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Q8IVT5

- KSR1_HUMAN

UniProt

Q8IVT5 - KSR1_HUMAN

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Protein

Kinase suppressor of Ras 1

Gene
KSR1, KSR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Location-regulated scaffolding protein connecting MEK to RAF. Promotes MEK and RAF phosphorylation and activity through assembly of an activated signaling complex. By itself, it has no demonstrated kinase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi348 – 3481Zinc 1 By similarity
Metal bindingi360 – 3601Zinc 2 By similarity
Metal bindingi363 – 3631Zinc 2 By similarity
Metal bindingi373 – 3731Zinc 1 By similarity
Metal bindingi376 – 3761Zinc 1 By similarity
Metal bindingi381 – 3811Zinc 2 By similarity
Metal bindingi384 – 3841Zinc 2 By similarity
Metal bindingi391 – 3911Zinc 1 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri347 – 39145Phorbol-ester/DAG-typeAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: InterPro
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct
  4. protein kinase activity Source: UniProtKB
  5. protein serine/threonine kinase activity Source: InterPro

GO - Biological processi

  1. Ras protein signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ8IVT5.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinase suppressor of Ras 1
Gene namesi
Name:KSR1
Synonyms:KSR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:6465. KSR1.

Subcellular locationi

Cytoplasm. Membrane; Peripheral membrane protein By similarity. Endoplasmic reticulum membrane
Note: In unstimulated cells, where the phosphorylated form is bound to a 14-3-3 protein, sequestration in the cytoplasm occurs. Following growth factor treatment, the protein is free for membrane translocation, and it moves from the cytoplasm to the cell periphery By similarity.1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 923923Kinase suppressor of Ras 1PRO_0000086229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei270 – 2701Phosphothreonine
Modified residuei274 – 2741Phosphothreonine
Modified residuei311 – 3111Phosphoserine
Modified residuei334 – 3341Phosphoserine
Modified residuei406 – 4061Phosphoserine
Modified residuei569 – 5691Phosphoserine

Post-translational modificationi

Phosphorylated on Ser-311 and, to a higher extent, on Ser-406 by MARK3. Dephosphorylated on Ser-406 by PPP2CA. In resting cells, phosphorylated KSR1 is cytoplasmic and in stimulated cells, dephosphorylated KSR1 is membrane-associated By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8IVT5.
PaxDbiQ8IVT5.
PRIDEiQ8IVT5.

PTM databases

PhosphoSiteiQ8IVT5.

Expressioni

Gene expression databases

ArrayExpressiQ8IVT5.
BgeeiQ8IVT5.
CleanExiHS_KSR1.
GenevestigatoriQ8IVT5.

Organism-specific databases

HPAiCAB009623.
HPA011215.

Interactioni

Subunit structurei

Interacts with HSPCA/HSP90, YWHAB/14-3-3, CDC37, MAP2K/MEK, MARK3, PPP2R1A and PPP2CA. Also interacts with RAF and MAPK/ERK, in a Ras-dependent manner By similarity. The binding of 14-3-3 proteins to phosphorylated KSR prevents the membrane localization. Interacts with isoform 1 of VRK2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
VRK2Q86Y074EBI-486984,EBI-1207615

Protein-protein interaction databases

BioGridi114371. 11 interactions.
IntActiQ8IVT5. 17 interactions.
MINTiMINT-87143.
STRINGi9606.ENSP00000268763.

Structurei

3D structure databases

ProteinModelPortaliQ8IVT5.
SMRiQ8IVT5. Positions 25-170, 343-390, 598-906.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini613 – 883271Protein kinaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 215Poly-Gly
Compositional biasi289 – 2924Poly-Pro

Domaini

The protein kinase domain is predicted to be catalytically inactive.

