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UniProtKB - Q13557 (KCC2D_HUMAN)

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Protein

Calcium/calmodulin-dependent protein kinase type II subunit delta

Gene

CAMK2D

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

Functioni

Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca2+ homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca2+ influx into the myocyte, Ca2+ release from the sarcoplasmic reticulum (SR), SR Ca2+ uptake and Na+ and K+ channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca2+ release via direct phosphorylation of RYR2 Ca2+ channel on 'Ser-2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca2+ influx to myocytes by binding and phosphorylating the L-type Ca2+ channel subunit beta-2 CACNB2. In addition to Ca2+ channels, can target and regulate the cardiac sarcolemmal Na+ channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca2+ uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis. May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca2+ transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor-coupling factor.2 Publications

Miscellaneous

Expression of CAMK2D is significantly increased in patients suffering from dilated cardiomyopathy in PubMed:10189359.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by Ca2+/calmodulin. Binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows autophosphorylation of Thr-287 which turns the kinase in a constitutively active form and confers to the kinase a Ca2+-independent activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43ATPPROSITE-ProRule annotation1
Active sitei136Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi20 – 28ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calmodulin binding Source: BHF-UCL
  • calmodulin-dependent protein kinase activity Source: BHF-UCL
  • identical protein binding Source: IntAct
  • ion channel binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • protein serine/threonine kinase activity Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • sodium channel inhibitor activity Source: BHF-UCL
  • titin binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cardiac muscle cell contraction Source: BHF-UCL
  • cell differentiation Source: GO_Central
  • cellular response to calcium ion Source: BHF-UCL
  • endoplasmic reticulum calcium ion homeostasis Source: BHF-UCL
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • MAPK cascade Source: Reactome
  • negative regulation of sodium ion transmembrane transport Source: BHF-UCL
  • negative regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
  • nervous system development Source: GO_Central
  • peptidyl-serine phosphorylation Source: BHF-UCL
  • peptidyl-threonine phosphorylation Source: BHF-UCL
  • positive regulation of cardiac muscle cell apoptotic process Source: BHF-UCL
  • positive regulation of cardiac muscle hypertrophy Source: UniProtKB
  • protein autophosphorylation Source: BHF-UCL
  • protein complex oligomerization Source: BHF-UCL
  • protein phosphorylation Source: UniProtKB
  • regulation of calcium ion transmembrane transport via high voltage-gated calcium channel Source: BHF-UCL
  • regulation of cardiac muscle cell action potential Source: BHF-UCL
  • regulation of cardiac muscle cell action potential involved in regulation of contraction Source: BHF-UCL
  • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: UniProtKB
  • regulation of cell communication by electrical coupling Source: BHF-UCL
  • regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
  • regulation of cell growth Source: UniProtKB
  • regulation of cellular localization Source: UniProtKB
  • regulation of heart contraction Source: UniProtKB
  • regulation of heart rate by cardiac conduction Source: BHF-UCL
  • regulation of histone deacetylase activity Source: BHF-UCL
  • regulation of membrane depolarization Source: BHF-UCL
  • regulation of relaxation of cardiac muscle Source: BHF-UCL
  • regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  • regulation of ryanodine-sensitive calcium-release channel activity Source: UniProtKB
  • regulation of the force of heart contraction Source: BHF-UCL
  • regulation of transcription by RNA polymerase II Source: BHF-UCL
  • relaxation of cardiac muscle Source: BHF-UCL
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionCalmodulin-binding, Kinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.17 2681
ReactomeiR-HSA-3371571 HSF1-dependent transactivation
R-HSA-399719 Trafficking of AMPA receptors
R-HSA-438066 Unblocking of NMDA receptor, glutamate binding and activation
R-HSA-442729 CREB phosphorylation through the activation of CaMKII
R-HSA-442742 CREB phosphorylation through the activation of Ras
R-HSA-442982 Ras activation upon Ca2+ influx through NMDA receptor
R-HSA-5576892 Phase 0 - rapid depolarisation
R-HSA-5578775 Ion homeostasis
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-877300 Interferon gamma signaling
R-HSA-936837 Ion transport by P-type ATPases
SignaLinkiQ13557
SIGNORiQ13557

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium/calmodulin-dependent protein kinase type II subunit delta (EC:2.7.11.17)
Short name:
CaM kinase II subunit delta
Short name:
CaMK-II subunit delta
Gene namesi
Name:CAMK2D
Synonyms:CAMKD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000145349.16
HGNCiHGNC:1462 CAMK2D
MIMi607708 gene
neXtProtiNX_Q13557

