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Protein

Alpha-actinin-2

Gene

ACTN2

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

Functioni

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi766 – 7771; possibly ancestralAdd BLAST12
Calcium bindingi802 – 8132; possibly ancestralAdd BLAST12

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • cytoskeletal protein binding Source: UniProtKB
  • FATZ binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • integrin binding Source: UniProtKB
  • ion channel binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • structural constituent of muscle Source: ProtInc
  • thyroid hormone receptor coactivator activity Source: Ensembl
  • titin binding Source: BHF-UCL
  • titin Z domain binding Source: UniProtKB

GO - Biological processi

  • actin filament uncapping Source: UniProtKB
  • cardiac muscle cell development Source: Ensembl
  • cell adhesion Source: UniProtKB
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • focal adhesion assembly Source: UniProtKB
  • MAPK cascade Source: Reactome
  • microspike assembly Source: UniProtKB
  • muscle filament sliding Source: Reactome
  • negative regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  • negative regulation of potassium ion transport Source: BHF-UCL
  • negative regulation of protein localization to cell surface Source: BHF-UCL
  • phospholipase C-activating angiotensin-activated signaling pathway Source: UniProtKB
  • platelet degranulation Source: Reactome
  • positive regulation of cation channel activity Source: UniProtKB
  • positive regulation of endocytic recycling Source: UniProtKB
  • positive regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  • positive regulation of potassium ion transport Source: BHF-UCL
  • protein homotetramerization Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • regulation of membrane potential Source: BHF-UCL
  • sarcomere organization Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000077522-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-373753. Nephrin interactions.
R-HSA-390522. Striated Muscle Contraction.
R-HSA-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-HSA-442729. CREB phosphorylation through the activation of CaMKII.
R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-HSA-5673001. RAF/MAP kinase cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-actinin-2
Alternative name(s):
Alpha-actinin skeletal muscle isoform 2
F-actin cross-linking protein
Gene namesi
Name:ACTN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:164. ACTN2.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: ProtInc
  • cortical actin cytoskeleton Source: Ensembl
  • cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • dendritic spine Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • filopodium Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • platelet alpha granule lumen Source: Reactome
  • pseudopodium Source: UniProtKB
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Cardiomyopathy, familial hypertrophic 23, with or without left ventricular non-compaction (CMH23)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.
See also OMIM:612158
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071970119A → T in CMH23 and CMD1AA. 2 PublicationsCorresponds to variant rs727502886dbSNPEnsembl.1
Natural variantiVAR_074292228M → T in CMH23. 1 PublicationCorresponds to variant rs786205144dbSNPEnsembl.1
Natural variantiVAR_071971495T → M in CMH23. 1 PublicationCorresponds to variant rs200248944dbSNPEnsembl.1
Natural variantiVAR_071972583E → A in CMH23. 1 PublicationCorresponds to variant rs200631005dbSNPEnsembl.1
Natural variantiVAR_071973628E → G in CMH23. 1 PublicationCorresponds to variant rs786204951dbSNPEnsembl.1
Cardiomyopathy, dilated 1AA, with or without left ventricular non-compaction (CMD1AA)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:612158
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0546289Q → R in CMD1AA. 1 PublicationCorresponds to variant rs121434525dbSNPEnsembl.1
Natural variantiVAR_071970119A → T in CMH23 and CMD1AA. 2 PublicationsCorresponds to variant rs727502886dbSNPEnsembl.1

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

DisGeNETi88.
MalaCardsiACTN2.
MIMi612158. phenotype.
OpenTargetsiENSG00000077522.
Orphaneti154. Familial isolated dilated cardiomyopathy.
PharmGKBiPA25.

Polymorphism and mutation databases

DMDMi543742.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000734351 – 894Alpha-actinin-2Add BLAST894

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei237PhosphothreonineBy similarity1

Post-translational modificationi

Ubiquitinated by FBXL22, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP35609.
MaxQBiP35609.
PaxDbiP35609.
PeptideAtlasiP35609.
PRIDEiP35609.

PTM databases

iPTMnetiP35609.
PhosphoSitePlusiP35609.
SwissPalmiP35609.

