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Protein

Tubulin polymerization-promoting protein

Gene

TPPP

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

Functioni

May play a role in the polymerization of tubulin into microtubules, microtubule bundling and the stabilization of existing microtubules, thus maintaining the integrity of the microtubule network. May play a role in mitotic spindle assembly and nuclear envelope breakdown.3 Publications

GO - Molecular functioni

  1. microtubule binding Source: HGNC
  2. tubulin binding Source: UniProtKB

GO - Biological processi

  1. microtubule bundle formation Source: UniProtKB
  2. microtubule polymerization Source: UniProtKB
  3. positive regulation of protein complex assembly Source: HGNC
  4. positive regulation of protein polymerization Source: HGNC
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin polymerization-promoting protein
Short name:
TPPP
Alternative name(s):
25 kDa brain-specific protein
TPPP/p25
p24
p25-alpha
Gene namesi
Name:TPPP
Synonyms:TPPP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:24164. TPPP.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeleton. Nucleus
Note: Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. microtubule Source: Ensembl
  3. nucleus Source: UniProtKB
  4. perinuclear region of cytoplasm Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162406809.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219Tubulin polymerization-promoting proteinPRO_0000221135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphothreonine; by CDK5; in vitro2 Publications
Modified residuei18 – 181Phosphoserine; by CDK5 and MAPK1; in vitro2 Publications
Modified residuei32 – 321Phosphoserine; by PKA; in vitro4 Publications
Modified residuei35 – 351Phosphoserine1 Publication
Modified residuei45 – 451Phosphoserine1 Publication
Modified residuei92 – 921Phosphothreonine; by PKA; in vitro1 Publication
Glycosylationi152 – 1521O-linked (GlcNAc)By similarity
Modified residuei159 – 1591Phosphoserine; by PKA; in vitro1 Publication
Modified residuei160 – 1601Phosphoserine; by CDK5 and MAPK1; in vitro1 Publication

Post-translational modificationi

Poor substrate for GSK3 (By similarity). Phosphorylated by LIMK1 on serine residues. Phosphorylation may alter the tubulin polymerization activity.By similarity5 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO94811.
PaxDbiO94811.
PRIDEiO94811.

2D gel databases

UCD-2DPAGEO94811.

PTM databases

PhosphoSiteiO94811.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiO94811.
CleanExiHS_TPPP.
ExpressionAtlasiO94811. baseline and differential.
GenevestigatoriO94811.

Organism-specific databases

HPAiHPA036575.
HPA036576.

Interactioni

Subunit structurei

Homodimer. Binds tubulin; binding is inhibited by GTP (By similarity). Interacts with GSK3 (By similarity). Interacts with MAPK1 (By similarity). Interacts with GAPDH; the interaction is direct (By similarity). Interacts with LIMK1 (via the PDZ domain); the interaction is direct.By similarity2 Publications

Protein-protein interaction databases

BioGridi116259. 6 interactions.
IntActiO94811. 3 interactions.
MINTiMINT-2798227.
STRINGi9606.ENSP00000353785.

Structurei

3D structure databases

ProteinModelPortaliO94811.
SMRiO94811. Positions 43-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 116116Mediates interaction with LIMK1Add
BLAST

Sequence similaritiesi

Belongs to the TPPP family.Curated

Phylogenomic databases

eggNOGiNOG271804.
HOGENOMiHOG000260314.
HOVERGENiHBG036683.
InParanoidiO94811.
OMAiIHGDTRA.
OrthoDBiEOG7NGQDH.
PhylomeDBiO94811.
TreeFamiTF314440.

Family and domain databases

InterProiIPR008907. P25-alpha.
[Graphical view]
PANTHERiPTHR12932. PTHR12932. 1 hit.
PfamiPF05517. p25-alpha. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O94811-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADKAKPAKA ANRTPPKSPG DPSKDRAAKR LSLESEGAGE GAAASPELSA
60 70 80 90 100
LEEAFRRFAV HGDARATGRE MHGKNWSKLC KDCQVIDGRN VTVTDVDIVF
110 120 130 140 150
SKIKGKSCRT ITFEQFQEAL EELAKKRFKD KSSEEAVREV HRLIEGKAPI
160 170 180 190 200
ISGVTKAISS PTVSRLTDTT KFTGSHKERF DPSGKGKGKA GRVDLVDESG
210
YVSGYKHAGT YDQKVQGGK
Length:219
Mass (Da):23,694
Last modified:May 1, 1999 - v1
Checksum:iF8B2C814EA59129A
GO

Sequence cautioni

The sequence AAH40496.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017016 mRNA. Translation: BAA36164.1.
BT020035 mRNA. Translation: AAV38838.1.
BC040496 mRNA. Translation: AAH40496.1. Different initiation.
CCDSiCCDS3856.1.
RefSeqiNP_008961.1. NM_007030.2.
UniGeneiHs.481466.