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

DisGeNETi817
OpenTargetsiENSG00000145349
PharmGKBiPA92

Chemistry databases

ChEMBLiCHEMBL2801
GuidetoPHARMACOLOGYi1558

Polymorphism and mutation databases

BioMutaiCAMK2D
DMDMi116242602

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000860992 – 499Calcium/calmodulin-dependent protein kinase type II subunit deltaAdd BLAST498

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei287Phosphothreonine; by autocatalysis1 Publication1
Modified residuei306Phosphothreonine; by autocatalysisCurated1
Modified residuei307Phosphothreonine; by autocatalysisCurated1
Modified residuei315PhosphoserineCombined sources1
Modified residuei318N6-acetyllysineBy similarity1
Modified residuei319PhosphoserineCombined sources1
Modified residuei330PhosphoserineCombined sources1
Modified residuei331PhosphothreonineCombined sources1
Modified residuei333PhosphoserineBy similarity1
Modified residuei336PhosphothreonineBy similarity1
Modified residuei337PhosphothreonineCombined sources1
Modified residuei404PhosphoserineCombined sources1
Modified residuei490PhosphoserineCombined sources1
Modified residuei494PhosphoserineBy similarity1

Post-translational modificationi

Autophosphorylation of Thr-287 following activation by Ca2+/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13557
MaxQBiQ13557
PaxDbiQ13557
PeptideAtlasiQ13557
PRIDEiQ13557
ProteomicsDBi59548
59549 [Q13557-10]
59550 [Q13557-11]
59551 [Q13557-12]
59552 [Q13557-3]
59553 [Q13557-4]
59554 [Q13557-5]
59555 [Q13557-6]
59556 [Q13557-8]
59557 [Q13557-9]

PTM databases

iPTMnetiQ13557
PhosphoSitePlusiQ13557
SwissPalmiQ13557

Expressioni

Tissue specificityi

Expressed in cardiac muscle and skeletal muscle. Isoform Delta 3, isoform Delta 2, isoform Delta 8 and isoform Delta 9 are expressed in cardiac muscle. Isoform Delta 11 is expressed in skeletal muscle.2 Publications

Inductioni

Activity is induced in skeletal muscle during exercise.1 Publication

Gene expression databases

BgeeiENSG00000145349
CleanExiHS_CAMK2D
ExpressionAtlasiQ13557 baseline and differential
GenevisibleiQ13557 HS

Organism-specific databases

HPAiHPA026281
HPA051783
HPA051785
HPA053973

Interactioni

Subunit structurei

CAMK2 is composed of 4 different chains: alpha (CAMK2A), beta (CAMK2B), gamma (CAMK2G), and delta (CAMK2D). The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 12 subunits with two hexameric rings stacked one on top of the other. Interacts with RRAD and CACNB2 (By similarity).By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

  • calmodulin binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • ion channel binding Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • titin binding Source: BHF-UCL
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi107267, 92 interactors
CORUMiQ13557
DIPiDIP-33129N
IntActiQ13557, 101 interactors
MINTiQ13557
STRINGi9606.ENSP00000339740

Chemistry databases

BindingDBiQ13557

Structurei

Secondary structure

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 13Combined sources4
Beta strandi14 – 23Combined sources10
Beta strandi26 – 33Combined sources8
Turni34 – 36Combined sources3
Beta strandi39 – 46Combined sources8
Helixi47 – 49Combined sources3
Helixi52 – 67Combined sources16
Beta strandi76 – 82Combined sources7
Beta strandi85 – 90Combined sources6
Helixi98 – 105Combined sources8
Helixi110 – 129Combined sources20
Helixi139 – 141Combined sources3
Beta strandi142 – 148Combined sources7
Beta strandi153 – 155Combined sources3
Helixi158 – 160Combined sources3
Helixi178 – 180Combined sources3
Helixi183 – 186Combined sources4
Helixi194 – 209Combined sources16
Helixi219 – 228Combined sources10
Turni235 – 240Combined sources6
Helixi243 – 252Combined sources10
Turni257 – 259Combined sources3
Helixi263 – 266Combined sources4
Helixi270 – 273Combined sources4
Helixi275 – 278Combined sources4
Helixi296 – 310Combined sources15
Helixi340 – 363Combined sources24
Helixi366 – 372Combined sources7
Beta strandi373 – 380Combined sources8
Helixi382 – 384Combined sources3
Beta strandi389 – 392Combined sources4
Helixi393 – 401Combined sources9
Beta strandi410 – 421Combined sources12
Beta strandi426 – 438Combined sources13
Beta strandi444 – 458Combined sources15
Beta strandi461 – 470Combined sources10

3D structure databases

ProteinModelPortaliQ13557
SMRiQ13557
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13557

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 272Protein kinasePROSITE-ProRule annotationAdd BLAST259

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni283 – 292Autoinhibitory domainBy similarity10
Regioni291 – 301Calmodulin-bindingBy similarityAdd BLAST11

Domaini

The CAMK2 protein kinases contain a unique C-terminal subunit association domain responsible for oligomerization.

