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Entry version 150 (17 Jun 2020)
Sequence version 1 (01 May 1999)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath (PubMed:31522887). Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath (PubMed:31522887). Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes (PubMed:31522887). Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (PubMed:21995432, PubMed:21316364). In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network (PubMed:17105200, PubMed:17693641, PubMed:18028908, PubMed:26289831). Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (PubMed:20308065, PubMed:23093407). Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in increased acetylation of tubulin and increased cell motility (PubMed:23093407). Plays a role in cell proliferation by regulating the G1/S-phase transition (PubMed:23355470). Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (PubMed:22328514).11 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 0.018 min(-1) for GTP.1 Publication

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi61Zinc1 Publication1
      Metal bindingi72Zinc1 Publication1
      Metal bindingi80Zinc1 Publication1
      Metal bindingi83Zinc1 Publication1

      <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

      GO - Biological processi

      <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

      Molecular functionHydrolase
      Biological processCell cycle, Cell division, Mitosis
      LigandMagnesium, Metal-binding, Zinc

      <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
      Recommended name:
      Tubulin polymerization-promoting protein1 Publication (EC:3.6.5.-2 Publications)
      Short name:
      TPPP1 Publication
      Alternative name(s):
      25 kDa brain-specific protein1 Publication
      TPPP/p251 Publication
      p24
      p25-alpha1 Publication
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
      Name:TPPP1 PublicationImported
      Synonyms:TPPP1
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
      • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

      Organism-specific databases

      Eukaryotic Pathogen Database Resources

      More...
      EuPathDBi
      HostDB:ENSG00000171368.11

      Human Gene Nomenclature Database

      More...
      HGNCi
      HGNC:24164 TPPP

      Online Mendelian Inheritance in Man (OMIM)

      More...
      MIMi
      608773 gene

      neXtProt; the human protein knowledge platform

      More...
      neXtProti
      NX_O94811

      <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

      Keywords - Cellular componenti

      Cell junction, Cytoplasm, Cytoskeleton, Golgi apparatus, Nucleus, Synapse

      <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

      Mutagenesis

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi14T → A in 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-18, A-45 and A-160. 1 Publication1
      Mutagenesisi14T → E in 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-18, E-45 and E-160. 1 Publication1
      Mutagenesisi18S → A in 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-14, A-45 and A-160. 1 Publication1
      Mutagenesisi18S → E in 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-14, E-45 and E-160. 1 Publication1
      Mutagenesisi32S → A in 3Ala; abolished phosphorylation by ROCK1, leading to delayed entry into S-phase; when associated with A-107 and A-159. 2 Publications1
      Mutagenesisi32S → E in 3Glu; phosphomimetic mutant, leading to decreased transition of the G1/S-phase; when associated with E-07 and E-159. 2 Publications1
      Mutagenesisi45S → A in 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-14, A-18 and A-160. 1 Publication1
      Mutagenesisi45S → E in 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-14, E-18 and E-160. 1 Publication1
      Mutagenesisi107S → A in 3Ala; abolished phosphorylation by ROCK1, leading to delayed entry into S-phase; when associated with A-32 and A-159. 2 Publications1
      Mutagenesisi107S → E in 3Glu; phosphomimetic mutant, leading to decreased transition of the G1/S-phase; when associated with E-32 and E-159. 2 Publications1
      Mutagenesisi159S → A in 3Ala; abolished phosphorylation by ROCK1, leading to delayed entry into S-phase; when associated with A-32 and A-107. 2 Publications1
      Mutagenesisi159S → E in 3Glu; phosphomimetic mutant, leading to decreased transition of the G1/S-phase; when associated with E-32 and E-107. 2 Publications1
      Mutagenesisi160S → A in 4Ala; abolished phosphorylation by CDK1 without affecting G1/S-phase transition; when associated with A-14, A-18 and A-45. 1 Publication1
      Mutagenesisi160S → E in 4Glu; phosphomimetic mutant, does not affect G1/S-phase transition; when associated with E-14, E-18 and E-45. 1 Publication1