Expressioni

Tissue specificityi

Expressed in both skeletal and cardiac muscle.

Gene expression databases

BgeeiENSG00000077522.
CleanExiHS_ACTN2.
ExpressionAtlasiP35609. baseline and differential.
GenevisibleiP35609. HS.

Organism-specific databases

HPAiHPA006035.
HPA008315.

Interactioni

Subunit structurei

Homodimer; antiparallel. Also forms heterodimers with ACTN3. Interacts with ADAM12, MYOZ1, MYOZ2 and MYOZ3. Interacts via its C-terminal region with the LDB3 PDZ domain. Interacts with XIRP2. Interacts with DST isoform 1 (via N-terminus). Interacts with PARVB.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-77797,EBI-77797
Adam12Q618243EBI-77797,EBI-77785From a different organism.
ANGP039504EBI-77797,EBI-525291
APPL1Q9UKG12EBI-77797,EBI-741243
BRMS1LQ5PSV45EBI-77797,EBI-5666615
CSRP3P504614EBI-77797,EBI-5658719
DISC1Q9NRI53EBI-77797,EBI-529989
DYSFO759232EBI-77797,EBI-2799016
KCNA5P224606EBI-77797,EBI-6426121
MICALL2Q8IY335EBI-77797,EBI-2555563
MOSP005403EBI-77797,EBI-1757866
MYOM2P542962EBI-77797,EBI-5357134
MYOZ2Q9NPC66EBI-77797,EBI-746712
NRAPQ86VF72EBI-77797,EBI-5660292
PDLIM3Q53GG54EBI-77797,EBI-5658852
RTP5Q14D335EBI-77797,EBI-10217913
SAXO1Q8IYX73EBI-77797,EBI-3957636
SNAI1O958635EBI-77797,EBI-1045459
SP100P234975EBI-77797,EBI-751145
TTNQ8WZ4216EBI-77797,EBI-681210

GO - Molecular functioni

  • cytoskeletal protein binding Source: UniProtKB
  • FATZ binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • integrin binding Source: UniProtKB
  • ion channel binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • titin binding Source: BHF-UCL
  • titin Z domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106603. 60 interactors.
DIPiDIP-383N.
IntActiP35609. 51 interactors.
MINTiMINT-145583.
STRINGi9606.ENSP00000355537.

