A6NNZ2 (TBB8L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Tubulin beta-8 chain-like protein LOC260334
Organism	Homo sapiens (Human) [Reference proteome]
Taxonomic identifier	9606 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity.
Subunit structure	Dimer of alpha and beta chains By similarity.
Subcellular location	Cytoplasm › cytoskeleton By similarity.
Post-translational modification	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.
Sequence similarities	Belongs to the tubulin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	microtubule-based process Inferred from electronic annotation. Source: InterPro protein polymerization Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule cytoskeleton Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro structural constituent of cytoskeleton Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Tubulin beta-8 chain-like protein LOC260334		PRO_0000332739
Regions
	Nucleotide binding	140 – 146	7	GTP Potential
Amino acid modifications
	Modified residue	172	1	Phosphoserine; by CDK1 By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6NNZ2 [UniParc]. Last modified July 24, 2007. Version 1. Checksum: 3E7C6CEBDB11BE72	FASTA	444	49,573
	10 20 30 40 50 60 MREIVLTQTG QCGNQIGAKF WEVISDEHAI DSAGTYHGDS HLQLERINVH HHEASGGRYV 70 80 90 100 110 120 PRAVLVDLEP GTMDSVHSGP FGQVFRPDNF ISGQCGAGNN WAKGRYTEGA ELTESVMDVV 130 140 150 160 170 180 RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIINTFSIL PSPKVSDTVV 190 200 210 220 230 240 EPYNATLSVH QLIENADETF CIDNEALYDI CSRTLKLPTP TYGDLNHLVS ATMSGVTTCL 250 260 270 280 290 300 RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVAELT QQMFDAKNMM 310 320 330 340 350 360 AACDPRHGCY LTVAAIFRGR MPMREVDEQM FNIQDKNSSY FADWFPDNVK TAVCDIPPRG 370 380 390 400 410 420 LKMSATFIGN NAAIQELFTC VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 430 440 EYQQYQDATA EEEEDEEYAE EEVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"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(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCYLATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP001005 Genomic DNA. No translation available.
IPI	IPI00174849.
3D structure databases
ProteinModelPortal	A6NNZ2.
ModBase	Search...
Protein-protein interaction databases
IntAct	A6NNZ2. 1 interaction.
Proteomic databases
PaxDb	A6NNZ2.
PRIDE	A6NNZ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
H-InvDB	HIX0034873. HIX0200674.
HPA	HPA043640. HPA046280.
neXtProt	NX_A6NNZ2.
Phylogenomic databases
eggNOG	COG5023.
HOGENOM	HOG000165710.
HOVERGEN	HBG000089.
InParanoid	A6NNZ2.
OMA	ERINVHH.
OrthoDB	EOG48SGT2.
PhylomeDB	A6NNZ2.
Gene expression databases
ArrayExpress	A6NNZ2.
Bgee	A6NNZ2.
Genevestigator	A6NNZ2.
Family and domain databases
Gene3D	1.10.287.600. 1 hit. 3.30.1330.20. 1 hit. 3.40.50.1440. 1 hit.
InterPro	IPR013838. Beta-tubulin_BS. IPR002453. Beta_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]
PANTHER	PTHR11588. PTHR11588. 1 hit.
Pfam	PF00091. Tubulin. 1 hit. PF03953. Tubulin_C. 1 hit. [Graphical view]
PRINTS	PR01163. BETATUBULIN. PR01161. TUBULIN.
SMART	SM00864. Tubulin. 1 hit. SM00865. Tubulin_C. 1 hit. [Graphical view]
SUPFAM	SSF55307. Tub_FtsZ_C. 1 hit. SSF52490. Tubulin_FtsZ. 1 hit.
PROSITE	PS00227. TUBULIN. 1 hit. PS00228. TUBULIN_B_AUTOREG. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	35462716.

Entry information

Entry name

TBB8L_HUMAN

Accession

Primary (citable) accession number: A6NNZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	July 24, 2007
Last modified:	May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.