336799; ENSG00000123416.
DR GeneID; 10376; -.
DR KEGG; hsa:10376; -.
DR UCSC; uc001rtl.3; human.
DR CTD; 10376; -.
DR GeneCards; GC12M049523; -.
DR H-InvDB; HIX0079488; -.
DR HGNC; HGNC:18809; TUBA1B.
DR HPA; CAB011513; -.
DR HPA; HPA039247; -.
DR HPA; HPA043684; -.
DR MIM; 602530; gene.
DR neXtProt; NX_P68363; -.
DR PharmGKB; PA162407332; -.
DR eggNOG; COG5023; -.
DR HOGENOM; HOG000165711; -.
DR HOVERGEN; HBG000089; -.
DR InParanoid; P68363; -.
DR KO; K07374; -.
DR OMA; KRATHES; -.
DR OrthoDB; EOG7TBC1W; -.
DR PhylomeDB; P68363; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; TUBA1B; human.
DR EvolutionaryTrace; P68363; -.
DR GeneWiki; TUBA1B; -.
DR GenomeRNAi; 10376; -.
DR NextBio; 39315; -.
DR PRO; PR:P68363; -.
DR ArrayExpress; P68363; -.
DR Bgee; P68363; -.
DR CleanEx; HS_TUBA1B; -.
DR Genevestigator; P68363; -.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; TAS:BHF-UCL.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR GO; GO:0051301; P:cell division; TAS:BHF-UCL.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0007017; P:microtubule-based process; TAS:BHF-UCL.
DR GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002452; Alpha_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Isopeptide bond; Methylation;
KW Microtubule; Nitration; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1 451 Tubulin alpha-1B chain.
FT /FTId=PRO_0000048108.
FT NP_BIND 142 148 GTP (Potential).
FT SITE 451 451 Involved in polymerization.
FT MOD_RES 48 48 Phosphoserine.
FT MOD_RES 83 83 Nitrated tyrosine (By similarity).
FT MOD_RES 232 232 Phosphoserine.
FT MOD_RES 282 282 Nitrated tyrosine (By similarity).
FT MOD_RES 339 339 Omega-N-methylarginine.
FT MOD_RES 432 432 Phosphotyrosine (By similarity).
FT MOD_RES 439 439 Phosphoserine (By similarity).
FT CROSSLNK 326 326 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 370 370 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CONFLICT 131 131 G -> R (in Ref. 1; AAA91576).
FT CONFLICT 290 290 E -> D (in Ref. 1; AAA91576).
FT CONFLICT 308 308 R -> G (in Ref. 1; AAA91576).
FT CONFLICT 340 340 S -> T (in Ref. 1; AAA91576).
SQ SEQUENCE 451 AA; 50152 MW; 94355B4EC2086429 CRC64;
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y
//
MIM
602530
*RECORD*
*FIELD* NO
602530
*FIELD* TI
*602530 TUBULIN, ALPHA-1B; TUBA1B
;;TUBULIN, ALPHA, UBIQUITOUS;;
K-ALPHA-1
*FIELD* TX
read more
GENE FAMILY
See 602529 for general information about the alpha-tubulin gene family.
NOMENCLATURE
See Khodiyar et al. (2007) for a revised nomenclature of the
alpha-tubulin gene family.
CLONING
The human counterpart of the mouse tubulin gene M-alpha-2 is the
k-alpha-1 gene, cloned from a human keratinocyte cDNA library by Cowan
et al. (1983). The k-alpha-1 gene encodes a predicted 451-amino acid
protein that differs from the b-alpha-1 protein by only one amino acid.
By Northern blotting, k-alpha-1 mRNA was expressed in all tissues
tested.
By Northern blot analysis and in situ hybridization, Miller et al.
(1987) found that the rat homolog of k-alpha-1, which they called T26,
is expressed constitutively at a low level in most or all neural cell
types throughout development, with some enrichment in proliferative
zones.
MAPPING
Khodiyar et al. (2007) stated that the TUBA1B gene maps to human
chromosome 12q13.12 and mouse chromosome 15F1.