Sequence similaritiesi

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.Curated

Phylogenomic databases

eggNOGiKOG0033 Eukaryota
ENOG410XNRX LUCA
GeneTreeiENSGT00760000118944
HOVERGENiHBG108055
InParanoidiQ13557
KOiK04515
PhylomeDBiQ13557
TreeFamiTF315229

Family and domain databases

InterProiView protein in InterPro
IPR013543 Ca/CaM-dep_prot_kinase-assoc
IPR039071 CAMK2
IPR011009 Kinase-like_dom_sf
IPR032710 NTF2-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PANTHERiPTHR43940 PTHR43940, 2 hits
PfamiView protein in Pfam
PF08332 CaMKII_AD, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF54427 SSF54427, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (10)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 10 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Delta 2 (identifier: Q13557-1) [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
MASTTTCTRF TDEYQLFEEL GKGAFSVVRR CMKIPTGQEY AAKIINTKKL 
        60         70         80         90        100
SARDHQKLER EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE 
       110        120        130        140        150
DIVAREYYSE ADASHCIQQI LESVNHCHLN GIVHRDLKPE NLLLASKSKG 
       160        170        180        190        200
AAVKLADFGL AIEVQGDQQA WFGFAGTPGY LSPEVLRKDP YGKPVDMWAC 
       210        220        230        240        250
GVILYILLVG YPPFWDEDQH RLYQQIKAGA YDFPSPEWDT VTPEAKDLIN 
       260        270        280        290        300
KMLTINPAKR ITASEALKHP WICQRSTVAS MMHRQETVDC LKKFNARRKL 
       310        320        330        340        350
KGAILTTMLA TRNFSAAKSL LKKPDGVKES TESSNTTIED EDVKARKQEI 
       360        370        380        390        400
IKVTEQLIEA INNGDFEAYT KICDPGLTAF EPEALGNLVE GMDFHRFYFE 
       410        420        430        440        450
NALSKSNKPI HTIILNPHVH LVGDDAACIA YIRLTQYMDG SGMPKTMQSE 
       460        470        480        490 
ETRVWHRRDG KWQNVHFHRS GSPTVPIKPP CIPNGKENFS GGTSLWQNI
Length:499
Mass (Da):56,369
Last modified:October 17, 2006 - v3
Checksum:i62999FBAB98120CE
GO
Isoform Delta 3 (identifier: Q13557-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: K → KKRKSSSSVQMM

Show »
Length:510
Mass (Da):57,620
Checksum:i0F312AC0E5938A07
GO
Isoform Delta 4 (identifier: Q13557-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: K → KINNKANVVTSPKENIPTPAL

Show »
Length:519
Mass (Da):58,472
Checksum:i184D4250A261D923
GO
Isoform Delta 6 (identifier: Q13557-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     479-499: Missing.

Show »
Length:478
Mass (Da):54,128
Checksum:i571DA27C914E4F7E
GO
Isoform Delta 7 (identifier: Q13557-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: K → KKRKSSSSVQMM
     479-499: Missing.

Show »
Length:489
Mass (Da):55,378
Checksum:iA45841A7EBFBFA5E
GO
Isoform Delta 8 (identifier: Q13557-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: K → KINNKANVVTSPKENIPTPAL
     479-499: Missing.

Show »
Length:498
Mass (Da):56,230
Checksum:i3EE4353E136343BB
GO
Isoform Delta 9 (identifier: Q13557-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-329: E → EPQTTVIHNPDGNKE

Show »
Length:513
Mass (Da):57,901
Checksum:i79B81366F7E1C69B
GO
Isoform Delta 10 (identifier: Q13557-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-329: E → EPQTTVIHNPDGNKE
     479-499: Missing.

