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O94811 (TPPP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin polymerization-promoting protein

Short name=TPPP
Alternative name(s):
25 kDa brain-specific protein
TPPP/p25
p24
p25-alpha
Gene names
Name:TPPP
Synonyms:TPPP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7 Ref.8

Subunit structure

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. Ref.4 Ref.7 Ref.8

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Nucleus. Note: Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies. Ref.4 Ref.5 Ref.6

Tissue specificity

Widely expressed. Ref.1

Post-translational modification

Poor substrate for GSK3 By similarity. Phosphorylated by LIMK1 on serine residues. Phosphorylation may alter the tubulin polymerization activity. Ref.7 Ref.8

Miscellaneous

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

Sequence similarities

Belongs to the TPPP family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 219219Tubulin polymerization-promoting protein
PRO_0000221135

Regions

Region1 – 116116Mediates interaction with LIMK1

Amino acid modifications

Modified residue141Phosphothreonine; by CDK5; in vitro Ref.8 Ref.10
Modified residue181Phosphoserine; by CDK5 and MAPK1; in vitro Ref.8 Ref.10
Modified residue321Phosphoserine; by PKA; in vitro Ref.8 Ref.9 Ref.10 Ref.12
Modified residue351Phosphoserine Ref.10
Modified residue451Phosphoserine Ref.10
Modified residue921Phosphothreonine; by PKA; in vitro Ref.8
Modified residue1591Phosphoserine; by PKA; in vitro Ref.8
Modified residue1601Phosphoserine; by CDK5 and MAPK1; in vitro Ref.8
Glycosylation1521O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
O94811 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: F8B2C814EA59129A

FASTA21923,694
        10         20         30         40         50         60 
MADKAKPAKA ANRTPPKSPG DPSKDRAAKR LSLESEGAGE GAAASPELSA LEEAFRRFAV 

        70         80         90        100        110        120 
HGDARATGRE MHGKNWSKLC KDCQVIDGRN VTVTDVDIVF SKIKGKSCRT ITFEQFQEAL 

       130        140        150        160        170        180 
EELAKKRFKD KSSEEAVREV HRLIEGKAPI ISGVTKAISS PTVSRLTDTT KFTGSHKERF 

       190        200        210 
DPSGKGKGKA GRVDLVDESG YVSGYKHAGT YDQKVQGGK 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB017016 mRNA. Translation: BAA36164.1.
BT020035 mRNA. Translation: AAV38838.1.
BC040496 mRNA. Translation: AAH40496.1. Different initiation.
RefSeqNP_008961.1. NM_007030.2.
UniGeneHs.481466.

3D structure databases

ProteinModelPortalO94811.
SMRO94811. Positions 43-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116259. 4 interactions.
IntActO94811. 3 interactions.
MINTMINT-2798227.
STRING9606.ENSP00000353785.

Chemistry

BindingDBO94811.

PTM databases

PhosphoSiteO94811.

2D gel databases

UCD-2DPAGEO94811.

Proteomic databases

PaxDbO94811.
PRIDEO94811.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360578; ENSP00000353785; ENSG00000171368.
GeneID11076.
KEGGhsa:11076.
UCSCuc003jbg.4. human.

Organism-specific databases

CTD11076.
GeneCardsGC05M000659.
HGNCHGNC:24164. TPPP.
HPAHPA036575.
HPA036576.
MIM608773. gene.
neXtProtNX_O94811.
PharmGKBPA162406809.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271804.
HOGENOMHOG000260314.
HOVERGENHBG036683.
InParanoidO94811.
OMAIHGDTRA.
OrthoDBEOG7NGQDH.
PhylomeDBO94811.
TreeFamTF314440.

Gene expression databases

ArrayExpressO94811.
BgeeO94811.
CleanExHS_TPPP.
GenevestigatorO94811.

Family and domain databases

InterProIPR008907. P25-alpha.
[Graphical view]
PANTHERPTHR12932. PTHR12932. 1 hit.
PfamPF05517. p25-alpha. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTPPP.
GenomeRNAi11076.
NextBio42106.
PROO94811.
SOURCESearch...

Entry information

Entry nameTPPP_HUMAN
AccessionPrimary (citable) accession number: O94811
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM