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P78368

- KC1G2_HUMAN

UniProt

P78368 - KC1G2_HUMAN

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Protein

Casein kinase I isoform gamma-2

Gene
CSNK1G2, CK1G2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. Involved in brain development and vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. Regulates fast synaptic transmission mediated by glutamate. SMAD3 phosphorylation promotes its ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Hyperphosphorylation of the serine-repeat motif of COL4A3BP/CERT leads to its inactivation by dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis. Triggers PER1 proteasomal degradation probably through phosphorylation.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Stimulated by estrogen. Repressed by 5-iodotubercidin (DB04604).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei75 – 751ATP By similarity
Active sitei165 – 1651Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi52 – 609ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: Ensembl
  3. peptide binding Source: Ensembl
  4. protein binding Source: UniProtKB
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. protein autophosphorylation Source: Ensembl
  2. protein phosphorylation Source: ProtInc
  3. signal transduction Source: ProtInc
  4. small molecule metabolic process Source: Reactome
  5. sphingolipid biosynthetic process Source: Reactome
  6. sphingolipid metabolic process Source: Reactome
  7. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
SignaLinkiP78368.

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase I isoform gamma-2 (EC:2.7.11.1)
Short name:
CKI-gamma 2
Gene namesi
Name:CSNK1G2
Synonyms:CK1G2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:2455. CSNK1G2.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26955.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415Casein kinase I isoform gamma-2PRO_0000192842Add
BLAST

Post-translational modificationi

Autophosphorylated By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78368.
PaxDbiP78368.
PRIDEiP78368.

PTM databases

PhosphoSiteiP78368.

Expressioni

Tissue specificityi

Testis.

Gene expression databases

ArrayExpressiP78368.
BgeeiP78368.
CleanExiHS_CSNK1G2.
GenevestigatoriP78368.

Organism-specific databases

HPAiHPA034868.

Interactioni

Subunit structurei

Monomer By similarity. Interacts with MTA1 (short isoform) in the cytoplasm. Interacts with SMAD3.2 Publications

Protein-protein interaction databases

BioGridi107839. 12 interactions.
IntActiP78368. 5 interactions.
MINTiMINT-1473562.
STRINGi9606.ENSP00000255641.

Structurei

Secondary structure

1
415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi46 – 516
Beta strandi60 – 656
Turni66 – 683
Beta strandi71 – 788
Helixi86 – 9510
Turni96 – 983
Beta strandi105 – 1117
Beta strandi114 – 1207
Helixi126 – 1327
Turni133 – 1353
Helixi139 – 15820
Helixi168 – 1703
Beta strandi171 – 1733
Turni179 – 1824
Beta strandi183 – 1864
Beta strandi193 – 1964
Turni198 – 2003
Turni216 – 2183
Helixi221 – 2244
Helixi231 – 24717
Turni251 – 2544
Beta strandi257 – 2593
Helixi260 – 27213
Helixi276 – 2794
Turni280 – 2823
Helixi285 – 29511
Helixi305 – 31814
Turni328 – 3314

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C47X-ray2.40A/B/C/D43-353[»]
ProteinModelPortaliP78368.
SMRiP78368. Positions 17-338.

Miscellaneous databases

EvolutionaryTraceiP78368.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 316271Protein kinaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000182054.
HOVERGENiHBG000176.
InParanoidiP78368.
KOiK08958.
OMAiHTKHQVM.
OrthoDBiEOG7G1V66.
PhylomeDBiP78368.
TreeFamiTF313349.

