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Entry version 208 (16 Oct 2019)
Sequence version 3 (05 May 2009)
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Protein

Activated CDC42 kinase 1

Gene

TNK2

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

Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr-287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR. Phosphorylates WASP (PubMed:20110370).12 Publications

<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

Mg2+3 Publications

<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

Inhibited by AIM-100 (4-amino-5,6-biaryl-furo[2,3-d]pyrimidine), which suppresses activating phosphorylation at Tyr-284. Repressed by dasatinib.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei158ATP1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei252Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi132 – 140ATP9

<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 functionKinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase
Biological processEndocytosis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.2 2681

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q07912

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q07912

<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:
Activated CDC42 kinase 1 (EC:2.7.10.25 Publications, EC:2.7.11.12 Publications)
Short name:
ACK-1
Alternative name(s):
Tyrosine kinase non-receptor protein 2
<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:TNK2
Synonyms:ACK1
<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 3

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:19297 TNK2

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
606994 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q07912

<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, Cell membrane, Coated pit, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane, Nucleus

<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_and_biotech_section">'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>Mutagenesisi120L → Q: No effect on autophosphorylation at Y-284. 1 Publication1
Mutagenesisi158K → R: Loss of autophosphorylation at Y-284. 2 Publications1
Mutagenesisi197L → Q: No effect on autophosphorylation at Y-284. 1 Publication1
Mutagenesisi365V → R: Increased autophosphorylation at Y-284. 1 Publication1
Mutagenesisi487L → F: Constantly active kinase. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
10188

MalaCards human disease database

More...
MalaCardsi
TNK2

Open Targets

More...
OpenTargetsi
ENSG00000061938

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
391316 Infantile-onset mesial temporal lobe epilepsy with severe cognitive regression

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA134909759

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q07912

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4599

Drug and drug target database

More...
DrugBanki
DB00171 ATP
DB04367 Debromohymenialdisine
DB12010 Fostamatinib

DrugCentral

More...
DrugCentrali
Q07912

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2246

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
TNK2

Domain mapping of disease mutations (DMDM)

More...
DMDMi
229462980

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000880581 – 1038Activated CDC42 kinase 1Add BLAST1038

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 residuei284Phosphotyrosine; by SRC and autocatalysisCombined sources7 Publications1
Modified residuei518Phosphotyrosine1 Publication1
Modified residuei724PhosphoserineCombined sources1
Modified residuei827Phosphotyrosine1 Publication1
Modified residuei839Omega-N-methylarginineBy similarity1
Modified residuei859Phosphotyrosine1 Publication1
Modified residuei872Phosphotyrosine1 Publication1
Modified residuei881PhosphoserineCombined sources1

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

Autophosphorylation regulates kinase activity. Phosphorylation on Tyr-518 is required for interaction with SRC and is observed during association with clathrin-coated pits.7 Publications
Polyubiquitinated by NEDD4 and NEDD4L. Degradation can be induced by EGF and is lysosome-dependent (By similarity).By similarity

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
CPTAC-1779
CPTAC-2789

Encyclopedia of Proteome Dynamics

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EPDi
Q07912

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q07912

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q07912

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q07912

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

More...
PaxDbi
Q07912

PeptideAtlas

More...
PeptideAtlasi
Q07912

PRoteomics IDEntifications database

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PRIDEi
Q07912

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
58556 [Q07912-1]
58557 [Q07912-2]
58558 [Q07912-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q07912

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

More...
PhosphoSitePlusi
Q07912

<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

The Tyr-284 phosphorylated form shows a significant increase in expression in breast cancers during the progressive stages i.e. normal to hyperplasia (ADH), ductal carcinoma in situ (DCIS), invasive ductal carcinoma (IDC) and lymph node metastatic (LNMM) stages. It also shows a significant increase in expression in prostate cancers during the progressive stages.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000061938 Expressed in 220 organ(s), highest expression level in anterior cingulate cortex

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q07912 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q07912 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA041954

<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

Interacts with NEDD4 (via WW3 domain). NEDD4L and EGF promote association with NEDD4 (By similarity). Homodimer.