      Organism-specific databases

      DisGeNET

      More...
      DisGeNETi
      11076

      Open Targets

      More...
      OpenTargetsi
      ENSG00000171368

      The Pharmacogenetics and Pharmacogenomics Knowledge Base

      More...
      PharmGKBi
      PA162406809

      Miscellaneous databases

      Pharos NIH Druggable Genome Knowledgebase

      More...
      Pharosi
      O94811 Tbio

      Polymorphism and mutation databases

      BioMuta curated single-nucleotide variation and disease association database

      More...
      BioMutai
      TPPP

      <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002211351 – 219Tubulin polymerization-promoting proteinAdd BLAST219

      Amino acid modifications

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei14Phosphothreonine; by CDK1 and CDK5Combined sources2 Publications1
      Modified residuei18Phosphoserine; by CDK1, CDK5 and MAPK1Combined sources2 Publications1
      Modified residuei32Phosphoserine; by ROCK1Combined sources2 Publications1
      Modified residuei35PhosphoserineCombined sources1
      Modified residuei45Phosphoserine; by CDK1Combined sources1 Publication1
      Modified residuei92Phosphothreonine; by PKA; in vitro1 Publication1
      Modified residuei107Phosphoserine; by ROCK11 Publication1
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi152O-linked (GlcNAc) serineBy similarity1
      Modified residuei159Phosphoserine; by ROCK1Combined sources2 Publications1
      Modified residuei160Phosphoserine; by CDK1, CDK5 and MAPK12 Publications1

      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

      Phosphorylated by LIMK1 on serine residues; phosphorylation may alter the tubulin polymerization activity (PubMed:17693641, PubMed:18028908). Phosphorylation by LIMK2, but not LIMK1, regulates astral microtubule organization at early stage of mitosis (PubMed:22328514). Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 inhibits interaction with HDAC6, resulting in increased acetylation of tubulin, increased cell motility and entry into S-phase (PubMed:23093407, PubMed:23355470). Phosphorylation by CDK1 inhibits the microtubule polymerizing activity (PubMed:23355470).5 Publications
      Degraded by the proteasome; zinc-binding inhibits degradation by the proteasome.1 Publication

      Keywords - PTMi

      Glycoprotein, Phosphoprotein

      Proteomic databases

      Encyclopedia of Proteome Dynamics

      More...
      EPDi
      O94811

      jPOST - Japan Proteome Standard Repository/Database

      More...
      jPOSTi
      O94811

      MassIVE - Mass Spectrometry Interactive Virtual Environment

      More...
      MassIVEi
      O94811

      PaxDb, a database of protein abundance averages across all three domains of life

      More...
      PaxDbi
      O94811

      PeptideAtlas

      More...
      PeptideAtlasi
      O94811

      PRoteomics IDEntifications database

      More...
      PRIDEi
      O94811

      ProteomicsDB: a multi-organism proteome resource

      More...
      ProteomicsDBi
      50451

      2D gel databases

      University College Dublin 2-DE Proteome Database

      More...
      UCD-2DPAGEi
      O94811

      PTM databases

      iPTMnet integrated resource for PTMs in systems biology context

      More...
      iPTMneti
      O94811

      Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

      More...
      PhosphoSitePlusi
      O94811

      <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

      <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

      Widely expressed.1 Publication

      <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

      enriched in cerebrospinal fluid of multiple sclerosis patients (at protein level).1 Publication

      Gene expression databases

      Bgee dataBase for Gene Expression Evolution

      More...
      Bgeei
      ENSG00000171368 Expressed in Brodmann (1909) area 23 and 206 other tissues

      ExpressionAtlas, Differential and Baseline Expression

      More...
      ExpressionAtlasi
      O94811 baseline and differential

      Genevisible search portal to normalized and curated expression data from Genevestigator

      More...
      Genevisiblei
      O94811 HS

      Organism-specific databases

      Human Protein Atlas

      More...
      HPAi
      ENSG00000171368 Tissue enriched (brain)

      <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

      <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

      Homodimer (PubMed:17693641, PubMed:22484033, PubMed:26289831). Binds tubulin; binding is inhibited by GTP (PubMed:17105200, PubMed:26289831).