Family and domain databases

InterProiIPR022247. Casein_kinase-1_gamma_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF12605. CK1gamma_C. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P78368-1 [UniParc]FASTAAdd to Basket

« Hide

MDFDKKGGKG ETEEGRRMSK AGGGRSSHGI RSSGTSSGVL MVGPNFRVGK    50
KIGCGNFGEL RLGKNLYTNE YVAIKLEPIK SRAPQLHLEY RFYKQLSATE 100
GVPQVYYFGP CGKYNAMVLE LLGPSLEDLF DLCDRTFTLK TVLMIAIQLI 150
TRMEYVHTKS LIYRDVKPEN FLVGRPGTKR QHAIHIIDFG LAKEYIDPET 200
KKHIPYREHK SLTGTARYMS INTHLGKEQS RRDDLEALGH MFMYFLRGSL 250
PWQGLKADTL KERYQKIGDT KRATPIEVLC ENFPEEMATY LRYVRRLDFF 300
EKPDYDYLRK LFTDLFDRSG FVFDYEYDWA GKPLPTPIGT VHTDLPSQPQ 350
LRDKTQPHSK NQALNSTNGE LNADDPTAGH SNAPITAPAE VEVADETKCC 400
CFFKRRKRKS LQRHK 415
Length:415
Mass (Da):47,457
Last modified:May 1, 1997 - v1
Checksum:i036A39148A1DA038
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti189 – 1891F → L.1 Publication
VAR_042086
Natural varianti194 – 1941E → G.1 Publication
VAR_042087
Natural varianti196 – 1961I → T.1 Publication
VAR_042088
Natural varianti206 – 2061Y → C.1 Publication
VAR_042089
Natural varianti206 – 2061Y → H.1 Publication
VAR_042090
Natural varianti207 – 2071R → S.1 Publication
VAR_042091
Natural varianti208 – 2081E → Q.1 Publication
VAR_042092
Natural varianti217 – 2171R → C.1 Publication
VAR_042093
Natural varianti223 – 2231T → M.1 Publication
VAR_042094

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131K → N in AAP88924. 1 Publication
Sequence conflicti113 – 1131K → N in AAH20972. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U89896 mRNA. Translation: AAB88627.1.
BT009922 mRNA. Translation: AAP88924.1.
AF001177 Transcribed RNA. Translation: AAC00212.1.
AB451278 mRNA. Translation: BAG70092.1.
AB451410 mRNA. Translation: BAG70224.1.
AC005306 Genomic DNA. Translation: AAC26983.1.
CH471139 Genomic DNA. Translation: EAW69430.1.
BC018693 mRNA. Translation: AAH18693.1.
BC018699 mRNA. Translation: AAH18699.1.
BC020972 mRNA. Translation: AAH20972.1.
CCDSiCCDS12077.1.
RefSeqiNP_001310.3. NM_001319.6.
UniGeneiHs.651905.

Genome annotation databases

EnsembliENST00000255641; ENSP00000255641; ENSG00000133275.
GeneIDi1455.
KEGGihsa:1455.
UCSCiuc002lul.4. human.

Polymorphism databases

DMDMi3024060.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U89896 mRNA. Translation: AAB88627.1 .
BT009922 mRNA. Translation: AAP88924.1 .
AF001177 Transcribed RNA. Translation: AAC00212.1 .
AB451278 mRNA. Translation: BAG70092.1 .
AB451410 mRNA. Translation: BAG70224.1 .
AC005306 Genomic DNA. Translation: AAC26983.1 .
CH471139 Genomic DNA. Translation: EAW69430.1 .
BC018693 mRNA. Translation: AAH18693.1 .
BC018699 mRNA. Translation: AAH18699.1 .
BC020972 mRNA. Translation: AAH20972.1 .
CCDSi CCDS12077.1.
RefSeqi NP_001310.3. NM_001319.6.
UniGenei Hs.651905.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C47 X-ray 2.40 A/B/C/D 43-353 [» ]
ProteinModelPortali P78368.
SMRi P78368. Positions 17-338.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107839. 12 interactions.
IntActi P78368. 5 interactions.
MINTi MINT-1473562.
STRINGi 9606.ENSP00000255641.