Show »
Length:492
Mass (Da):55,660
Checksum:iE78D0E736590F908
GO
Isoform Delta 11 (identifier: Q13557-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: K → KKRKSSSSVQMMEPQTTVIHNPDGNK

Show »
Length:524
Mass (Da):59,152
Checksum:i3BFC4B5CAF9B3B88
GO
Isoform Delta 12 (identifier: Q13557-12) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     478-478: K → N
     479-499: Missing.

Note: No experimental confirmation available.
Show »
Length:478
Mass (Da):54,114
Checksum:i506DA27C914E4F7E
GO

Sequence cautioni

The sequence BAD92525 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti39E → G in AAD20442 (PubMed:10189359).Curated1
Sequence conflicti272I → T in AAX88806 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040602167D → E1 PublicationCorresponds to variant dbSNP:rs35367671Ensembl.1
Natural variantiVAR_028196463Q → E. Corresponds to variant dbSNP:rs1053668Ensembl.1
Natural variantiVAR_040603493T → I1 PublicationCorresponds to variant dbSNP:rs35765784Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_023095328K → KKRKSSSSVQMMEPQTTVIH NPDGNK in isoform Delta 11. Curated1
Alternative sequenceiVSP_023096328K → KKRKSSSSVQMM in isoform Delta 3 and isoform Delta 7. 1 Publication1
Alternative sequenceiVSP_023097328K → KINNKANVVTSPKENIPTPA L in isoform Delta 4 and isoform Delta 8. Curated1
Alternative sequenceiVSP_023098329E → EPQTTVIHNPDGNKE in isoform Delta 9 and isoform Delta 10. 1 Publication1
Alternative sequenceiVSP_041820478K → N in isoform Delta 12. 1 Publication1
Alternative sequenceiVSP_023099479 – 499Missing in isoform Delta 6, isoform Delta 7, isoform Delta 8, isoform Delta 10 and isoform Delta 12. 4 PublicationsAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071569 mRNA Translation: AAD20442.1
AK055642 mRNA Translation: BAG51545.1
AB209288 mRNA Translation: BAD92525.1 Different initiation.
AY987011 mRNA Translation: AAX88806.1
AC004056 Genomic DNA No translation available.
AC004168 Genomic DNA No translation available.
AC093900 Genomic DNA No translation available.
AC107386 Genomic DNA No translation available.
BC032784 mRNA Translation: AAH32784.1
AJ252239 mRNA Translation: CAB65123.1
U50361 mRNA Translation: AAB16866.1
CCDSiCCDS3703.1 [Q13557-1]
CCDS3704.1 [Q13557-8]
CCDS43263.1 [Q13557-12]
CCDS47127.1 [Q13557-10]
CCDS54797.1 [Q13557-9]
RefSeqiNP_001212.2, NM_001221.3 [Q13557-1]
NP_001308495.1, NM_001321566.1 [Q13557-6]
NP_001308502.1, NM_001321573.1 [Q13557-11]
NP_001308509.1, NM_001321580.1 [Q13557-4]
NP_001308518.1, NM_001321589.1 [Q13557-10]
NP_742112.1, NM_172114.1 [Q13557-10]
NP_742113.1, NM_172115.2 [Q13557-8]
NP_742125.1, NM_172127.2 [Q13557-8]
NP_742126.1, NM_172128.2 [Q13557-12]
NP_742127.1, NM_172129.1 [Q13557-9]
XP_011530591.1, XM_011532289.1 [Q13557-3]
XP_011530593.1, XM_011532291.1 [Q13557-9]
UniGeneiHs.144114

Genome annotation databases

EnsembliENST00000296402; ENSP00000296402; ENSG00000145349 [Q13557-8]
ENST00000342666; ENSP00000339740; ENSG00000145349 [Q13557-1]
ENST00000379773; ENSP00000369098; ENSG00000145349 [Q13557-8]
ENST00000394522; ENSP00000378030; ENSG00000145349 [Q13557-10]
ENST00000394524; ENSP00000378032; ENSG00000145349 [Q13557-12]
ENST00000508738; ENSP00000422566; ENSG00000145349 [Q13557-9]
ENST00000515496; ENSP00000423482; ENSG00000145349 [Q13557-3]
GeneIDi817
KEGGihsa:817
UCSCiuc003ibi.4 human [Q13557-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiKCC2D_HUMAN
AccessioniPrimary (citable) accession number: Q13557
Secondary accession number(s): A8MVS8
, Q52PK4, Q59G21, Q8N553, Q9UGH6, Q9UQE9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: July 18, 2018
This is version 197 of the entry and version 3 of the sequence. See 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 4
    Human chromosome 4: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

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