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000113263.
HOVERGENiHBG052293.
InParanoidiQ8IVT5.
KOiK14958.
OMAiEVSPMRF.
OrthoDBiEOG7BP81Z.
PhylomeDBiQ8IVT5.
TreeFamiTF317006.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR025561. KSR_SAM-like_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13543. KSR1-SAM. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8IVT5-1) [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

MDRAALRAAA MGEKKEGGGG GDAAAAEGGA GAAASRALQQ CGQLQKLIDI    50
SIGSLRGLRT KCAVSNDLTQ QEIRTLEAKL VRYICKQRQC KLSVAPGERT 100
PELNSYPRFS DWLYTFNVRP EVVQEIPRDL TLDALLEMNE AKVKETLRRC 150
GASGDECGRL QYALTCLRKV TGLGGEHKED SSWSSLDARR ESGSGPSTDT 200
LSAASLPWPP GSSQLGRAGN SAQGPRSISV SALPASDSPT PSFSEGLSDT 250
CIPLHASGRL TPRALHSFIT PPTTPQLRRH TKLKPPRTPP PPSRKVFQLL 300
PSFPTLTRSK SHESQLGNRI DDVSSMRFDL SHGSPQMVRR DIGLSVTHRF 350
STKSWLSQVC HVCQKSMIFG VKCKHCRLKC HNKCTKEAPA CRISFLPLTR 400
LRRTESVPSD INNPVDRAAE PHFGTLPKAL TKKEHPPAMN HLDSSSNPSS 450
TTSSTPSSPA PFPTSSNPSS ATTPPNPSPG QRDSRFNFPA AYFIHHRQQF 500
IFPVPSAGHC WKCLLIAESL KENAFNISAF AHAAPLPEAA DGTRLDDQPK 550
ADVLEAHEAE AEEPEAGKSE AEDDEDEVDD LPSSRRPWRG PISRKASQTS 600
VYLQEWDIPF EQVELGEPIG QGRWGRVHRG RWHGEVAIRL LEMDGHNQDH 650
LKLFKKEVMN YRQTRHENVV LFMGACMNPP HLAIITSFCK GRTLHSFVRD 700
PKTSLDINKT RQIAQEIIKG MGYLHAKGIV HKDLKSKNVF YDNGKVVITD 750
FGLFGISGVV REGRRENQLK LSHDWLCYLA PEIVREMTPG KDEDQLPFSK 800
AADVYAFGTV WYELQARDWP LKNQAAEASI WQIGSGEGMK RVLTSVSLGK 850
EVSEILSACW AFDLQERPSF SLLMDMLEKL PKLNRRLSHP GHFWKSADIN 900
SSKVVPRFER FGLGVLESSN PKM 923
Length:923
Mass (Da):102,160
Last modified:September 3, 2014 - v3
Checksum:i61BF0F1598349540
GO
Isoform 2 (identifier: Q8IVT5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     504-526: VPSAGHCWKCLLIAESLKENAFN → D
     898-923: DINSSKVVPRFERFGLGVLESSNPKM → EL

Note: No experimental confirmation available.

Show »
Length:877
Mass (Da):97,115
Checksum:iB316183895D9A4BD
GO
Isoform 3 (identifier: Q8IVT5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.

Note: No experimental confirmation available.

Show »
Length:786
Mass (Da):87,344
Checksum:i7BDD722CFE4B87BA
GO
Isoform 4 (identifier: Q8IVT5-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.
     898-923: DINSSKVVPRFERFGLGVLESSNPKM → EL

Note: No experimental confirmation available.

Show »
Length:762
Mass (Da):84,697
Checksum:i3034D20D01F33E66
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti227 – 2271S → P.
VAR_040658
Natural varianti359 – 3591V → A.
VAR_046048
Natural varianti663 – 6631Q → H.
VAR_046049

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 137137Missing in isoform 3 and isoform 4. VSP_055655Add
BLAST
Alternative sequencei504 – 52623VPSAG…ENAFN → D in isoform 2. VSP_055656Add
BLAST
Alternative sequencei898 – 92326DINSS…SNPKM → EL in isoform 2 and isoform 4. VSP_055657Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 26523FSEGL…TPRAL → EFRHTSALTQHTAHTQHTSA HTQ in AAH42106. 1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC069366 Genomic DNA. No translation available.
AC015688 Genomic DNA. No translation available.
BC042106 mRNA. Translation: AAH42106.1.
U43586 mRNA. Translation: AAC50354.1.
RefSeqiNP_055053.1. NM_014238.1.
UniGeneiHs.133534.