Genome annotation databases

EnsembliENST00000360578; ENSP00000353785; ENSG00000171368.
GeneIDi11076.
KEGGihsa:11076.
UCSCiuc003jbg.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017016 mRNA. Translation: BAA36164.1.
BT020035 mRNA. Translation: AAV38838.1.
BC040496 mRNA. Translation: AAH40496.1. Different initiation.
CCDSiCCDS3856.1.
RefSeqiNP_008961.1. NM_007030.2.
UniGeneiHs.481466.

3D structure databases

ProteinModelPortaliO94811.
SMRiO94811. Positions 43-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116259. 6 interactions.
IntActiO94811. 3 interactions.
MINTiMINT-2798227.
STRINGi9606.ENSP00000353785.

Chemistry

BindingDBiO94811.

PTM databases

PhosphoSiteiO94811.

2D gel databases

UCD-2DPAGEO94811.

Proteomic databases

MaxQBiO94811.
PaxDbiO94811.
PRIDEiO94811.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360578; ENSP00000353785; ENSG00000171368.
GeneIDi11076.
KEGGihsa:11076.
UCSCiuc003jbg.4. human.

Organism-specific databases

CTDi11076.
GeneCardsiGC05M000659.
HGNCiHGNC:24164. TPPP.
HPAiHPA036575.
HPA036576.
MIMi608773. gene.
neXtProtiNX_O94811.
PharmGKBiPA162406809.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG271804.
HOGENOMiHOG000260314.
HOVERGENiHBG036683.
InParanoidiO94811.
OMAiIHGDTRA.
OrthoDBiEOG7NGQDH.
PhylomeDBiO94811.
TreeFamiTF314440.

Miscellaneous databases

GeneWikiiTPPP.
GenomeRNAii11076.
NextBioi42106.
PROiO94811.
SOURCEiSearch...

Gene expression databases

BgeeiO94811.
CleanExiHS_TPPP.
ExpressionAtlasiO94811. baseline and differential.
GenevestigatoriO94811.

Family and domain databases

InterProiIPR008907. P25-alpha.
[Graphical view]
PANTHERiPTHR12932. PTHR12932. 1 hit.
PfamiPF05517. p25-alpha. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel human gene whose product shares significant homology with the bovine brain-specific protein p25 on chromosome 5p15.3."
    Seki N., Hattori A., Sugano S., Suzuki Y., Nakagawara A., Muramatsu M.-A., Hori T.-A., Saito T.
    J. Hum. Genet. 44:121-122(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Neuroblastoma.
  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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "p25alpha Stimulates alpha-synuclein aggregation and is co-localized with aggregated alpha-synuclein in alpha-synucleinopathies."
    Lindersson E., Lundvig D., Petersen C., Madsen P., Nyengaard J.R., Hoejrup P., Moos T., Otzen D., Gai W.-P., Blumbergs P.C., Jensen P.H.
    J. Biol. Chem. 280:5703-5715(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AGGREGATED SNCA, SUBCELLULAR LOCATION.
  5. "Tubulin polymerization promoting proteins (TPPPs): members of a new family with distinct structures and functions."
    Vincze O., Toekesi N., Olah J., Hlavanda E., Zotter A., Horvath I., Lehotzky A., Tirian L., Medzihradszky K.F., Kovacs J., Orosz F., Ovadi J.
    Biochemistry 45:13818-13826(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Interaction of TPPP/p25 protein with glyceraldehyde-3-phosphate dehydrogenase and their co-localization in Lewy bodies."
    Olah J., Toekesi N., Vincze O., Horvath I., Lehotzky A., Erdei A., Szajli E., Medzihradszky K.F., Orosz F., Kovacs G.G., Ovadi J.
    FEBS Lett. 580:5807-5814(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "The phosphorylation of p25/TPPP by LIM kinase 1 inhibits its ability to assemble microtubules."
    Acevedo K., Li R., Soo P., Suryadinata R., Sarcevic B., Valova V.A., Graham M.E., Robinson P.J., Bernard O.
    Exp. Cell Res. 313:4091-4106(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LIMK1, PHOSPHORYLATION.
  8. "Phosphorylation blocks the activity of tubulin polymerization-promoting protein (TPPP): identification of sites targeted by different kinases."
    Hlavanda E., Klement E., Kokai E., Kovacs J., Vincze O., Toekesi N., Orosz F., Medzihradszky K.F., Dombradi V., Ovadi J.
    J. Biol. Chem. 282:29531-29539(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMERIZATION, PHOSPHORYLATION AT THR-14; SER-18; SER-32; THR-92; SER-159 AND SER-160.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-18; SER-32; SER-35 AND SER-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiTPPP_HUMAN
AccessioniPrimary (citable) accession number: O94811
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 108 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

Unstructured protein. Interacts with aggregated SNCA and may have a pro-aggregatory role in synucleinopathies.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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.