Full text data of TUBA1C
TUBA1C
(TUBA6)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Tubulin alpha-1C chain (Alpha-tubulin 6; Tubulin alpha-6 chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tubulin alpha-1C chain (Alpha-tubulin 6; Tubulin alpha-6 chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00218343
IPI00218343 Tubulin alpha-6 chain Tubulin alpha-6 chain membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoskeleton match also tubulin alpha 1 chain found at its expected molecular weight found at molecular weight
IPI00218343 Tubulin alpha-6 chain Tubulin alpha-6 chain membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoskeleton match also tubulin alpha 1 chain found at its expected molecular weight found at molecular weight
UniProt
Q9BQE3
ID TBA1C_HUMAN Reviewed; 449 AA.
AC Q9BQE3;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Tubulin alpha-1C chain;
DE AltName: Full=Alpha-tubulin 6;
DE AltName: Full=Tubulin alpha-6 chain;
GN Name=TUBA1C; Synonyms=TUBA6;
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 [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Duodenum, Lymph, and Skin;
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 [2]
RP PROTEIN SEQUENCE OF 65-79 AND 244-280, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-432 AND SER-439, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
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 -!- 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; BC004949; AAH04949.1; -; mRNA.
DR EMBL; BC005946; AAH05946.1; -; mRNA.
DR EMBL; BC011790; AAH11790.1; -; mRNA.
DR EMBL; BC019298; AAH19298.1; -; mRNA.
DR EMBL; BC021088; AAH21088.1; -; mRNA.
DR EMBL; BC051297; AAH51297.1; -; mRNA.
DR EMBL; BC063036; AAH63036.1; -; mRNA.
DR RefSeq; NP_116093.1; NM_032704.3.
DR UniGene; Hs.652390; -.
DR ProteinModelPortal; Q9BQE3; -.
DR SMR; Q9BQE3; 1-439.
DR IntAct; Q9BQE3; 42.
DR MINT; MINT-3060519; -.
DR STRING; 9606.ENSP00000301072; -.
DR ChEMBL; CHEMBL2095182; -.
DR PhosphoSite; Q9BQE3; -.
DR DMDM; 20455322; -.
DR REPRODUCTION-2DPAGE; Q9BQE3; -.
DR PRIDE; Q9BQE3; -.
DR DNASU; 84790; -.
DR Ensembl; ENST00000301072; ENSP00000301072; ENSG00000167553.
DR GeneID; 84790; -.
DR KEGG; hsa:84790; -.
DR UCSC; uc001rtt.1; human.
DR CTD; 84790; -.
DR GeneCards; GC12P049658; -.
DR HGNC; HGNC:20768; TUBA1C.
DR HPA; HPA039247; -.
DR HPA; HPA043684; -.
DR neXtProt; NX_Q9BQE3; -.
DR PharmGKB; PA162407345; -.
DR HOVERGEN; HBG000089; -.
DR InParanoid; Q9BQE3; -.
DR KO; K07374; -.
DR PhylomeDB; Q9BQE3; -.
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; TUBA1C; human.
DR GeneWiki; TUBA1C; -.
DR GenomeRNAi; 84790; -.
DR NextBio; 74948; -.
DR PMAP-CutDB; Q9BQE3; -.
DR PRO; PR:Q9BQE3; -.
DR ArrayExpress; Q9BQE3; -.
DR Bgee; Q9BQE3; -.
DR CleanEx; HS_TUBA1C; -.
DR Genevestigator; Q9BQE3; -.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; TAS:BHF-UCL.
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:InterPro.
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:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL.
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 Acetylation; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Microtubule; Nitration;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1 449 Tubulin alpha-1C chain.
FT /FTId=PRO_0000048112.
FT NP_BIND 142 148 GTP (Potential).
FT SITE 449 449 Involved in polymerization.
FT MOD_RES 48 48 Phosphoserine (By similarity).
FT MOD_RES 83 83 Nitrated tyrosine (By similarity).
FT MOD_RES 282 282 Nitrated tyrosine (By similarity).
FT MOD_RES 432 432 Phosphotyrosine.
