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Protein

Tubulin alpha-4A chain

Gene

TUBA4A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: Reactome
  2. blood coagulation Source: Reactome
  3. cellular protein metabolic process Source: Reactome
  4. G2/M transition of mitotic cell cycle Source: Reactome
  5. microtubule-based process Source: InterPro
  6. mitotic cell cycle Source: Reactome
  7. organelle organization Source: Reactome
  8. platelet activation Source: Reactome
  9. platelet degranulation Source: Reactome
  10. protein folding Source: Reactome
  11. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_267965. Anchoring of the basal body to the plasma membrane.
REACT_268024. Intraflagellar transport.
REACT_268265. Assembly of the primary cilium.
REACT_268323. Hedgehog 'off' state.
REACT_318. Platelet degranulation.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-4A chain
Alternative name(s):
Alpha-tubulin 1
Testis-specific alpha-tubulin
Tubulin H2-alpha
Tubulin alpha-1 chain
Gene namesi
Name:TUBA4A
Synonyms:TUBA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12407. TUBA4A.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular region Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162407391.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Tubulin alpha-4A chainPRO_0000048106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481Phosphoserine1 Publication
Modified residuei83 – 831Nitrated tyrosineBy similarity
Modified residuei282 – 2821Nitrated tyrosineBy similarity
Modified residuei432 – 4321PhosphotyrosineBy similarity
Modified residuei439 – 4391PhosphoserineBy similarity

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable).1 Publication
Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity).By similarity

Keywords - PTMi

Acetylation, Nitration, Phosphoprotein

Proteomic databases

MaxQBiP68366.
PRIDEiP68366.

2D gel databases

DOSAC-COBS-2DPAGEP68366.
OGPiP05215.

PTM databases

PhosphoSiteiP68366.

Miscellaneous databases

PMAP-CutDBP68366.

Expressioni

Gene expression databases

BgeeiP68366.
CleanExiHS_TUBA4A.
ExpressionAtlasiP68366. baseline and differential.
GenevestigatoriP68366.

Organism-specific databases

HPAiCAB004621.
CAB005887.
HPA039247.
HPA043684.
HPA063394.

Interactioni

Subunit structurei

Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.

Binary interactionsi

WithEntry#Exp.IntActNotes
CLIP1P306223EBI-351772,EBI-2683569

Protein-protein interaction databases

BioGridi113128. 103 interactions.
IntActiP68366. 38 interactions.
MINTiMINT-1394538.
STRINGi9606.ENSP00000248437.

Structurei

3D structure databases

ProteinModelPortaliP68366.
SMRiP68366. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP68366.
KOiK07374.
OMAiSEGREDM.
OrthoDBiEOG7TBC1W.
PhylomeDBiP68366.
TreeFamiTF300314.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P68366-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRECISVHVG QAGVQMGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFT
60 70 80 90 100
TFFCETGAGK HVPRAVFVDL EPTVIDEIRN GPYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTI GKEIIDPVLD RIRKLSDQCT GLQGFLVFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSVD YGKKSKLEFS IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
310 320 330 340 350
QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAAIKTKRS IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440
KRAFVHWYVG EGMEEGEFSE AREDMAALEK DYEEVGIDSY EDEDEGEE
Length:448
Mass (Da):49,924
Last modified:August 13, 1987 - v1
Checksum:iC00ED90A183FE8F2
GO
Isoform 2 (identifier: P68366-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: Missing.

Show »
Length:433
Mass (Da):48,329
Checksum:i0448FC0BE3F4872A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515Missing in isoform 2. 1 PublicationVSP_055194Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06956 Genomic DNA. Translation: CAA30026.1.
BT006731 mRNA. Translation: AAP35377.1.
AK054731 mRNA. Translation: BAG51418.1.
AK299958 mRNA. Translation: BAH13182.1.
AY895018 Genomic DNA. Translation: AAW65371.1.
AC068946 Genomic DNA. No translation available.
AC114803 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70718.1.
CH471063 Genomic DNA. Translation: EAW70719.1.
BC009238 mRNA. Translation: AAH09238.1.
CCDSiCCDS2438.1. [P68366-1]
CCDS63131.1. [P68366-2]
PIRiA25873.
RefSeqiNP_001265481.1. NM_001278552.1. [P68366-2]
NP_005991.1. NM_006000.2. [P68366-1]
XP_005246889.1. XM_005246832.1. [P68366-2]
UniGeneiHs.75318.

