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UniProtKB - Q13976 (KGP1_HUMAN)

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Protein

cGMP-dependent protein kinase 1

Gene

PRKG1

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

Functioni

Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca2+ release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca2+ levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

In the absence of cGMP, PRKG1 activity is suppressed by autoinhibitory contacts.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei282cGMP 2Combined sources2 Publications1
Binding sitei336cAMP or cGMP 2Combined sources2 Publications1
Binding sitei390ATPPROSITE-ProRule annotation1
Active sitei484Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi167 – 170cAMP or cGMP 1Combined sources1 Publication4
Nucleotide bindingi177 – 178cAMP or cGMP 1Combined sources1 Publication2
Nucleotide bindingi291 – 294cAMP or cGMP 2Combined sources2 Publications4
Nucleotide bindingi301 – 302cAMP or cGMP 2Combined sources2 Publications2
Nucleotide bindingi366 – 374ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium channel regulator activity Source: UniProtKB
  • cGMP binding Source: UniProtKB-KW
  • cGMP-dependent protein kinase activity Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein kinase activity Source: BHF-UCL
  • protein serine/threonine kinase activity Source: Reactome
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • actin cytoskeleton organization Source: ProtInc
  • cGMP-mediated signaling Source: Ensembl
  • dendrite development Source: Ensembl
  • forebrain development Source: Ensembl
  • negative regulation of platelet aggregation Source: UniProtKB
  • negative regulation of vascular associated smooth muscle cell migration Source: BHF-UCL
  • negative regulation of vascular smooth muscle cell proliferation Source: BHF-UCL
  • neuron migration Source: Ensembl
  • protein phosphorylation Source: ProtInc
  • regulation of GTPase activity Source: UniProtKB
  • relaxation of vascular smooth muscle Source: Ensembl
  • signal transduction Source: ProtInc
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionAllosteric enzyme, Kinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, cGMP, cGMP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.12 2681
ReactomeiR-HSA-392517 Rap1 signalling
R-HSA-4086398 Ca2+ pathway
R-HSA-418457 cGMP effects
SABIO-RKiQ13976
SignaLinkiQ13976
SIGNORiQ13976

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-dependent protein kinase 1 (EC:2.7.11.12)
Short name:
cGK 1
Short name:
cGK1
Alternative name(s):
cGMP-dependent protein kinase I
Short name:
cGKI
Gene namesi
Name:PRKG1
Synonyms:PRKG1B, PRKGR1A, PRKGR1B
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 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000185532.15
HGNCiHGNC:9414 PRKG1
MIMi176894 gene
neXtProtiNX_Q13976

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

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Aortic aneurysm, familial thoracic 8 (AAT8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.
See also OMIM:615436
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070434177R → Q in AAT8; impairs cGMP binding; the mutant protein is constitutively active. 1 PublicationCorresponds to variant dbSNP:rs397515330EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi12L → A: Loss of binding to PPP1R12A. 1 Publication1
Mutagenesisi19I → A: Loss of binding to PPP1R12A. 1 Publication1
Mutagenesisi26L → P: Loss of binding to PPP1R12A. 1 Publication1
Mutagenesisi33I → A: Loss of binding to PPP1R12A. 1 Publication1
Mutagenesisi40L → A: Loss of binding to PPP1R12A. 1 Publication1
Mutagenesisi281L → A: Reduces cGMP binding affinity. 1 Publication1
Mutagenesisi282R → A: Reduces cGMP binding affinity. 1 Publication1
Mutagenesisi302T → A: Reduces cGMP binding affinity. 1 Publication1
Mutagenesisi336Y → A: Reduces cGMP binding affinity. 1 Publication1

Keywords - Diseasei

Aortic aneurysm, Disease mutation

Organism-specific databases

DisGeNETi5592
MalaCardsiPRKG1
MIMi615436 phenotype
OpenTargetsiENSG00000185532
Orphaneti91387 Familial thoracic aortic aneurysm and aortic dissection
PharmGKBiPA33777

Chemistry databases

ChEMBLiCHEMBL4273
GuidetoPHARMACOLOGYi1492

Polymorphism and mutation databases

BioMutaiPRKG1
DMDMi6225588

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000861152 – 671cGMP-dependent protein kinase 1Add BLAST670

