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UniProtKB - P02554 (TBB_PIG)

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Protein

Tubulin beta chain

Gene
N/A
Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -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.

Miscellaneous

The highly acidic C-terminal region may bind cations such as calcium.
Pig brain contains at least two forms of this protein.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 146GTPSequence analysis7

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

LigandGTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta chain
Alternative name(s):
Beta-tubulin
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2788

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000482611 – 445Tubulin beta chainAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineBy similarity1
Modified residuei58N6-acetyllysine; alternateBy similarity1
Modified residuei58N6-succinyllysine; alternateBy similarity1
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei172Phosphoserine; by CDK1By similarity1
Modified residuei285PhosphothreonineBy similarity1
Modified residuei290PhosphothreonineBy similarity1
Modified residuei318Omega-N-methylarginineBy similarity1
Cross-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei4385-glutamyl polyglutamateBy similarity1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation 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 polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.By similarity
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). 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).By similarity
Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP02554
PeptideAtlasiP02554
PRIDEiP02554

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. Interacts with NCKAP5L (PubMed:26482847).1 Publication

Protein-protein interaction databases

IntActiP02554, 2 interactors
STRINGi9823.ENSSSCP00000001076

Chemistry databases

BindingDBiP02554

Structurei

Secondary structure

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi10 – 28Combined sources19
Beta strandi34 – 36Combined sources3
Helixi41 – 43Combined sources3
Turni44 – 46Combined sources3
Helixi47 – 49Combined sources3
Beta strandi51 – 54Combined sources4
Turni55 – 57Combined sources3
Beta strandi58 – 61Combined sources4
Beta strandi63 – 70Combined sources8
Helixi71 – 78Combined sources8
Beta strandi79 – 81Combined sources3
Helixi82 – 84Combined sources3
Helixi87 – 89Combined sources3
Beta strandi90 – 92Combined sources3
Helixi101 – 105Combined sources5
Helixi108 – 125Combined sources18
Beta strandi132 – 142Combined sources11
Helixi143 – 158Combined sources16
Beta strandi162 – 170Combined sources9
Helixi173 – 175Combined sources3
Beta strandi177 – 180Combined sources4
Helixi181 – 195Combined sources15
Beta strandi197 – 203Combined sources7
Helixi204 – 212Combined sources9
Turni213 – 215Combined sources3
Helixi222 – 241Combined sources20
Beta strandi245 – 247Combined sources3
Helixi250 – 257Combined sources8
Beta strandi259 – 262Combined sources4
Beta strandi265 – 272Combined sources8
Beta strandi276 – 278Combined sources3
Beta strandi280 – 282Combined sources3
Helixi286 – 293Combined sources8
Helixi296 – 298Combined sources3
Beta strandi299 – 301Combined sources3
Helixi305 – 307Combined sources3
Beta strandi310 – 320Combined sources11
Helixi323 – 336Combined sources14
Helixi338 – 340Combined sources3
Beta strandi345 – 347Combined sources3
Beta strandi349 – 355Combined sources7
Beta strandi362 – 371Combined sources10
Helixi372 – 374Combined sources3
Helixi375 – 389Combined sources15
Turni390 – 395Combined sources6
Helixi396 – 399Combined sources4
Turni400 – 402Combined sources3
Helixi405 – 427Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFXX-ray3.95B/D1-445[»]
1IA0electron microscopy15.00B1-445[»]
1JFFX-ray3.50B1-445[»]
1TUBX-ray3.70B1-427[»]
2HXFelectron microscopy10.00B1-445[»]
2HXHelectron microscopy11.00B1-445[»]
3J6Eelectron microscopy4.70B/D/F/H/J/L/N/P/R1-427[»]
3J6Felectron microscopy4.90B/D/F/H/J/L/N/P/R1-427[»]
3J6Gelectron microscopy5.50B/D/F/H/J/L/N/P/R1-427[»]
3J6Helectron microscopy8.10B2-427[»]
3J6Pelectron microscopy8.20B1-445[»]
3J7Ielectron microscopy8.90B1-445[»]
3JAKelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JALelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JARelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JASelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JATelectron microscopy3.50B/D/F/G/H/I1-445[»]
3JAWelectron microscopy3.90B/D1-445[»]
4ABOelectron microscopy8.60A/C/E/G1-445[»]
4ZHQX-ray2.55B/D1-445[»]
4ZI7X-ray2.51B/D1-445[»]
4ZOLX-ray2.50B/D1-445[»]
5BMVX-ray2.50B/D1-445[»]
5FNVX-ray2.61B/D1-445[»]
5JCBX-ray2.30B/D1-445[»]
5JQGX-ray2.24B/D1-445[»]
5KMGelectron microscopy3.50B1-431[»]
5OAMelectron microscopy5.50B1-445[»]
5OCUelectron microscopy5.20B1-445[»]
5OGCelectron microscopy4.80B1-445[»]
5SYCelectron microscopy3.50B1-426[»]
5SYEelectron microscopy3.50B1-426[»]
5SYFelectron microscopy3.50B1-426[»]
5SYGelectron microscopy3.50B1-426[»]
5XP3X-ray2.30B/D1-445[»]
6BJCelectron microscopy3.30B/D/F/G/H/I1-445[»]
ProteinModelPortaliP02554
SMRiP02554
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02554

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
HOGENOMiHOG000165710
HOVERGENiHBG000089

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR013838 Beta-tubulin_BS
IPR002453 Beta_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PTHR11588:SF256 PTHR11588:SF256, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01163 BETATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit
PS00228 TUBULIN_B_AUTOREG, 1 hit

Sequencei

Sequence statusi: Complete.

P02554-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY 
        60         70         80         90        100
YNEAAGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN 
       110        120        130        140        150
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL 
       160        170        180        190        200
LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY 
       210        220        230        240        250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL 
       260        270        280        290        300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM 
       310        320        330        340        350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK 
       360        370        380        390        400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG 
       410        420        430        440 
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEG EEDEA
Length:445
Mass (Da):49,861
Last modified:July 21, 1986 - v1
Checksum:iEF71423B12C5E1B2
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti37H → V in 2nd form. 1
Natural varianti48N → S in 2nd form. 1
Natural varianti55 – 57AGN → SSH in 2nd form. 3
Natural varianti275S → A in 2nd form. 1

Sequence databases

PIRiA02973 UBPGB

Similar proteinsi

Entry informationi

Entry nameiTBB_PIG
AccessioniPrimary (citable) accession number: P02554
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 28, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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