      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 (PubMed:18028908, PubMed:22328514).

      Interacts with LIMK2 (PubMed:22328514).

      Interacts with HDAC6; thereby inhibiting the tubulin deacetylase activity of HDAC6 (PubMed:20308065, PubMed:23093407).

      Interacts with aggregated SNCA; may have a pro-aggregatory role in synucleinopathies (PubMed:15590652, PubMed:17027006).

      Interacts with DYNLL1 (PubMed:31505170).

      By similarity11 Publications

      <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

      Hide details

      GO - Molecular functioni

      Protein-protein interaction databases

      The Biological General Repository for Interaction Datasets (BioGRID)

      More...
      BioGRIDi
      116259, 15 interactors

      Protein interaction database and analysis system

      More...
      IntActi
      O94811, 13 interactors

      Molecular INTeraction database

      More...
      MINTi
      O94811

      STRING: functional protein association networks

      More...
      STRINGi
      9606.ENSP00000353785

      Chemistry databases

      BindingDB database of measured binding affinities

      More...
      BindingDBi
      O94811

      Miscellaneous databases

      RNAct, Protein-RNA interaction predictions for model organisms.

      More...
      RNActi
      O94811 protein

      <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

      Region

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 116Mediates interaction with LIMK11 PublicationAdd BLAST116
      Regioni1 – 46DisorderedSequence analysisAdd BLAST46
      Regioni171 – 192DisorderedSequence analysisAdd BLAST22

      <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

      Most of the protein is composed of disordered regions (PubMed:21316364). Zinc-binding induces structural rearrangement by promoting molten globule state formation (PubMed:21995432).2 Publications

      <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

      Belongs to the TPPP family.Curated

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...
      eggNOGi
      KOG4070 Eukaryota
      ENOG4111H9J LUCA

      Ensembl GeneTree

      More...
      GeneTreei
      ENSGT00940000153875

      The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

      More...
      HOGENOMi
      CLU_091734_0_0_1

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      O94811

      Identification of Orthologs from Complete Genome Data

      More...
      OMAi
      CRDCQVI

      Database of Orthologous Groups

      More...
      OrthoDBi
      1317210at2759

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      O94811

      TreeFam database of animal gene trees

      More...
      TreeFami
      TF314440

      Family and domain databases

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR011992 EF-hand-dom_pair
      IPR008907 P25-alpha
      IPR030792 TPPP1

      The PANTHER Classification System

      More...
      PANTHERi
      PTHR12932 PTHR12932, 1 hit
      PTHR12932:SF18 PTHR12932:SF18, 1 hit

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF05517 p25-alpha, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF47473 SSF47473, 1 hit

      <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

      <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
      <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF8B2C814EA59129A
      GO

      <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

      Sequence databases

      Select the link destinations:

      EMBL nucleotide sequence database

      More...
      EMBLi

      GenBank nucleotide sequence database

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      GenBanki

      DNA Data Bank of Japan; a nucleotide sequence database

      More...
      DDBJi
      Links Updated
      AB017016 mRNA Translation: BAA36164.1
      BT020035 mRNA Translation: AAV38838.1
      BC040496 mRNA Translation: AAH40496.1 Different initiation.

      The Consensus CDS (CCDS) project

      More...
      CCDSi
      CCDS3856.1

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_008961.1, NM_007030.2
      XP_005248294.2, XM_005248237.3
      XP_016864483.1, XM_017008994.1

      Genome annotation databases

      Ensembl eukaryotic genome annotation project

      More...
      Ensembli
      ENST00000360578; ENSP00000353785; ENSG00000171368

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      11076

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      hsa:11076

      <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

      <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
      XP_005248294.2, XM_005248237.3
      XP_016864483.1, XM_017008994.1

      3D structure databases

      Database of comparative protein structure models

      More...
      ModBasei
      Search...