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Disulfide bondi43InterchainBy similarity
Modified residuei59Phosphothreonine; by autocatalysisBy similarity1
Modified residuei515PhosphothreonineBy similarity1

Post-translational modificationi

Autophosphorylation increases kinase activity.
65 kDa monomer is produced by proteolytic cleavage.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ13976
MaxQBiQ13976
PeptideAtlasiQ13976
PRIDEiQ13976
ProteomicsDBi59781
59782 [Q13976-2]

PTM databases

iPTMnetiQ13976
PhosphoSitePlusiQ13976

Expressioni

Tissue specificityi

Primarily expressed in lung and placenta.1 Publication

Gene expression databases

BgeeiENSG00000185532
CleanExiHS_PRKG1
ExpressionAtlasiQ13976 baseline and differential
GenevisibleiQ13976 HS

Organism-specific databases

HPAiCAB009629
HPA007699

Interactioni

Subunit structurei

Isoform alpha: parallel homodimer or heterodimer and also heterotetramer. Interacts directly with PPP1R12A. Non-covalent dimer of dimer of PRKG1-PRKG1 and PPP1R12A-PPP1R12A. This interaction targets PRKG1 to stress fibers to mediate smooth muscle cell relaxation and vasodilation in responses to rises in cGMP. Isoform beta: antiparallel homodimer. Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1 (By similarity). Interacts with MRVI1. Forms a stable complex with ITPR1, MRVI1, and isoform beta of PRKG1. Interacts with TRPC7 (via ankyrin repeat domain). Isoform alpha interacts with RGS2. Interacts with GTF2I.By similarity9 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi111578, 26 interactors
DIPiDIP-41118N
DIP-46288N
IntActiQ13976, 12 interactors
MINTiQ13976

Chemistry databases

BindingDBiQ13976

Structurei

Secondary structure

1671
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 44Combined sources42
Helixi88 – 100Combined sources13
Turni102 – 106Combined sources5
Helixi109 – 118Combined sources10
Beta strandi120 – 124Combined sources5
Beta strandi129 – 131Combined sources3
Beta strandi139 – 145Combined sources7
Beta strandi148 – 152Combined sources5
Beta strandi155 – 160Combined sources6
Beta strandi165 – 167Combined sources3
Helixi169 – 173Combined sources5
Beta strandi174 – 176Combined sources3
Beta strandi178 – 185Combined sources8
Beta strandi187 – 193Combined sources7
Helixi194 – 201Combined sources8
Helixi209 – 217Combined sources9
Helixi220 – 222Combined sources3
Helixi227 – 236Combined sources10
Beta strandi238 – 242Combined sources5
Beta strandi247 – 249Combined sources3
Beta strandi257 – 264Combined sources8
Beta strandi266 – 270Combined sources5
Beta strandi274 – 276Combined sources3
Beta strandi279 – 284Combined sources6
Helixi292 – 296Combined sources5
Beta strandi297 – 300Combined sources4
Beta strandi303 – 317Combined sources15
Helixi318 – 325Combined sources8
Turni326 – 329Combined sources4
Helixi330 – 349Combined sources20

3D structure databases

ProteinModelPortaliQ13976
SMRiQ13976
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13976

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini360 – 619Protein kinasePROSITE-ProRule annotationAdd BLAST260
Domaini620 – 671AGC-kinase C-terminalAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 102Required for dimerizationAdd BLAST101
Regioni9 – 44Leucine-zipperAdd BLAST36
Regioni50 – 75Autoinhibitory domainBy similarityAdd BLAST26
Regioni103 – 220cGMP-binding, high affinityAdd BLAST118
Regioni221 – 341cGMP-binding, low affinityAdd BLAST121

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili2 – 591 PublicationAdd BLAST58

Domaini

Composed of an N-terminal leucine-zipper domain followed by an autoinhibitory domain, which mediate homodimer formation and inhibit kinase activity, respectively. Next, two cGMP-binding domains are followed by the catalytic domain at the C-terminus. Binding of cGMP to cGMP-binding domains results in a conformational change that activates kinase activity by removing the autoinhibitory domain from the catalytic cleft leaving the catalytic domain free to phosphorylate downstream substrates. Isoforms alpha and beta have identical cGMP-binding and catalytic domains but differ in their leucine zipper and autoinhibitory sequences and therefore differ in their dimerization substrates and kinase enzyme activity.
Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase.