Genome annotation databases

EnsembliENST00000268763; ENSP00000268763; ENSG00000141068.
ENST00000319524; ENSP00000323178; ENSG00000141068.
ENST00000398988; ENSP00000381958; ENSG00000141068.
GeneIDi8844.
KEGGihsa:8844.

Polymorphism databases

DMDMi56749095.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC069366 Genomic DNA. No translation available.
AC015688 Genomic DNA. No translation available.
BC042106 mRNA. Translation: AAH42106.1 .
U43586 mRNA. Translation: AAC50354.1 .
RefSeqi NP_055053.1. NM_014238.1.
UniGenei Hs.133534.

3D structure databases

ProteinModelPortali Q8IVT5.
SMRi Q8IVT5. Positions 25-170, 343-390, 598-906.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114371. 11 interactions.
IntActi Q8IVT5. 17 interactions.
MINTi MINT-87143.
STRINGi 9606.ENSP00000268763.

PTM databases

PhosphoSitei Q8IVT5.

Polymorphism databases

DMDMi 56749095.

Proteomic databases

MaxQBi Q8IVT5.
PaxDbi Q8IVT5.
PRIDEi Q8IVT5.

Protocols and materials databases

DNASUi 8844.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268763 ; ENSP00000268763 ; ENSG00000141068 .
ENST00000319524 ; ENSP00000323178 ; ENSG00000141068 .
ENST00000398988 ; ENSP00000381958 ; ENSG00000141068 .
GeneIDi 8844.
KEGGi hsa:8844.

Organism-specific databases

CTDi 8844.
GeneCardsi GC17P025783.
H-InvDB HIX0018394.
HIX0025516.
HIX0029273.
HGNCi HGNC:6465. KSR1.
HPAi CAB009623.
HPA011215.
MIMi 601132. gene.
neXtProti NX_Q8IVT5.
PharmGKBi PA30254.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000113263.
HOVERGENi HBG052293.
InParanoidi Q8IVT5.
KOi K14958.
OMAi EVSPMRF.
OrthoDBi EOG7BP81Z.
PhylomeDBi Q8IVT5.
TreeFami TF317006.

Enzyme and pathway databases

SignaLinki Q8IVT5.

Miscellaneous databases

ChiTaRSi KSR1. human.
GeneWikii KSR1.
GenomeRNAii 8844.
NextBioi 33204.
PROi Q8IVT5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8IVT5.
Bgeei Q8IVT5.
CleanExi HS_KSR1.
Genevestigatori Q8IVT5.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR025561. KSR_SAM-like_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF13543. KSR1-SAM. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
SMARTi SM00109. C1. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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] OF 1-628 (ISOFORM 3).
    Tissue: Brain.
  3. "KSR, a novel protein kinase required for RAS signal transduction."
    Therrien M., Chang H.C., Solomon N.M., Karim F.D., Wassarman D.A., Rubin G.M.
    Cell 83:879-888(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 243-899 (ISOFORM 2).
  4. "MAP kinase module: the Ksr connection."
    Roy F., Therrien M.
    Curr. Biol. 12:R325-R327(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270 AND SER-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270; THR-274; SER-334; SER-406 AND SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "VRK2 inhibits mitogen-activated protein kinase signaling and inversely correlates with ErbB2 in human breast cancer."
    Fernandez I.F., Blanco S., Lozano J., Lazo P.A.
    Mol. Cell. Biol. 30:4687-4697(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VRK2.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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] PRO-227; ALA-359 AND HIS-663.

Entry informationi

Entry nameiKSR1_HUMAN
AccessioniPrimary (citable) accession number: Q8IVT5
Secondary accession number(s): F8WEA9, H7BYU0, Q13476
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: September 3, 2014
Last modified: September 3, 2014
This is version 114 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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