Genome annotation databases

EnsembliENST00000248437; ENSP00000248437; ENSG00000127824. [P68366-1]
ENST00000392088; ENSP00000375938; ENSG00000127824. [P68366-2]
GeneIDi7277.
KEGGihsa:7277.
UCSCiuc002vkt.1. human. [P68366-1]

Polymorphism databases

DMDMi55977476.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Tubulin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06956 Genomic DNA. Translation: CAA30026.1.
BT006731 mRNA. Translation: AAP35377.1.
AK054731 mRNA. Translation: BAG51418.1.
AK299958 mRNA. Translation: BAH13182.1.
AY895018 Genomic DNA. Translation: AAW65371.1.
AC068946 Genomic DNA. No translation available.
AC114803 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70718.1.
CH471063 Genomic DNA. Translation: EAW70719.1.
BC009238 mRNA. Translation: AAH09238.1.
CCDSiCCDS2438.1. [P68366-1]
CCDS63131.1. [P68366-2]
PIRiA25873.
RefSeqiNP_001265481.1. NM_001278552.1. [P68366-2]
NP_005991.1. NM_006000.2. [P68366-1]
XP_005246889.1. XM_005246832.1. [P68366-2]
UniGeneiHs.75318.

3D structure databases

ProteinModelPortaliP68366.
SMRiP68366. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113128. 103 interactions.
IntActiP68366. 38 interactions.
MINTiMINT-1394538.
STRINGi9606.ENSP00000248437.

Chemistry

ChEMBLiCHEMBL2095182.
DrugBankiDB06772. Cabazitaxel.
DB01179. Podofilox.
DB00541. Vincristine.

PTM databases

PhosphoSiteiP68366.

Polymorphism databases

DMDMi55977476.

2D gel databases

DOSAC-COBS-2DPAGEP68366.
OGPiP05215.

Proteomic databases

MaxQBiP68366.
PRIDEiP68366.

Protocols and materials databases

DNASUi7277.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248437; ENSP00000248437; ENSG00000127824. [P68366-1]
ENST00000392088; ENSP00000375938; ENSG00000127824. [P68366-2]
GeneIDi7277.
KEGGihsa:7277.
UCSCiuc002vkt.1. human. [P68366-1]

Organism-specific databases

CTDi7277.
GeneCardsiGC02M220114.
HGNCiHGNC:12407. TUBA4A.
HPAiCAB004621.
CAB005887.
HPA039247.
HPA043684.
HPA063394.
MIMi191110. gene.
neXtProtiNX_P68366.
PharmGKBiPA162407391.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiP68366.
KOiK07374.
OMAiSEGREDM.
OrthoDBiEOG7TBC1W.
PhylomeDBiP68366.
TreeFamiTF300314.

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_267965. Anchoring of the basal body to the plasma membrane.
REACT_268024. Intraflagellar transport.
REACT_268265. Assembly of the primary cilium.
REACT_268323. Hedgehog 'off' state.
REACT_318. Platelet degranulation.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Miscellaneous databases

ChiTaRSiTUBA4A. human.
GeneWikiiTUBA4A.
GenomeRNAii7277.
NextBioi28459.
PMAP-CutDBP68366.
PROiP68366.
SOURCEiSearch...

Gene expression databases

BgeeiP68366.
CleanExiHS_TUBA4A.
ExpressionAtlasiP68366. baseline and differential.
GenevestigatoriP68366.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Alternative 5' exons either provide or deny an initiator methionine codon to the same alpha-tubulin coding region."
    Dobner P.R., Kislauskis E., Wentworth B.M., Villa-Komaroff L.
    Nucleic Acids Res. 15:199-218(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Cerebellum.
  4. NIEHS SNPs program
    Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  8. Bienvenut W.V., Claeys D.
    Submitted (OCT-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-164; 216-280; 327-336; 340-370; 391-401 AND 403-430, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
    Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
    Cell 137:1076-1087(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCYLATION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTBA4A_HUMAN
AccessioniPrimary (citable) accession number: P68366
Secondary accession number(s): A8MUB1, B3KNQ6, P05215
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 1, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

This tubulin does not have a C-terminal tyrosine.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.