Chemistry

BindingDBi P78368.
ChEMBLi CHEMBL2543.
GuidetoPHARMACOLOGYi 2000.

PTM databases

PhosphoSitei P78368.

Polymorphism databases

DMDMi 3024060.

Proteomic databases

MaxQBi P78368.
PaxDbi P78368.
PRIDEi P78368.

Protocols and materials databases

DNASUi 1455.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000255641 ; ENSP00000255641 ; ENSG00000133275 .
GeneIDi 1455.
KEGGi hsa:1455.
UCSCi uc002lul.4. human.

Organism-specific databases

CTDi 1455.
GeneCardsi GC19P001941.
HGNCi HGNC:2455. CSNK1G2.
HPAi HPA034868.
MIMi 602214. gene.
neXtProti NX_P78368.
PharmGKBi PA26955.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000182054.
HOVERGENi HBG000176.
InParanoidi P78368.
KOi K08958.
OMAi HTKHQVM.
OrthoDBi EOG7G1V66.
PhylomeDBi P78368.
TreeFami TF313349.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_115810. Sphingolipid de novo biosynthesis.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
SignaLinki P78368.

Miscellaneous databases

ChiTaRSi CSNK1G2. human.
EvolutionaryTracei P78368.
GenomeRNAii 1455.
NextBioi 5975.
PROi P78368.
SOURCEi Search...

Gene expression databases

ArrayExpressi P78368.
Bgeei P78368.
CleanExi HS_CSNK1G2.
Genevestigatori P78368.

Family and domain databases

InterProi IPR022247. Casein_kinase-1_gamma_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF12605. CK1gamma_C. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and chromosomal mapping of human casein kinase I gamma 2 (CSNK1G2)."
    Kitabayashi A.N., Kusuda J., Hirai M., Hashimoto K.
    Genomics 46:133-137(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon and Muscle.
  7. "Polymorphisms of casein kinase I gamma 2 gene associated with simple febrile seizures in Chinese Han population."
    Yinan M., Yu Q., Zhiyue C., Jianjun L., Lie H., Liping Z., Jianhui Z., Fang S., Dingfang B., Qing L., Xiru W.
    Neurosci. Lett. 368:2-6(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BRAIN DEVELOPMENT.
  8. "Metastatic tumor antigen 1 short form (MTA1s) associates with casein kinase I-gamma2, an estrogen-responsive kinase."
    Mishra S.K., Yang Z., Mazumdar A., Talukder A.H., Larose L., Kumar R.
    Oncogene 23:4422-4429(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS MTA1 KINASE, INTERACTION WITH MTA1, SUBCELLULAR LOCATION, ENZYME REGULATION.
  9. "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein."
    Shirogane T., Jin J., Ang X.L., Harper J.W.
    J. Biol. Chem. 280:26863-26872(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PER1 STABILITY.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Ligand-dependent ubiquitination of Smad3 is regulated by casein kinase 1 gamma 2, an inhibitor of TGF-beta signaling."
    Guo X., Waddell D.S., Wang W., Wang Z., Liberati N.T., Yong S., Liu X., Wang X.-F.
    Oncogene 27:7235-7247(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS SMAD3 KINASE, INTERACTION WITH SMAD3.
  12. "Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelin."
    Tomishige N., Kumagai K., Kusuda J., Nishijima M., Hanada K.
    Mol. Biol. Cell 20:348-357(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS COL4A3BP/CERT KINASE.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 43-353 IN COMPLEX WITH 5-IODOTUBERCIDIN.
  16. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-189; GLY-194; THR-196; CYS-206; HIS-206; SER-207; GLN-208; CYS-217 AND MET-223.

Entry informationi

Entry nameiKC1G2_HUMAN
AccessioniPrimary (citable) accession number: P78368
Secondary accession number(s): B5BU42, O00704, Q8WUB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: September 3, 2014
This is version 145 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 19
    Human chromosome 19: 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

External Data

Dasty 3

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