Interacts with AR, CDC42, WWASL and WWOX.

Interacts with CSPG4 (activated).

Interacts with MERTK (activated); stimulates autophosphorylation. May interact (phosphorylated) with HSP90AB1; maintains kinase activity.

Interacts with NPHP1.

Interacts with SNX9 (via SH3 domain).

Interacts with SRC (via SH2 and SH3 domain).

Interacts with EGFR, and this interaction is dependent on EGF stimulation and kinase activity of EGFR.

Interacts (via kinase domain) with AKT1.

Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas.

Interacts with BCAR1/p130cas via SH3 domains. Forms complexes with GRB2 and numerous receptor tyrosine kinases (RTK) including LTK, AXL or PDGFRL, in which GRB2 promotes RTK recruitment by TNK2.

By similarity15 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
115485, 88 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q07912

Database of interacting proteins

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DIPi
DIP-33858N

Protein interaction database and analysis system

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IntActi
Q07912, 42 interactors

Molecular INTeraction database

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MINTi
Q07912

STRING: functional protein association networks

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STRINGi
9606.ENSP00000371341

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q07912

<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

11038
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
Q07912

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q07912

<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 <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini126 – 385Protein kinasePROSITE-ProRule annotationAdd BLAST260
Domaini388 – 448SH3PROSITE-ProRule annotationAdd BLAST61
Domaini454 – 466CRIBAdd BLAST13
Domaini958 – 996UBAAdd BLAST39

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 – 110SAM-like domainAdd BLAST110
Regioni623 – 652Required for interaction with SRC1 PublicationAdd BLAST30
Regioni632 – 635Required for interaction with NEDD4By similarity4
Regioni733 – 876EBD domainBy similarityAdd BLAST144

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi577 – 958Pro-richAdd BLAST382

<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

The EBD (EGFR-binding domain) domain is necessary for interaction with EGFR.By similarity
The SAM-like domain is necessary for NEDD4-mediated ubiquitination. Promotes membrane localization and dimerization to allow for autophosphorylation.1 Publication
The UBA domain binds both poly- and mono-ubiquitin.1 Publication

<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 protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation

Keywords - Domaini

SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0199 Eukaryota
ENOG410XPRC LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160853

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000168225

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q07912

KEGG Orthology (KO)

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KOi
K08886

Database of Orthologous Groups

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OrthoDBi
1008736at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q07912

TreeFam database of animal gene trees

More...
TreeFami
TF316643

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
4.10.680.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR030220 Ack1
IPR037085 Cdc42-bd-like_dom_sf
IPR015116 Cdc42_binding_dom-like
IPR011009 Kinase-like_dom_sf
IPR021619 Mig-6
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom

