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Protein

Neuroblast differentiation-associated protein AHNAK

Gene

AHNAK

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

Functioni

May be required for neuronal cell differentiation.

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • poly(A) RNA binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB
  • structural molecule activity conferring elasticity Source: UniProtKB

GO - Biological processi

  • protein oligomerization Source: UniProtKB
  • regulation of RNA splicing Source: UniProtKB
  • regulation of voltage-gated calcium channel activity Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124942-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroblast differentiation-associated protein AHNAK
Alternative name(s):
Desmoyokin
Gene namesi
Name:AHNAK
Synonyms:PM227
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:347. AHNAK.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cell-cell adherens junction Source: BHF-UCL
  • cell-cell contact zone Source: UniProtKB
  • costamere Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • sarcolemma Source: UniProtKB
  • T-tubule Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi79026.
OpenTargetsiENSG00000124942.
PharmGKBiPA24640.

Polymorphism and mutation databases

DMDMi160332335.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000645041 – 5890Neuroblast differentiation-associated protein AHNAKAdd BLAST5890

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei41PhosphoserineCombined sources1
Modified residuei93PhosphoserineCombined sources1
Modified residuei101PhosphothreonineCombined sources1
Modified residuei115PhosphoserineCombined sources1
Cross-linki134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei135PhosphoserineCombined sources1
Modified residuei158PhosphothreonineCombined sources1
Modified residuei177PhosphoserineCombined sources1
Modified residuei210PhosphoserineCombined sources1
Modified residuei212PhosphoserineCombined sources1
Modified residuei216PhosphoserineCombined sources1
Modified residuei218PhosphothreonineCombined sources1
Modified residuei220PhosphoserineCombined sources1
Modified residuei256PhosphoserineCombined sources1
Modified residuei270Omega-N-methylarginineCombined sources1
Modified residuei332PhosphoserineCombined sources1
Modified residuei337PhosphoserineCombined sources1
Modified residuei379PhosphoserineCombined sources1
Modified residuei470PhosphoserineCombined sources1
Modified residuei490PhosphothreonineCombined sources1
Modified residuei511PhosphoserineCombined sources1
Modified residuei551PhosphothreonineCombined sources1
Modified residuei553PhosphothreonineCombined sources1
Modified residuei559PhosphoserineCombined sources1
Modified residuei570PhosphoserineCombined sources1
Modified residuei572PhosphoserineCombined sources1
Modified residuei658PhosphoserineCombined sources1
Cross-linki712Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei793PhosphoserineCombined sources1
Modified residuei819PhosphoserineCombined sources1
Cross-linki942Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki961Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki961Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1010PhosphoserineCombined sources1
Modified residuei1042PhosphoserineCombined sources1
Modified residuei1068PhosphoserineCombined sources1
Modified residuei1170PhosphoserineCombined sources1
Modified residuei1192PhosphothreonineCombined sources1
Modified residuei1196PhosphoserineCombined sources1
Modified residuei1208N6-methyllysineCombined sources1
Modified residuei1286PhosphoserineCombined sources1
Modified residuei1298PhosphoserineCombined sources1
Modified residuei1580PhosphoserineCombined sources1
Modified residuei1654PhosphoserineCombined sources1
Modified residuei1666N6-methyllysineCombined sources1
Modified residuei1856PhosphoserineCombined sources1
Modified residuei1868N6-methyllysineCombined sources1
Modified residuei1923PhosphoserineCombined sources1
Modified residuei1935N6-methyllysineCombined sources1
Modified residuei1986PhosphothreonineCombined sources1
Modified residuei1990PhosphoserineCombined sources1
Modified residuei2002N6-methyllysineCombined sources1
Modified residuei2092PhosphoserineCombined sources1
Modified residuei2118PhosphoserineCombined sources1
Modified residuei2130N6-methyllysineCombined sources1
Cross-linki2132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2138PhosphoserineCombined sources1
Modified residuei2181PhosphothreonineCombined sources1
Modified residuei2287PhosphoserineCombined sources1
Modified residuei2309PhosphothreonineCombined sources1
Modified residuei2397PhosphoserineCombined sources1
Cross-linki2575Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2580PhosphoserineCombined sources1
Cross-linki2594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2600PhosphoserineCombined sources1
Modified residuei2670PhosphoserineCombined sources1
Cross-linki2703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2708PhosphoserineCombined sources1
Cross-linki2722Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2728PhosphoserineCombined sources1
Modified residuei2798PhosphoserineCombined sources1
Modified residuei2832PhosphothreonineCombined sources1
Modified residuei2845PhosphothreonineCombined sources1
Cross-linki2959Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3054PhosphoserineCombined sources1
Cross-linki3087Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3092PhosphoserineCombined sources1
Modified residuei3182PhosphoserineCombined sources1
Cross-linki3215Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3220PhosphoserineCombined sources1
Modified residuei3362PhosphoserineCombined sources1
Modified residuei3409PhosphoserineCombined sources1
Modified residuei3412PhosphoserineCombined sources1
Modified residuei3426PhosphoserineCombined sources1
Modified residuei3544PhosphoserineCombined sources1
Cross-linki3667Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3716PhosphothreonineCombined sources1
Modified residuei3746PhosphoserineCombined sources1
Cross-linki3760Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3766PhosphoserineCombined sources1
Modified residuei3836PhosphoserineCombined sources1
Cross-linki3869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3874PhosphoserineCombined sources1
Modified residuei3964PhosphoserineCombined sources1
Cross-linki3997Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4002PhosphoserineCombined sources1
Cross-linki4016Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4022PhosphoserineCombined sources1
Modified residuei4092PhosphoserineCombined sources1
Modified residuei4100PhosphothreonineCombined sources1
Modified residuei4150PhosphoserineCombined sources1
Modified residuei4220PhosphoserineCombined sources1
Cross-linki4253Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4258PhosphoserineCombined sources1
Cross-linki4272Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4278PhosphoserineCombined sources1
Modified residuei4360PhosphoserineCombined sources1
Cross-linki4381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki4400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4406PhosphoserineCombined sources1
Modified residuei4425PhosphoserineCombined sources1
Modified residuei4430PhosphothreonineCombined sources1
Cross-linki4455Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4460PhosphoserineCombined sources1
Cross-linki4474Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4480PhosphoserineCombined sources1
Modified residuei4486PhosphoserineCombined sources1
Modified residuei4516PhosphoserineCombined sources1
Modified residuei4520PhosphoserineCombined sources1
Modified residuei4564PhosphothreonineCombined sources1
Modified residuei4684PhosphoserineCombined sources1
Modified residuei4722PhosphoserineCombined sources1
Modified residuei4766PhosphothreonineCombined sources1
Modified residuei4812PhosphoserineCombined sources1
Modified residuei4900PhosphoserineCombined sources1
Modified residuei4903PhosphoserineCombined sources1
Modified residuei4908PhosphoserineCombined sources1
Modified residuei4953PhosphoserineCombined sources1
Modified residuei4960PhosphoserineCombined sources1
Modified residuei4986PhosphoserineCombined sources1
Modified residuei4993PhosphoserineCombined sources1
Modified residuei5009PhosphothreonineCombined sources1
Modified residuei5077PhosphoserineCombined sources1
Modified residuei5099PhosphoserineCombined sources1
Modified residuei5110PhosphoserineCombined sources1
Modified residuei5125PhosphoserineCombined sources1
Modified residuei5261PhosphoserineCombined sources1
Modified residuei5318PhosphoserineCombined sources1
Modified residuei5332PhosphoserineCombined sources1
Modified residuei5369PhosphoserineCombined sources1
Modified residuei5386PhosphoserineCombined sources1
Modified residuei5393PhosphoserineCombined sources1
Modified residuei5400PhosphoserineCombined sources1
Modified residuei5415PhosphothreonineCombined sources1
Modified residuei5448PhosphoserineCombined sources1
Modified residuei5519PhosphoserineCombined sources1
Modified residuei5530PhosphoserineCombined sources1
Modified residuei5552PhosphoserineCombined sources1
Modified residuei5577PhosphoserineCombined sources1
Modified residuei5620PhosphoserineCombined sources1
Modified residuei5641PhosphoserineCombined sources1
Modified residuei5731PhosphoserineCombined sources1
Modified residuei5739PhosphoserineCombined sources1
Modified residuei5749PhosphoserineCombined sources1
Modified residuei5752PhosphoserineCombined sources1
Modified residuei5762PhosphoserineCombined sources1
Modified residuei5763PhosphoserineCombined sources1
Modified residuei5780PhosphoserineCombined sources1
Modified residuei5782PhosphoserineCombined sources1
Modified residuei5790PhosphoserineCombined sources1
Modified residuei5793PhosphoserineCombined sources1
Modified residuei5794PhosphothreonineCombined sources1
Modified residuei5824PhosphothreonineCombined sources1
Modified residuei5830PhosphoserineCombined sources1
Modified residuei5841PhosphoserineCombined sources1
Modified residuei5845PhosphothreonineCombined sources1
Modified residuei5851PhosphoserineCombined sources1
Modified residuei5857PhosphoserineCombined sources1
Modified residuei5863PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ09666.
MaxQBiQ09666.
PaxDbiQ09666.
PeptideAtlasiQ09666.
PRIDEiQ09666.