Sequence similaritiesi

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cGMP subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00810000125385
HOGENOMiHOG000233033
HOVERGENiHBG006211
InParanoidiQ13976
KOiK07376
OMAiEPQTHQD
OrthoDBiEOG091G0S9R
PhylomeDBiQ13976
TreeFamiTF313261

Family and domain databases

CDDicd00038 CAP_ED, 2 hits
cd05572 STKc_cGK, 1 hit
Gene3Di2.60.120.10, 2 hits
InterProiView protein in InterPro
IPR000961 AGC-kinase_C
IPR002374 cGMP_dep_kinase
IPR018490 cNMP-bd-like
IPR018488 cNMP-bd_CS
IPR000595 cNMP-bd_dom
IPR011009 Kinase-like_dom_sf
IPR031831 PKcGMP_CC
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR014710 RmlC-like_jellyroll
IPR008271 Ser/Thr_kinase_AS
IPR035014 STKc_cGK
PfamiView protein in Pfam
PF00027 cNMP_binding, 2 hits
PF16808 PKcGMP_CC, 1 hit
PF00069 Pkinase, 1 hit
PIRSFiPIRSF000559 cGMP-dep_kinase, 1 hit
PRINTSiPR00104 CGMPKINASE
SMARTiView protein in SMART
SM00100 cNMP, 2 hits
SM00133 S_TK_X, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF51206 SSF51206, 2 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51285 AGC_KINASE_CTER, 1 hit
PS00888 CNMP_BINDING_1, 2 hits
PS00889 CNMP_BINDING_2, 2 hits
PS50042 CNMP_BINDING_3, 2 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha (identifier: Q13976-1) [UniParc]FASTAAdd to basket
Also known as: CGK1-alpha

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
MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP 
        60         70         80         90        100
STHIGPRTTR AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD 
       110        120        130        140        150
NDFMKNLELS QIQEIVDCMY PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV 
       160        170        180        190        200
TKEGVKLCTM GPGKVFGELA ILYNCTRTAT VKTLVNVKLW AIDRQCFQTI 
       210        220        230        240        250
MMRTGLIKHT EYMEFLKSVP TFQSLPEEIL SKLADVLEET HYENGEYIIR 
       260        270        280        290        300
QGARGDTFFI ISKGTVNVTR EDSPSEDPVF LRTLGKGDWF GEKALQGEDV 
       310        320        330        340        350
RTANVIAAEA VTCLVIDRDS FKHLIGGLDD VSNKAYEDAE AKAKYEAEAA 
       360        370        380        390        400
FFANLKLSDF NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT 
       410        420        430        440        450
RQQEHIRSEK QIMQGAHSDF IVRLYRTFKD SKYLYMLMEA CLGGELWTIL 
       460        470        480        490        500
RDRGSFEDST TRFYTACVVE AFAYLHSKGI IYRDLKPENL ILDHRGYAKL 
       510        520        530        540        550
VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD YWSLGILMYE 
       560        570        580        590        600
LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS 
       610        620        630        640        650
ERLGNLKNGV KDIQKHKWFE GFNWEGLRKG TLTPPIIPSV ASPTDTSNFD 
       660        670 
SFPEDNDEPP PDDNSGWDID F
Length:671
Mass (Da):76,364
Last modified:January 23, 2007 - v3
Checksum:i51389502A5E5FBD2
GO
Isoform Beta (identifier: Q13976-2) [UniParc] [UniParc]FASTAAdd to basket
Also known as: CGK1-beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: MSELEEDFAK...AFRKFTKSER → MGTLRDLQYA...TLPFYPKSPQ

Show »
Length:686
Mass (Da):77,804
Checksum:iA097041AB284F1E6
GO
Isoform 3 (identifier: Q13976-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSELEEDFAKILMLK → MEKQNMFLHGSYILR
     16-297: Missing.