FT MOD_RES 439 439 Phosphoserine.
SQ SEQUENCE 449 AA; 49895 MW; 0CFE7212CB5E14F9 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 AYHEQLTVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAVAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGADSA DGEDEGEEY
//
ID TBA1C_HUMAN Reviewed; 449 AA.
AC Q9BQE3;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Tubulin alpha-1C chain;
DE AltName: Full=Alpha-tubulin 6;
DE AltName: Full=Tubulin alpha-6 chain;
GN Name=TUBA1C; Synonyms=TUBA6;
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 [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Duodenum, Lymph, and Skin;
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 [2]
RP PROTEIN SEQUENCE OF 65-79 AND 244-280, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-432 AND SER-439, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
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 -!- 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; BC004949; AAH04949.1; -; mRNA.
DR EMBL; BC005946; AAH05946.1; -; mRNA.
DR EMBL; BC011790; AAH11790.1; -; mRNA.
DR EMBL; BC019298; AAH19298.1; -; mRNA.
DR EMBL; BC021088; AAH21088.1; -; mRNA.
DR EMBL; BC051297; AAH51297.1; -; mRNA.
DR EMBL; BC063036; AAH63036.1; -; mRNA.
DR RefSeq; NP_116093.1; NM_032704.3.
DR UniGene; Hs.652390; -.
DR ProteinModelPortal; Q9BQE3; -.
DR SMR; Q9BQE3; 1-439.
DR IntAct; Q9BQE3; 42.
DR MINT; MINT-3060519; -.
DR STRING; 9606.ENSP00000301072; -.
DR ChEMBL; CHEMBL2095182; -.
DR PhosphoSite; Q9BQE3; -.
DR DMDM; 20455322; -.
DR REPRODUCTION-2DPAGE; Q9BQE3; -.
DR PRIDE; Q9BQE3; -.
DR DNASU; 84790; -.
DR Ensembl; ENST00000301072; ENSP00000301072; ENSG00000167553.
DR GeneID; 84790; -.
DR KEGG; hsa:84790; -.
DR UCSC; uc001rtt.1; human.
DR CTD; 84790; -.
DR GeneCards; GC12P049658; -.
DR HGNC; HGNC:20768; TUBA1C.
DR HPA; HPA039247; -.
DR HPA; HPA043684; -.
DR neXtProt; NX_Q9BQE3; -.
DR PharmGKB; PA162407345; -.
DR HOVERGEN; HBG000089; -.
DR InParanoid; Q9BQE3; -.
DR KO; K07374; -.
DR PhylomeDB; Q9BQE3; -.
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; TUBA1C; human.
DR GeneWiki; TUBA1C; -.
DR GenomeRNAi; 84790; -.
DR NextBio; 74948; -.
DR PMAP-CutDB; Q9BQE3; -.
DR PRO; PR:Q9BQE3; -.
DR ArrayExpress; Q9BQE3; -.
DR Bgee; Q9BQE3; -.
DR CleanEx; HS_TUBA1C; -.
DR Genevestigator; Q9BQE3; -.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; TAS:BHF-UCL.
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:InterPro.
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:0030705; P:cytoskeleton-dependent intracellular transport; TAS:BHF-UCL.
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 Acetylation; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; GTP-binding; Microtubule; Nitration;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1 449 Tubulin alpha-1C chain.
FT /FTId=PRO_0000048112.
FT NP_BIND 142 148 GTP (Potential).
FT SITE 449 449 Involved in polymerization.
FT MOD_RES 48 48 Phosphoserine (By similarity).
FT MOD_RES 83 83 Nitrated tyrosine (By similarity).
FT MOD_RES 282 282 Nitrated tyrosine (By similarity).
FT MOD_RES 432 432 Phosphotyrosine.
FT MOD_RES 439 439 Phosphoserine.
SQ SEQUENCE 449 AA; 49895 MW; 0CFE7212CB5E14F9 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 AYHEQLTVAE ITNACFEPAN
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP
TVVPGGDLAK VQRAVCMLSN TTAVAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
AREDMAALEK DYEEVGADSA DGEDEGEEY
//