Structurei

Secondary structure

1894
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 29Combined sources9
Helixi36 – 52Combined sources17
Helixi53 – 55Combined sources3
Turni62 – 68Combined sources7
Helixi70 – 80Combined sources11
Beta strandi90 – 92Combined sources3
Helixi93 – 110Combined sources18
Helixi119 – 123Combined sources5
Helixi127 – 142Combined sources16
Turni143 – 145Combined sources3
Helixi153 – 164Combined sources12
Turni165 – 167Combined sources3
Beta strandi175 – 177Combined sources3
Helixi178 – 180Combined sources3
Helixi184 – 193Combined sources10
Helixi195 – 197Combined sources3
Helixi200 – 202Combined sources3
Helixi208 – 223Combined sources16
Helixi231 – 236Combined sources6
Beta strandi237 – 239Combined sources3
Helixi242 – 256Combined sources15
Helixi275 – 294Combined sources20
Helixi296 – 303Combined sources8
Beta strandi311 – 313Combined sources3
Turni314 – 317Combined sources4
Helixi318 – 329Combined sources12
Helixi331 – 340Combined sources10
Turni341 – 343Combined sources3
Helixi344 – 347Combined sources4
Turni351 – 356Combined sources6
Helixi364 – 366Combined sources3
Beta strandi368 – 370Combined sources3
Helixi371 – 382Combined sources12
Beta strandi389 – 392Combined sources4
Helixi393 – 416Combined sources24
Turni417 – 419Combined sources3
Helixi420 – 425Combined sources6
Helixi428 – 430Combined sources3
Helixi434 – 470Combined sources37
Helixi476 – 536Combined sources61
Turni537 – 540Combined sources4
Turni548 – 550Combined sources3
Helixi551 – 562Combined sources12
Helixi564 – 588Combined sources25
Helixi604 – 632Combined sources29
Turni666 – 669Combined sources4
Helixi672 – 704Combined sources33
Helixi716 – 741Combined sources26
Helixi753 – 762Combined sources10
Beta strandi767 – 770Combined sources4
Helixi777 – 784Combined sources8
Helixi794 – 799Combined sources6
Helixi812 – 820Combined sources9
Helixi828 – 835Combined sources8
Turni836 – 840Combined sources5
Beta strandi841 – 843Combined sources3
Helixi847 – 853Combined sources7
Helixi856 – 865Combined sources10
Beta strandi871 – 873Combined sources3
Helixi881 – 888Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H8BNMR-A822-894[»]
1HCIX-ray2.80A/B274-746[»]
1QUUX-ray2.50A391-637[»]
4D1EX-ray3.50A19-894[»]
5A36X-ray2.00A/B19-266[»]
5A37X-ray1.88A/B19-266[»]
5A38X-ray1.90A/B19-266[»]
5A4BX-ray2.01A/B19-266[»]
ProteinModelPortaliP35609.
SMRiP35609.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35609.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 254Actin-bindingAdd BLAST254
Domaini38 – 142CH 1PROSITE-ProRule annotationAdd BLAST105
Domaini151 – 254CH 2PROSITE-ProRule annotationAdd BLAST104
Repeati281 – 391Spectrin 1Add BLAST111
Repeati401 – 506Spectrin 2Add BLAST106
Repeati516 – 627Spectrin 3Add BLAST112
Repeati637 – 740Spectrin 4Add BLAST104
Domaini753 – 788EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini789 – 824EF-hand 2PROSITE-ProRule annotationAdd BLAST36

Sequence similaritiesi

Belongs to the alpha-actinin family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 4 spectrin repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiP35609.
KOiK05699.
OMAiAKWDKVK.
OrthoDBiEOG091G020R.
PhylomeDBiP35609.
TreeFamiTF352676.

Family and domain databases

CDDicd00014. CH. 2 hits.
cd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR002048. EF_hand_dom.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35609-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MNQIEPGVQY NYVYDEDEYM IQEEEWDRDL LLDPAWEKQQ RKTFTAWCNS
60 70 80 90 100
HLRKAGTQIE NIEEDFRNGL KLMLLLEVIS GERLPKPDRG KMRFHKIANV
110 120 130 140 150
NKALDYIASK GVKLVSIGAE EIVDGNVKMT LGMIWTIILR FAIQDISVEE
160 170 180 190 200
TSAKEGLLLW CQRKTAPYRN VNIQNFHTSW KDGLGLCALI HRHRPDLIDY
210 220 230 240 250
SKLNKDDPIG NINLAMEIAE KHLDIPKMLD AEDIVNTPKP DERAIMTYVS
260 270 280 290 300
CFYHAFAGAE QAETAANRIC KVLAVNQENE RLMEEYERLA SELLEWIRRT
310 320 330 340 350
IPWLENRTPE KTMQAMQKKL EDFRDYRRKH KPPKVQEKCQ LEINFNTLQT
360 370 380 390 400
KLRISNRPAF MPSEGKMVSD IAGAWQRLEQ AEKGYEEWLL NEIRRLERLE
410 420 430 440 450
HLAEKFRQKA STHETWAYGK EQILLQKDYE SASLTEVRAL LRKHEAFESD
460 470 480 490 500
LAAHQDRVEQ IAAIAQELNE LDYHDAVNVN DRCQKICDQW DRLGTLTQKR
510 520 530 540 550
REALERMEKL LETIDQLHLE FAKRAAPFNN WMEGAMEDLQ DMFIVHSIEE
560 570 580 590 600
IQSLITAHEQ FKATLPEADG ERQSIMAIQN EVEKVIQSYN IRISSSNPYS
610 620 630 640 650
TVTMDELRTK WDKVKQLVPI RDQSLQEELA RQHANERLRR QFAAQANAIG
660 670 680 690 700
PWIQNKMEEI ARSSIQITGA LEDQMNQLKQ YEHNIINYKN NIDKLEGDHQ
710 720 730 740 750
LIQEALVFDN KHTNYTMEHI RVGWELLLTT IARTINEVET QILTRDAKGI
760 770 780 790 800
TQEQMNEFRA SFNHFDRRKN GLMDHEDFRA CLISMGYDLG EAEFARIMTL
810 820 830 840 850
VDPNGQGTVT FQSFIDFMTR ETADTDTAEQ VIASFRILAS DKPYILAEEL
860 870 880 890
RRELPPDQAQ YCIKRMPAYS GPGSVPGALD YAAFSSALYG ESDL
Length:894
Mass (Da):103,854
Last modified:June 1, 1994 - v1
Checksum:i7F612C1C3B3E2299
GO
Isoform 2 (identifier: P35609-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     234-261: IVNTPKPDERAIMTYVSCFYHAFAGAEQ → LVYTARPDERAIMTYVSCYYHAFAGAQK