The PANTHER Classification System

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PANTHERi
PTHR14254:SF6 PTHR14254:SF6, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF09027 GTPase_binding, 1 hit
PF11555 Inhibitor_Mig-6, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF14604 SH3_9, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50044 SSF50044, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50002 SH3, 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>Sequences (3+)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.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q07912-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MQPEEGTGWL LELLSEVQLQ QYFLRLRDDL NVTRLSHFEY VKNEDLEKIG
60 70 80 90 100
MGRPGQRRLW EAVKRRKALC KRKSWMSKVF SGKRLEAEFP PHHSQSTFRK
110 120 130 140 150
TSPAPGGPAG EGPLQSLTCL IGEKDLRLLE KLGDGSFGVV RRGEWDAPSG
160 170 180 190 200
KTVSVAVKCL KPDVLSQPEA MDDFIREVNA MHSLDHRNLI RLYGVVLTPP
210 220 230 240 250
MKMVTELAPL GSLLDRLRKH QGHFLLGTLS RYAVQVAEGM GYLESKRFIH
260 270 280 290 300
RDLAARNLLL ATRDLVKIGD FGLMRALPQN DDHYVMQEHR KVPFAWCAPE
310 320 330 340 350
SLKTRTFSHA SDTWMFGVTL WEMFTYGQEP WIGLNGSQIL HKIDKEGERL
360 370 380 390 400
PRPEDCPQDI YNVMVQCWAH KPEDRPTFVA LRDFLLEAQP TDMRALQDFE
410 420 430 440 450
EPDKLHIQMN DVITVIEGRA ENYWWRGQNT RTLCVGPFPR NVVTSVAGLS
460 470 480 490 500
AQDISQPLQN SFIHTGHGDS DPRHCWGFPD RIDELYLGNP MDPPDLLSVE
510 520 530 540 550
LSTSRPPQHL GGVKKPTYDP VSEDQDPLSS DFKRLGLRKP GLPRGLWLAK
560 570 580 590 600
PSARVPGTKA SRGSGAEVTL IDFGEEPVVP ALRPCAPSLA QLAMDACSLL
610 620 630 640 650
DETPPQSPTR ALPRPLHPTP VVDWDARPLP PPPAYDDVAQ DEDDFEICSI
660 670 680 690 700
NSTLVGAGVP AGPSQGQTNY AFVPEQARPP PPLEDNLFLP PQGGGKPPSS
710 720 730 740 750
AQTAEIFQAL QQECMRQLQA PAGSPAPSPS PGGDDKPQVP PRVPIPPRPT
760 770 780 790 800
RPHVQLSPAP PGEEETSQWP GPASPPRVPP REPLSPQGSR TPSPLVPPGS
810 820 830 840 850
SPLPPRLSSS PGKTMPTTQS FASDPKYATP QVIQAPGPRA GPCILPIVRD
860 870 880 890 900
GKKVSSTHYY LLPERPSYLE RYQRFLREAQ SPEEPTPLPV PLLLPPPSTP
910 920 930 940 950
APAAPTATVR PMPQAALDPK ANFSTNNSNP GARPPPPRAT ARLPQRGCPG
960 970 980 990 1000
DGPEAGRPAD KIQMAMVHGV TTEECQAALQ CHGWSVQRAA QYLKVEQLFG
1010 1020 1030
LGLRPRGECH KVLEMFDWNL EQAGCHLLGS WGPAHHKR
Length:1,038
Mass (Da):114,569
Last modified:May 5, 2009 - v3
<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:i74A1980665BC3E6B
GO
Isoform 2 (identifier: Q07912-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     485-528: LYLGNPMDPP...DPVSEDQDPL → CPFSAFSPGH...HPVSSRTKGL
     529-1038: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:528
Mass (Da):60,062
Checksum:i6CE378AE9D186C20
GO
Isoform 3 (identifier: Q07912-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGERSAYQRLAGGEEGPQRLGGGRM
     514-514: K → KREPPPRPPQPAFFTQ
     965-994: Missing.

Note: No experimental confirmation available.
Show »
Length:1,047
Mass (Da):115,532
Checksum:i631443FD68560DDF
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9J1X3C9J1X3_HUMAN
Activated CDC42 kinase 1
TNK2
1,040Annotation score:

Annotation score:2 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>
A0A499FJ16A0A499FJ16_HUMAN
Activated CDC42 kinase 1
TNK2
1,086Annotation score:

Annotation score:2 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>

<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 AAH08884 differs from that shown. Unlikely isoform. Aberrant splice sites.Curated
The sequence BAD18675 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