Note: No experimental confirmation available.
Show »
Length:389
Mass (Da):44,185
Checksum:i9792149F93773D55
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070434177R → Q in AAT8; impairs cGMP binding; the mutant protein is constitutively active. 1 PublicationCorresponds to variant dbSNP:rs397515330EnsemblClinVar.1
Natural variantiVAR_046773249I → V1 PublicationCorresponds to variant dbSNP:rs56082459Ensembl.1
Natural variantiVAR_051632267N → S1 PublicationCorresponds to variant dbSNP:rs34997494Ensembl.1
Natural variantiVAR_070435474Y → F1 PublicationCorresponds to variant dbSNP:rs149710600EnsemblClinVar.1
Natural variantiVAR_070436666G → A1 PublicationCorresponds to variant dbSNP:rs750949508EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0387141 – 89MSELE…TKSER → MGTLRDLQYALQEKIEELRQ RDALIDELELELDQKDELIQ KLQNELDKYRSVIRPATQQA QKQSASTLQGEPRTKRQAIS AEPTAFDIQDLSHVTLPFYP KSPQ in isoform Beta. 3 PublicationsAdd BLAST89
Alternative sequenceiVSP_0555411 – 15MSELE…ILMLK → MEKQNMFLHGSYILR in isoform 3. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_05554216 – 297Missing in isoform 3. 1 PublicationAdd BLAST282

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07512 mRNA Translation: CAA68810.1
D45864 mRNA Translation: BAA08297.1
AK093436 mRNA Translation: BAG52715.1
EF560730 mRNA Translation: ABQ59040.1
Z92867
, Z92869, Z92870, Z92871, Z92872, Z92873, Z92874, Z92875, Z92876, Z92877, Z92878, Z92879, Z92880, Z92881, Z92882, Z92883, Z92884, Z92885 Genomic DNA Translation: CAB07436.1
Z92868
, Z92869, Z92870, Z92871, Z92872, Z92873, Z92874, Z92875, Z92876, Z92877, Z92878, Z92879, Z92880, Z92881, Z92882, Z92883, Z92884, Z92885 Genomic DNA Translation: CAB07437.1
AL391378
, AC009986, AC022537, AC022025, AC027118, AL731537, AL928686, AL157399, AC026228 Genomic DNA Translation: CAI39626.1
AL928686
, AC009986, AC022537, AL731537, AL391378, AL157399, AC027118, AC026228, AC022025 Genomic DNA Translation: CAI40743.1
AL157399
, AC022025, AC009986, AL928686, AL731537, AL391378, AC027118, AC026228, AC022537 Genomic DNA Translation: CAI41305.1
AL731537
, AL928686, AL391378, AL157399, AC027118, AC026228, AC022537, AC022025, AC009986 Genomic DNA Translation: CAI17115.1
AC068062 Genomic DNA No translation available.
AC069079 Genomic DNA No translation available.
AC073584 Genomic DNA No translation available.
AL596105 Genomic DNA No translation available.
AL607031 Genomic DNA No translation available.
CH471083 Genomic DNA Translation: EAW54140.1
BC062688 mRNA Translation: AAH62688.1
BC127090 mRNA Translation: AAI27091.1
CCDSiCCDS44399.1 [Q13976-1]
CCDS7244.1 [Q13976-2]
PIRiS05702
RefSeqiNP_001091982.1, NM_001098512.2 [Q13976-1]
NP_006249.1, NM_006258.3 [Q13976-2]
UniGeneiHs.407535

Genome annotation databases

EnsembliENST00000373980; ENSP00000363092; ENSG00000185532 [Q13976-2]
ENST00000373985; ENSP00000363097; ENSG00000185532 [Q13976-1]
ENST00000401604; ENSP00000384200; ENSG00000185532 [Q13976-1]
ENST00000646535; ENSP00000493966; ENSG00000185532 [Q13976-2]
GeneIDi5592
KEGGihsa:5592
UCSCiuc001jjo.4 human [Q13976-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiKGP1_HUMAN
AccessioniPrimary (citable) accession number: Q13976
Secondary accession number(s): A5YM56
, B3KSF3, E2PU10, P14619, Q5JP05, Q5JSJ6, Q6P5T7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 186 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 10
    Human chromosome 10: 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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