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Entry version 173 (11 Dec 2019)
Sequence version 2 (01 Nov 1997)
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Protein

Geranylgeranyl transferase type-2 subunit beta

Gene

RABGGTB

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

Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The enzymatic reaction requires the aid of a Rab escort protein (also called component A).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi238ZincBy similarity1
Metal bindingi238Zinc; catalyticBy similarity1
Metal bindingi240ZincBy similarity1
Metal bindingi240Zinc; catalyticBy similarity1
Metal bindingi290ZincBy similarity1
Metal bindingi290Zinc; via tele nitrogen; catalyticBy similarity1

<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 functionPrenyltransferase, Transferase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.5.1.60 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-6803205 TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain
R-HSA-8873719 RAB geranylgeranylation

<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_and_taxonomy_section">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:
Geranylgeranyl transferase type-2 subunit beta (EC:2.5.1.60)
Alternative name(s):
Geranylgeranyl transferase type II subunit beta
Short name:
GGTase-II-beta
Rab geranyl-geranyltransferase subunit beta
Short name:
Rab GG transferase beta
Short name:
Rab GGTase beta
Rab geranylgeranyltransferase subunit beta
Type II protein geranyl-geranyltransferase subunit beta
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:RABGGTB
Synonyms:GGTB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000137955.15

Human Gene Nomenclature Database

More...
HGNCi
HGNC:9796 RABGGTB

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
179080 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P53611

<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

<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

Organism-specific databases

Open Targets

More...
OpenTargetsi
ENSG00000137955

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA34157

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P53611 Tbio

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB07780 Farnesyl diphosphate
DB07841 Geranylgeranyl diphosphate
DB04464 N-Formylmethionine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
RABGGTB

Domain mapping of disease mutations (DMDM)

More...
DMDMi
2506788

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001197722 – 331Geranylgeranyl transferase type-2 subunit betaAdd BLAST330

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 residuei2N-acetylglycineCombined sources1
Modified residuei3PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P53611

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P53611

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P53611

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

More...
PaxDbi
P53611

PeptideAtlas

More...
PeptideAtlasi
P53611

PRoteomics IDEntifications database

More...
PRIDEi
P53611

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
56591

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P53611

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

More...
PhosphoSitePlusi
P53611

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000137955 Expressed in 239 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P53611 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P53611 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA026585
HPA027167
HPA030793

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterotrimer composed of RABGGTA, RABGGTB and CHM; within this trimer, RABGGTA and RABGGTB form the catalytic component B, while CHM (component A) mediates peptide substrate binding (By similarity). The Rab GGTase dimer (RGGT) interacts with CHM (component A) prior to Rab protein binding; the association is stabilized by geranylgeranyl pyrophosphate (GGpp) (PubMed:18532927). The CHM:RGGT:Rab complex is destabilized by GGpp (PubMed:18532927). Interaction of RABGGTB with prenylated PTP4A2 precludes its association with RABGGTA and inhibits enzyme activity (PubMed:11447212).

Interacts with CHODL (By similarity).

Interacts with non-phosphorylated form of RAB8A; phosphorylation of RAB8A at 'Thr-72' disrupts this interaction (PubMed:26824392).

By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111814, 74 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2919 Protein geranylgeranyltransferase type II complex

Protein interaction database and analysis system

More...
IntActi
P53611, 62 interactors

Molecular INTeraction database

More...
MINTi
P53611

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000317473

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P53611 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1331
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P53611

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati20 – 61PFTB 1Add BLAST42
Repeati68 – 109PFTB 2Add BLAST42
Repeati116 – 157PFTB 3Add BLAST42
Repeati164 – 205PFTB 4Add BLAST42
Repeati212 – 253PFTB 5Add BLAST42
Repeati260 – 302PFTB 6Add BLAST43

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>Regioni190 – 192Geranylgeranyl diphosphate bindingBy similarity3
Regioni232 – 244Geranylgeranyl diphosphate bindingBy similarityAdd BLAST13

<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

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0366 Eukaryota
COG5029 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183128

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000180334

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P53611

KEGG Orthology (KO)

More...
KOi
K05956

Identification of Orthologs from Complete Genome Data

More...
OMAi
VKRCQCP

Database of Orthologous Groups

More...
OrthoDBi
1042804at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P53611