Note: No experimental confirmation available.
Show »
Length:894
Mass (Da):103,920
Checksum:iBA180F6305E25A8D
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0546289Q → R in CMD1AA. 1 PublicationCorresponds to variant rs121434525dbSNPEnsembl.1
Natural variantiVAR_071970119A → T in CMH23 and CMD1AA. 2 PublicationsCorresponds to variant rs727502886dbSNPEnsembl.1
Natural variantiVAR_074292228M → T in CMH23. 1 PublicationCorresponds to variant rs786205144dbSNPEnsembl.1
Natural variantiVAR_071971495T → M in CMH23. 1 PublicationCorresponds to variant rs200248944dbSNPEnsembl.1
Natural variantiVAR_071972583E → A in CMH23. 1 PublicationCorresponds to variant rs200631005dbSNPEnsembl.1
Natural variantiVAR_033487604M → V.1 PublicationCorresponds to variant rs35997569dbSNPEnsembl.1
Natural variantiVAR_071973628E → G in CMH23. 1 PublicationCorresponds to variant rs786204951dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054923234 – 261IVNTP…AGAEQ → LVYTARPDERAIMTYVSCYY HAFAGAQK in isoform 2. 1 PublicationAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86406 mRNA. Translation: AAA51583.1.
M86804 Genomic DNA. Translation: AAA51584.1.
AJ249756
, AJ249757, AJ249758, AJ249759, AJ249760, AJ249761, AJ249762, AJ249763, AJ249764, AJ249765, AJ249766, AJ249767, AJ249768, AJ249769, AJ249770, AJ249771, AJ249772, AJ249773, AJ249774, AJ249775, AJ249776 Genomic DNA. Translation: CAB61269.1.
AK315250 mRNA. Translation: BAG37672.1.
AL359185, AL359921 Genomic DNA. Translation: CAH73201.1.
AL359921, AL359185 Genomic DNA. Translation: CAI13778.1.
CH471098 Genomic DNA. Translation: EAW70064.1.
CH471098 Genomic DNA. Translation: EAW70065.1.
BC047901 mRNA. Translation: AAH47901.2.
BC051770 mRNA. Translation: AAH51770.2.
CCDSiCCDS1613.1. [P35609-1]
CCDS60455.1. [P35609-2]
PIRiA40199. FAHUA2.
RefSeqiNP_001094.1. NM_001103.3. [P35609-1]
NP_001265272.1. NM_001278343.1. [P35609-2]
NP_001265273.1. NM_001278344.1.
UniGeneiHs.498178.

