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Protein

Putative tubulin-like protein alpha-4B

Gene

TUBA4B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein uncertaini

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi81 – 877GTPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-190840. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
R-HSA-190861. Gap junction assembly.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-389977. Post-chaperonin tubulin folding pathway.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5617833. Assembly of the primary cilium.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-983189. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative tubulin-like protein alpha-4B
Alternative name(s):
Alpha-tubulin 4B
Gene namesi
Name:TUBA4B
Synonyms:TUBA4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:18637. TUBA4B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi187663995.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Putative tubulin-like protein alpha-4BPRO_0000331573Add
BLAST

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold.By similarity
Some glutamate residues at the C-terminus are 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). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear.By similarity

Proteomic databases

EPDiQ9H853.
PRIDEiQ9H853.

PTM databases

iPTMnetiQ9H853.
PhosphoSiteiQ9H853.

Expressioni

Gene expression databases

GenevisibleiQ9H853. HS.

Interactioni

Protein-protein interaction databases

IntActiQ9H853. 2 interactions.
MINTiMINT-1149454.

Structurei

3D structure databases

ProteinModelPortaliQ9H853.
SMRiQ9H853. Positions 20-201.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119060.
HOVERGENiHBG000089.
InParanoidiQ9H853.
PhylomeDBiQ9H853.

Family and domain databases

Gene3Di3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_tubulin.
IPR000217. Tubulin.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9H853-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHQQTERQD PSQPLSRQHG TYRQIFHPEQ LITGKEDAAN NYAWGHYTIG
60 70 80 90 100
KEFIDLLLDR IRKLADQCTG LQGFLVFHSL GRGTGSDVTS FLMEWLSVNY
110 120 130 140 150
GKKSKLGFSI YPAPQVSTAM VQPYNSILTT HTTLEHSDCA FMVDNKAIYD
160 170 180 190 200
ICHCNLDIER PTYTNLNRLI SQIVSSITAS LRFDGALNVD LTEFQTNLVS
210 220 230 240
YLTSTSPWPP MHQSSLQKRY TTSSCWWQRL PMPALSLPTR W
Length:241
Mass (Da):27,551
Last modified:April 29, 2008 - v2
Checksum:i2CC581FEF7BF53BA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541C → R in BAB14767 (PubMed:14702039).Curated
Sequence conflicti219 – 2191R → K in BAB14767 (PubMed:14702039).Curated
Sequence conflicti226 – 2261W → R in BAB14767 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024002 mRNA. Translation: BAB14767.1.
AC068946 Genomic DNA. No translation available.
UniGeneiHs.664469.

Genome annotation databases

EnsembliENST00000490341; ENSP00000487719; ENSG00000243910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024002 mRNA. Translation: BAB14767.1.
AC068946 Genomic DNA. No translation available.
UniGeneiHs.664469.

3D structure databases

ProteinModelPortaliQ9H853.
SMRiQ9H853. Positions 20-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9H853. 2 interactions.
MINTiMINT-1149454.

PTM databases

iPTMnetiQ9H853.
PhosphoSiteiQ9H853.

Polymorphism and mutation databases

DMDMi187663995.

Proteomic databases

EPDiQ9H853.
PRIDEiQ9H853.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000490341; ENSP00000487719; ENSG00000243910.

Organism-specific databases

GeneCardsiTUBA4B.
HGNCiHGNC:18637. TUBA4B.
neXtProtiNX_Q9H853.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119060.
HOVERGENiHBG000089.
InParanoidiQ9H853.
PhylomeDBiQ9H853.

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-190840. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
R-HSA-190861. Gap junction assembly.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-389977. Post-chaperonin tubulin folding pathway.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5617833. Assembly of the primary cilium.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-983189. Kinesins.

Gene expression databases

GenevisibleiQ9H853. HS.

Family and domain databases

Gene3Di3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_tubulin.
IPR000217. Tubulin.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
[Graphical view]
PRINTSiPR01162. ALPHATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiTBA4B_HUMAN
AccessioniPrimary (citable) accession number: Q9H853
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: May 11, 2016
This is version 96 of the entry and version 2 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

Caution

Could be the product of a pseudogene.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.