PTM databases

iPTMnetiQ09666.
PhosphoSitePlusiQ09666.
SwissPalmiQ09666.

Expressioni

Gene expression databases

BgeeiENSG00000124942.
CleanExiHS_AHNAK.
ExpressionAtlasiQ09666. baseline and differential.
GenevisibleiQ09666. HS.

Organism-specific databases

HPAiHPA019010.
HPA019070.
HPA026643.

Interactioni

Subunit structurei

Interacts with DYSF; the interaction is direct and Ca2+-independent.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005333EBI-2555881,EBI-297353
NOL9Q5SY163EBI-10245106,EBI-1055462

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • S100 protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122494. 103 interactors.
IntActiQ09666. 42 interactors.
MINTiMINT-4998803.
STRINGi9606.ENSP00000367263.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4DRWX-ray3.50E/F5654-5673[»]
4FTGX-ray2.51E5654-5673[»]
4HRGX-ray2.00C/D5655-5668[»]
ProteinModelPortaliQ09666.
SMRiQ09666.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 90PDZPROSITE-ProRule annotationAdd BLAST82

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi4971 – 4979Nuclear localization signalSequence analysis9
Motifi5019 – 5027Nuclear localization signalSequence analysis9
Motifi5034 – 5039Nuclear localization signalSequence analysis6
Motifi5706 – 5716Nuclear localization signalSequence analysisAdd BLAST11
Motifi5772 – 5779Nuclear localization signalSequence analysis8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi5458 – 5654Gly-richAdd BLAST197

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410JR2V. Eukaryota.
ENOG410ZVP4. LUCA.
GeneTreeiENSGT00530000063716.
HOGENOMiHOG000033865.
HOVERGENiHBG104864.
InParanoidiQ09666.
OMAiFKMPNIK.
OrthoDBiEOG091G01FG.
PhylomeDBiQ09666.
TreeFamiTF350595.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
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