*FIELD* RF
1. Cowan, N. J.; Dobner, P. R.; Fuchs, E. V.; Cleveland, D. W.: Expression
of human alpha-tubulin genes: interspecies conservation of 3-prime
untranslated regions. Molec. Cell. Biol. 3: 1738-1745, 1983.
2. Khodiyar, V. K.; Maltais, L. J.; Ruef, B. J.; Sneddon, K. M. B.;
Smith, J. R.; Shimoyama, M.; Cabral, F.; Dumontet, C.; Dutcher, S.
K.; Harvey, R. J.; Lafanechere, L.; Murray, J. M.; Nogales, E.; Piquemal,
D.; Stanchi, F.; Povey, S.; Lovering, R. C.: A revised nomenclature
for the human and rodent alpha-tubulin gene family. Genomics 90:
285-289, 2007. Note: Erratum: Genomics 93: 397 only, 2009.
3. Miller, F. D.; Naus, C. C. G.; Durand, M.; Bloom, F. E.; Milner,
R. J.: Isotypes of alpha-tubulin are differentially regulated during
neuronal maturation. J. Cell Biol. 105: 3065-3073, 1987.
*FIELD* CD
Rebekah S. Rasooly: 4/16/1998
*FIELD* ED
terry: 11/28/2012
carol: 9/12/2007
carol: 9/11/2007
psherman: 4/20/1998
psherman: 4/16/1998
*RECORD*
*FIELD* NO
602530
*FIELD* TI
*602530 TUBULIN, ALPHA-1B; TUBA1B
;;TUBULIN, ALPHA, UBIQUITOUS;;
K-ALPHA-1
*FIELD* TX
read more
GENE FAMILY
See 602529 for general information about the alpha-tubulin gene family.
NOMENCLATURE
See Khodiyar et al. (2007) for a revised nomenclature of the
alpha-tubulin gene family.
CLONING
The human counterpart of the mouse tubulin gene M-alpha-2 is the
k-alpha-1 gene, cloned from a human keratinocyte cDNA library by Cowan
et al. (1983). The k-alpha-1 gene encodes a predicted 451-amino acid
protein that differs from the b-alpha-1 protein by only one amino acid.
By Northern blotting, k-alpha-1 mRNA was expressed in all tissues
tested.
By Northern blot analysis and in situ hybridization, Miller et al.
(1987) found that the rat homolog of k-alpha-1, which they called T26,
is expressed constitutively at a low level in most or all neural cell
types throughout development, with some enrichment in proliferative
zones.
MAPPING
Khodiyar et al. (2007) stated that the TUBA1B gene maps to human
chromosome 12q13.12 and mouse chromosome 15F1.
*FIELD* RF
1. Cowan, N. J.; Dobner, P. R.; Fuchs, E. V.; Cleveland, D. W.: Expression
of human alpha-tubulin genes: interspecies conservation of 3-prime
untranslated regions. Molec. Cell. Biol. 3: 1738-1745, 1983.
2. Khodiyar, V. K.; Maltais, L. J.; Ruef, B. J.; Sneddon, K. M. B.;
Smith, J. R.; Shimoyama, M.; Cabral, F.; Dumontet, C.; Dutcher, S.
K.; Harvey, R. J.; Lafanechere, L.; Murray, J. M.; Nogales, E.; Piquemal,
D.; Stanchi, F.; Povey, S.; Lovering, R. C.: A revised nomenclature
for the human and rodent alpha-tubulin gene family. Genomics 90:
285-289, 2007. Note: Erratum: Genomics 93: 397 only, 2009.
3. Miller, F. D.; Naus, C. C. G.; Durand, M.; Bloom, F. E.; Milner,
R. J.: Isotypes of alpha-tubulin are differentially regulated during
neuronal maturation. J. Cell Biol. 105: 3065-3073, 1987.
*FIELD* CD
Rebekah S. Rasooly: 4/16/1998
*FIELD* ED
terry: 11/28/2012
carol: 9/12/2007
carol: 9/11/2007
psherman: 4/20/1998
psherman: 4/16/1998