      SWISS-MODEL Interactive Workspace

      More...
      SWISS-MODEL-Workspacei
      Submit a new modelling project...

      Protein-protein interaction databases

      BioGRIDi116259, 15 interactors
      IntActiO94811, 13 interactors
      MINTiO94811
      STRINGi9606.ENSP00000353785

      Chemistry databases

      BindingDBiO94811

      PTM databases

      iPTMnetiO94811
      PhosphoSitePlusiO94811

      Polymorphism and mutation databases

      BioMutaiTPPP

      2D gel databases

      UCD-2DPAGEiO94811

      Proteomic databases

      EPDiO94811
      jPOSTiO94811
      MassIVEiO94811
      PaxDbiO94811
      PeptideAtlasiO94811
      PRIDEiO94811
      ProteomicsDBi50451

      Protocols and materials databases

      Antibodypedia a portal for validated antibodies

      More...
      Antibodypediai
      22256 242 antibodies

      Genome annotation databases

      EnsembliENST00000360578; ENSP00000353785; ENSG00000171368
      GeneIDi11076
      KEGGihsa:11076

      Organism-specific databases

      Comparative Toxicogenomics Database

      More...
      CTDi
      11076
      DisGeNETi11076
      EuPathDBiHostDB:ENSG00000171368.11

      GeneCards: human genes, protein and diseases

      More...
      GeneCardsi
      TPPP
      HGNCiHGNC:24164 TPPP
      HPAiENSG00000171368 Tissue enriched (brain)
      MIMi608773 gene
      neXtProtiNX_O94811
      OpenTargetsiENSG00000171368
      PharmGKBiPA162406809

      GenAtlas: human gene database

      More...
      GenAtlasi
      Search...

      Phylogenomic databases

      eggNOGiKOG4070 Eukaryota
      ENOG4111H9J LUCA
      GeneTreeiENSGT00940000153875
      HOGENOMiCLU_091734_0_0_1
      InParanoidiO94811
      OMAiCRDCQVI
      OrthoDBi1317210at2759
      PhylomeDBiO94811
      TreeFamiTF314440

      Miscellaneous databases

      BioGRID ORCS database of CRISPR phenotype screens

      More...
      BioGRID-ORCSi
      11076 4 hits in 790 CRISPR screens

      The Gene Wiki collection of pages on human genes and proteins

      More...
      GeneWikii
      TPPP

      Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

      More...
      GenomeRNAii
      11076
      PharosiO94811 Tbio

      Protein Ontology

      More...
      PROi
      PR:O94811
      RNActiO94811 protein

      The Stanford Online Universal Resource for Clones and ESTs

      More...
      SOURCEi
      Search...

      Gene expression databases

      BgeeiENSG00000171368 Expressed in Brodmann (1909) area 23 and 206 other tissues
      ExpressionAtlasiO94811 baseline and differential
      GenevisibleiO94811 HS

      Family and domain databases

      InterProiView protein in InterPro
      IPR011992 EF-hand-dom_pair
      IPR008907 P25-alpha
      IPR030792 TPPP1
      PANTHERiPTHR12932 PTHR12932, 1 hit
      PTHR12932:SF18 PTHR12932:SF18, 1 hit
      PfamiView protein in Pfam
      PF05517 p25-alpha, 1 hit
      SUPFAMiSSF47473 SSF47473, 1 hit

      ProtoNet; Automatic hierarchical classification of proteins

      More...
      ProtoNeti
      Search...

      MobiDB: a database of protein disorder and mobility annotations

      More...
      MobiDBi
      Search...

      <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

      <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTPPP_HUMAN
      <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O94811
      <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 12, 2003
      Last sequence update: May 1, 1999
      Last modified: June 17, 2020
      This is version 150 of the entry and version 1 of the sequence. See complete history.
      <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

      <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

      Keywords - Technical termi

      Reference proteome

      Documents

      1. SIMILARITY comments
        Index of protein domains and families
      2. MIM cross-references
        Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
      3. Human chromosome 5
        Human chromosome 5: entries, gene names and cross-references to MIM
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