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 conflicti138G → V in AAH08884 (PubMed:15489334).Curated1
Sequence conflicti304 – 352TRTFS…ERLPR → PPWRDISASSSTQFPHAVPC FPTSLLAKLLLRHSVPASSR EIKLVSILC in AAH08884 (PubMed:15489334).CuratedAdd BLAST49
Sequence conflicti353 – 1038Missing in AAH08884 (PubMed:15489334).CuratedAdd BLAST686
Sequence conflicti586A → P in AAA53570 (PubMed:8497321).Curated1
Sequence conflicti722Missing in AAA53570 (PubMed:8497321).Curated1
Sequence conflicti838 – 840PRA → AG in AAA53570 (PubMed:8497321).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03279234R → L in a lung adenocarcinoma sample; somatic mutation; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates; no effect on subcellular localization to perinuclear region. 2 Publications1
Natural variantiVAR_03279371K → R1 PublicationCorresponds to variant dbSNP:rs56036945Ensembl.1
Natural variantiVAR_03279499R → Q in an ovarian mucinous carcinoma sample; somatic mutation; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates and WASP; no effect on subcellular localization to perinuclear region. 2 PublicationsCorresponds to variant dbSNP:rs113498671Ensembl.1
Natural variantiVAR_03279599R → W1 PublicationCorresponds to variant dbSNP:rs3747673Ensembl.1
Natural variantiVAR_032796152T → M1 PublicationCorresponds to variant dbSNP:rs56161912Ensembl.1
Natural variantiVAR_032797346E → K in an ovarian endometrioid cancer sample; somatic mutation; undergoes autoactivation and causes phosphorylation on Y-284 leading to activation of AKT1; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates and WASP; no effect on catalytic activity itself as the purified kinase domain has activity in vitro comparable to wild-type protein; no effect on subcellular localization to perinuclear region. 3 PublicationsCorresponds to variant dbSNP:rs970946035Ensembl.1
Natural variantiVAR_032798409M → I in a gastric adenocarcinoma sample; somatic mutation; increased autophosphorylation at Y-284; increased function in phosphorylation of peptide substrates and WASP; no effect on subcellular localization to perinuclear region. 2 Publications1
Natural variantiVAR_032799507P → S1 PublicationCorresponds to variant dbSNP:rs35759128Ensembl.1
Natural variantiVAR_076966638V → M Found in patients with childhood-onset epilepsy; unknown pathological significance; loss of interaction with NEDD4 and NEDD4L; increased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs201407161EnsemblClinVar.1
Natural variantiVAR_032800725P → L2 PublicationsCorresponds to variant dbSNP:rs56260729EnsemblClinVar.1
Natural variantiVAR_032801748R → Q1 PublicationCorresponds to variant dbSNP:rs57872314Ensembl.1
Natural variantiVAR_057115802P → L. Corresponds to variant dbSNP:rs3749333Ensembl.1
Natural variantiVAR_0328021038R → H1 PublicationCorresponds to variant dbSNP:rs13433937EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0372841M → MGERSAYQRLAGGEEGPQRL GGGRM in isoform 3. 1 Publication1
Alternative sequenceiVSP_008655485 – 528LYLGN…DQDPL → CPFSAFSPGHPPAETCGQVL WTGRREACASDPRLHPVSSR TKGL in isoform 2. 1 PublicationAdd BLAST44
Alternative sequenceiVSP_037285514K → KREPPPRPPQPAFFTQ in isoform 3. 1 Publication1
Alternative sequenceiVSP_008656529 – 1038Missing in isoform 2. 1 PublicationAdd BLAST510
Alternative sequenceiVSP_037286965 – 994Missing in isoform 3. 1 PublicationAdd BLAST30

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L13738 mRNA Translation: AAA53570.2
AK131539 mRNA Translation: BAD18675.1 Different initiation.
AC124944 Genomic DNA No translation available.
BC008884 mRNA Translation: AAH08884.1 Sequence problems.
BC028164 mRNA Translation: AAH28164.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS33927.1 [Q07912-3]
CCDS33928.1 [Q07912-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
S33596

NCBI Reference Sequences

More...
RefSeqi
NP_001010938.1, NM_001010938.1 [Q07912-3]
NP_001294975.1, NM_001308046.1
NP_005772.3, NM_005781.4 [Q07912-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000333602; ENSP00000329425; ENSG00000061938 [Q07912-1]
ENST00000439230; ENSP00000395588; ENSG00000061938 [Q07912-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
10188

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:10188

UCSC genome browser

More...
UCSCi
uc003fvt.2 human [Q07912-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
L13738 mRNA Translation: AAA53570.2
AK131539 mRNA Translation: BAD18675.1 Different initiation.
AC124944 Genomic DNA No translation available.
BC008884 mRNA Translation: AAH08884.1 Sequence problems.
BC028164 mRNA Translation: AAH28164.1
CCDSiCCDS33927.1 [Q07912-3]
CCDS33928.1 [Q07912-1]
PIRiS33596
RefSeqiNP_001010938.1, NM_001010938.1 [Q07912-3]
NP_001294975.1, NM_001308046.1
NP_005772.3, NM_005781.4 [Q07912-1]