TreeFam database of animal gene trees

More...
TreeFami
TF105762

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02894 GGTase-II, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001330 PFTB_repeat
IPR026873 Ptb1
IPR008930 Terpenoid_cyclase/PrenylTrfase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00432 Prenyltrans, 5 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48239 SSF48239, 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_length">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P53611-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGTPQKDVII KSDAPDTLLL EKHADYIASY GSKKDDYEYC MSEYLRMSGI
60 70 80 90 100
YWGLTVMDLM GQLHRMNREE ILAFIKSCQH ECGGISASIG HDPHLLYTLS
110 120 130 140 150
AVQILTLYDS INVIDVNKVV EYVKGLQKED GSFAGDIWGE IDTRFSFCAV
160 170 180 190 200
ATLALLGKLD AINVEKAIEF VLSCMNFDGG FGCRPGSESH AGQIYCCTGF
210 220 230 240 250
LAITSQLHQV NSDLLGWWLC ERQLPSGGLN GRPEKLPDVC YSWWVLASLK
260 270 280 290 300
IIGRLHWIDR EKLRNFILAC QDEETGGFAD RPGDMVDPFH TLFGIAGLSL
310 320 330
LGEEQIKPVN PVFCMPEEVL QRVNVQPELV S
Length:331
Mass (Da):36,924
Last modified:November 1, 1997 - v2
<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:i37A8A6329146C49B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5T4U8Q5T4U8_HUMAN
Geranylgeranyl transferase type-2 s...
RABGGTB
152Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti153L → F in AAA91473 (Ref. 1) Curated1
Sequence conflicti177F → S in CAA69383 (PubMed:8954794).Curated1
Sequence conflicti211N → T in CAA69383 (PubMed:8954794).Curated1

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
U49245 mRNA Translation: AAA91473.1
X98001 mRNA Translation: CAA66638.1
Y08201 mRNA Translation: CAA69383.1
BC020790 mRNA Translation: AAH20790.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS669.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G02431

NCBI Reference Sequences

More...
RefSeqi
NP_004573.2, NM_004582.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000319942; ENSP00000317473; ENSG00000137955

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5876

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5876

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Rab geranylgeranyltransferase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49245 mRNA Translation: AAA91473.1
X98001 mRNA Translation: CAA66638.1
Y08201 mRNA Translation: CAA69383.1
BC020790 mRNA Translation: AAH20790.1
CCDSiCCDS669.1
PIRiG02431
RefSeqiNP_004573.2, NM_004582.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6O60X-ray2.50B1-331[»]
SMRiP53611
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi111814, 74 interactors
ComplexPortaliCPX-2919 Protein geranylgeranyltransferase type II complex
IntActiP53611, 62 interactors
MINTiP53611
STRINGi9606.ENSP00000317473

Chemistry databases

DrugBankiDB07780 Farnesyl diphosphate
DB07841 Geranylgeranyl diphosphate
DB04464 N-Formylmethionine

PTM databases

iPTMnetiP53611
PhosphoSitePlusiP53611

Polymorphism and mutation databases

BioMutaiRABGGTB
DMDMi2506788

Proteomic databases

EPDiP53611
jPOSTiP53611
MassIVEiP53611
PaxDbiP53611
PeptideAtlasiP53611
PRIDEiP53611
ProteomicsDBi56591

Genome annotation databases

EnsembliENST00000319942; ENSP00000317473; ENSG00000137955
GeneIDi5876
KEGGihsa:5876

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5876
EuPathDBiHostDB:ENSG00000137955.15

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RABGGTB
HGNCiHGNC:9796 RABGGTB
HPAiHPA026585
HPA027167
HPA030793
MIMi179080 gene
neXtProtiNX_P53611
OpenTargetsiENSG00000137955
PharmGKBiPA34157

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0366 Eukaryota
COG5029 LUCA
GeneTreeiENSGT00950000183128
HOGENOMiHOG000180334
InParanoidiP53611
KOiK05956
OMAiVKRCQCP
OrthoDBi1042804at2759
PhylomeDBiP53611
TreeFamiTF105762

Enzyme and pathway databases

BRENDAi2.5.1.60 2681
ReactomeiR-HSA-6803205 TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain
R-HSA-8873719 RAB geranylgeranylation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
RABGGTB human

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

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GenomeRNAii
5876
PharosiP53611 Tbio

Protein Ontology

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PROi
PR:P53611
RNActiP53611 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000137955 Expressed in 239 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiP53611 baseline and differential
GenevisibleiP53611 HS

Family and domain databases

CDDicd02894 GGTase-II, 1 hit
InterProiView protein in InterPro
IPR001330 PFTB_repeat
IPR026873 Ptb1
IPR008930 Terpenoid_cyclase/PrenylTrfase
PfamiView protein in Pfam
PF00432 Prenyltrans, 5 hits
SUPFAMiSSF48239 SSF48239, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiPGTB2_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: P53611
Secondary accession number(s): Q92697
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: December 11, 2019
This is version 173 of the entry and version 2 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

3D-structure, Reference proteome

Documents

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