Genome annotation databases

EnsembliENST00000366578; ENSP00000355537; ENSG00000077522. [P35609-1]
ENST00000542672; ENSP00000443495; ENSG00000077522. [P35609-2]
GeneIDi88.
KEGGihsa:88.
UCSCiuc001hyf.4. human. [P35609-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86406 mRNA. Translation: AAA51583.1.
M86804 Genomic DNA. Translation: AAA51584.1.
AJ249756
, AJ249757, AJ249758, AJ249759, AJ249760, AJ249761, AJ249762, AJ249763, AJ249764, AJ249765, AJ249766, AJ249767, AJ249768, AJ249769, AJ249770, AJ249771, AJ249772, AJ249773, AJ249774, AJ249775, AJ249776 Genomic DNA. Translation: CAB61269.1.
AK315250 mRNA. Translation: BAG37672.1.
AL359185, AL359921 Genomic DNA. Translation: CAH73201.1.
AL359921, AL359185 Genomic DNA. Translation: CAI13778.1.
CH471098 Genomic DNA. Translation: EAW70064.1.
CH471098 Genomic DNA. Translation: EAW70065.1.
BC047901 mRNA. Translation: AAH47901.2.
BC051770 mRNA. Translation: AAH51770.2.
CCDSiCCDS1613.1. [P35609-1]
CCDS60455.1. [P35609-2]
PIRiA40199. FAHUA2.
RefSeqiNP_001094.1. NM_001103.3. [P35609-1]
NP_001265272.1. NM_001278343.1. [P35609-2]
NP_001265273.1. NM_001278344.1.
UniGeneiHs.498178.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H8BNMR-A822-894[»]
1HCIX-ray2.80A/B274-746[»]
1QUUX-ray2.50A391-637[»]
4D1EX-ray3.50A19-894[»]
5A36X-ray2.00A/B19-266[»]
5A37X-ray1.88A/B19-266[»]
5A38X-ray1.90A/B19-266[»]
5A4BX-ray2.01A/B19-266[»]
ProteinModelPortaliP35609.
SMRiP35609.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106603. 60 interactors.
DIPiDIP-383N.
IntActiP35609. 51 interactors.
MINTiMINT-145583.
STRINGi9606.ENSP00000355537.

PTM databases

iPTMnetiP35609.
PhosphoSitePlusiP35609.
SwissPalmiP35609.

Polymorphism and mutation databases

DMDMi543742.

Proteomic databases

EPDiP35609.
MaxQBiP35609.
PaxDbiP35609.
PeptideAtlasiP35609.
PRIDEiP35609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366578; ENSP00000355537; ENSG00000077522. [P35609-1]
ENST00000542672; ENSP00000443495; ENSG00000077522. [P35609-2]
GeneIDi88.
KEGGihsa:88.
UCSCiuc001hyf.4. human. [P35609-1]

Organism-specific databases

CTDi88.
DisGeNETi88.
GeneCardsiACTN2.
GeneReviewsiACTN2.
HGNCiHGNC:164. ACTN2.
HPAiHPA006035.
HPA008315.
MalaCardsiACTN2.
MIMi102573. gene.
612158. phenotype.
neXtProtiNX_P35609.
OpenTargetsiENSG00000077522.
Orphaneti154. Familial isolated dilated cardiomyopathy.
PharmGKBiPA25.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiP35609.
KOiK05699.
OMAiAKWDKVK.
OrthoDBiEOG091G020R.
PhylomeDBiP35609.
TreeFamiTF352676.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000077522-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-373753. Nephrin interactions.
R-HSA-390522. Striated Muscle Contraction.
R-HSA-438066. Unblocking of NMDA receptor, glutamate binding and activation.
R-HSA-442729. CREB phosphorylation through the activation of CaMKII.
R-HSA-442982. Ras activation uopn Ca2+ infux through NMDA receptor.
R-HSA-5673001. RAF/MAP kinase cascade.

Miscellaneous databases

ChiTaRSiACTN2. human.
EvolutionaryTraceiP35609.
GeneWikiiActinin,_alpha_2.
GenomeRNAii88.
PROiP35609.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000077522.
CleanExiHS_ACTN2.
ExpressionAtlasiP35609. baseline and differential.
GenevisibleiP35609. HS.

Family and domain databases

CDDicd00014. CH. 2 hits.
cd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR002048. EF_hand_dom.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACTN2_HUMAN
AccessioniPrimary (citable) accession number: P35609
Secondary accession number(s): B1ANE4
, B2RCS5, Q86TF4, Q86TI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 30, 2016
This is version 188 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.