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
1CF4NMR-B448-489[»]
1U46X-ray2.00A/B109-395[»]
1U4DX-ray2.10A/B109-395[»]
1U54X-ray2.80A/B109-395[»]
3EQPX-ray2.30A/B117-392[»]
3EQRX-ray2.00A/B117-392[»]
4EWHX-ray2.50A/B117-391[»]
4HZRX-ray1.31A/B115-389[»]
4HZSX-ray3.23A/B/C/D115-453[»]
4ID7X-ray3.00A117-389[»]
5ZXBX-ray2.20A/B117-391[»]
SMRiQ07912
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi115485, 88 interactors
CORUMiQ07912
DIPiDIP-33858N
IntActiQ07912, 42 interactors
MINTiQ07912
STRINGi9606.ENSP00000371341

Chemistry databases

BindingDBiQ07912
ChEMBLiCHEMBL4599
DrugBankiDB00171 ATP
DB04367 Debromohymenialdisine
DB12010 Fostamatinib
DrugCentraliQ07912
GuidetoPHARMACOLOGYi2246

PTM databases

iPTMnetiQ07912
PhosphoSitePlusiQ07912

Polymorphism and mutation databases

BioMutaiTNK2
DMDMi229462980

Proteomic databases

CPTACiCPTAC-1779
CPTAC-2789
EPDiQ07912
jPOSTiQ07912
MassIVEiQ07912
MaxQBiQ07912
PaxDbiQ07912
PeptideAtlasiQ07912
PRIDEiQ07912
ProteomicsDBi58556 [Q07912-1]
58557 [Q07912-2]
58558 [Q07912-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
10188

Genome annotation databases

EnsembliENST00000333602; ENSP00000329425; ENSG00000061938 [Q07912-1]
ENST00000439230; ENSP00000395588; ENSG00000061938 [Q07912-2]
GeneIDi10188
KEGGihsa:10188
UCSCiuc003fvt.2 human [Q07912-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10188
DisGeNETi10188

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TNK2
HGNCiHGNC:19297 TNK2
HPAiHPA041954
MalaCardsiTNK2
MIMi606994 gene
neXtProtiNX_Q07912
OpenTargetsiENSG00000061938
Orphaneti391316 Infantile-onset mesial temporal lobe epilepsy with severe cognitive regression
PharmGKBiPA134909759

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0199 Eukaryota
ENOG410XPRC LUCA
GeneTreeiENSGT00940000160853
HOGENOMiHOG000168225
InParanoidiQ07912
KOiK08886
OrthoDBi1008736at2759
PhylomeDBiQ07912
TreeFamiTF316643

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
SignaLinkiQ07912
SIGNORiQ07912

Miscellaneous databases

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

More...
ChiTaRSi
TNK2 human
EvolutionaryTraceiQ07912

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
TNK2

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

More...
GenomeRNAii
10188
PharosiQ07912

Protein Ontology

More...
PROi
PR:Q07912

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000061938 Expressed in 220 organ(s), highest expression level in anterior cingulate cortex
ExpressionAtlasiQ07912 baseline and differential
GenevisibleiQ07912 HS

Family and domain databases

Gene3Di4.10.680.10, 1 hit
InterProiView protein in InterPro
IPR030220 Ack1
IPR037085 Cdc42-bd-like_dom_sf
IPR015116 Cdc42_binding_dom-like
IPR011009 Kinase-like_dom_sf
IPR021619 Mig-6
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PANTHERiPTHR14254:SF6 PTHR14254:SF6, 1 hit
PfamiView protein in Pfam
PF09027 GTPase_binding, 1 hit
PF11555 Inhibitor_Mig-6, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF14604 SH3_9, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS50002 SH3, 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 nameiACK1_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: Q07912
Secondary accession number(s): Q6ZMQ0, Q8N6U7, Q96H59
<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 24, 2003
Last sequence update: May 5, 2009
Last modified: October 16, 2019
This is version 208 of the entry and version 3 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, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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