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P10398

- ARAF_HUMAN

UniProt

P10398 - ARAF_HUMAN

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Protein

Serine/threonine-protein kinase A-Raf

Gene
ARAF, ARAF1, PKS, PKS2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade.2 Publications
Isoform 2: Serves as a positive regulator of myogenic differentiation by inducing cell cycle arrest, the expression of myogenin and other muscle-specific proteins, and myotube formation.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Binds 2 zinc ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991Zinc 1 By similarity
Metal bindingi112 – 1121Zinc 2 By similarity
Metal bindingi115 – 1151Zinc 2 By similarity
Metal bindingi125 – 1251Zinc 1 By similarity
Metal bindingi128 – 1281Zinc 1 By similarity
Metal bindingi133 – 1331Zinc 2 By similarity
Metal bindingi136 – 1361Zinc 2 By similarity
Metal bindingi144 – 1441Zinc 1 By similarity
Binding sitei336 – 3361ATP By similarity
Active sitei429 – 4291Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri98 – 14447Phorbol-ester/DAG-typeAdd
BLAST
Nucleotide bindingi316 – 3249ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. negative regulation of apoptotic process Source: UniProtKB
  3. positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  4. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  5. regulation of TOR signaling Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
SignaLinkiP10398.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase A-Raf (EC:2.7.11.1)
Alternative name(s):
Proto-oncogene A-Raf
Proto-oncogene A-Raf-1
Proto-oncogene Pks
Gene namesi
Name:ARAF
Synonyms:ARAF1, PKS, PKS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:646. ARAF.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA24928.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 606606Serine/threonine-protein kinase A-RafPRO_0000085622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861Phosphoserine1 Publication
Modified residuei257 – 2571Phosphoserine1 Publication
Modified residuei318 – 3181Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP10398.
PaxDbiP10398.
PRIDEiP10398.

PTM databases

PhosphoSiteiP10398.

Expressioni

Tissue specificityi

Predominantly in urogenital tissues.

Gene expression databases

ArrayExpressiP10398.
BgeeiP10398.
CleanExiHS_ARAF.
GenevestigatoriP10398.

Interactioni

Subunit structurei

Interacts with TH1L/NELFD.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ASS1P009664EBI-365961,EBI-536842
COPS3Q9UNS23EBI-365961,EBI-350590
CPS1P313273EBI-365961,EBI-536811
EFEMP1Q128053EBI-365961,EBI-536772
HSP90AB1P082383EBI-365961,EBI-352572
IRAK2O431872EBI-365961,EBI-447733
IRF7Q929852EBI-365961,EBI-968267
MAP2K2P365074EBI-365961,EBI-1056930
NELFCDQ8IXH75EBI-365961,EBI-536725
NUDT14O958483EBI-365961,EBI-536866
PBKQ96KB53EBI-365961,EBI-536853
PRPF6O949064EBI-365961,EBI-536755
RABGGTBP536113EBI-365961,EBI-536715
RRAS2P620703EBI-365961,EBI-491037
TIMM44O436153EBI-365961,EBI-861737
TIMM50Q3ZCQ83EBI-365961,EBI-355175
TIRAPP587532EBI-365961,EBI-528644
YWHAZP631043EBI-365961,EBI-347088

Protein-protein interaction databases

BioGridi106864. 43 interactions.
DIPiDIP-31374N.
IntActiP10398. 37 interactions.
MINTiMINT-88835.
STRINGi9606.ENSP00000366244.

Structurei

Secondary structure

1
606
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 246
Beta strandi26 – 283
Beta strandi30 – 345
Helixi42 – 509
Beta strandi56 – 6712
Beta strandi69 – 724
Beta strandi74 – 785
Beta strandi85 – 906

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXMNMR-A19-91[»]
ProteinModelPortaliP10398.
SMRiP10398. Positions 20-91, 96-146, 273-576.

Miscellaneous databases

EvolutionaryTraceiP10398.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 9173RBDAdd
BLAST
Domaini310 – 570261Protein kinaseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000252972.
HOVERGENiHBG001886.
KOiK08845.
OMAiLFHTTRL.
OrthoDBiEOG7F5128.
PhylomeDBiP10398.
TreeFamiTF317006.

Family and domain databases

InterProiIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR003116. Raf-like_ras-bd.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00130. C1_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF02196. RBD. 1 hit.
[Graphical view]
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 1 hit.
SM00455. RBD. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50898. RBD. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P10398-1) [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

MEPPRGPPAN GAEPSRAVGT VKVYLPNKQR TVVTVRDGMS VYDSLDKALK    50
VRGLNQDCCV VYRLIKGRKT VTAWDTAIAP LDGEELIVEV LEDVPLTMHN 100
FVRKTFFSLA FCDFCLKFLF HGFRCQTCGY KFHQHCSSKV PTVCVDMSTN 150
RQQFYHSVQD LSGGSRQHEA PSNRPLNELL TPQGPSPRTQ HCDPEHFPFP 200
APANAPLQRI RSTSTPNVHM VSTTAPMDSN LIQLTGQSFS TDAAGSRGGS 250
DGTPRGSPSP ASVSSGRKSP HSKSPAEQRE RKSLADDKKK VKNLGYRDSG 300
YYWEVPPSEV QLLKRIGTGS FGTVFRGRWH GDVAVKVLKV SQPTAEQAQA 350
FKNEMQVLRK TRHVNILLFM GFMTRPGFAI ITQWCEGSSL YHHLHVADTR 400
FDMVQLIDVA RQTAQGMDYL HAKNIIHRDL KSNNIFLHEG LTVKIGDFGL 450
ATVKTRWSGA QPLEQPSGSV LWMAAEVIRM QDPNPYSFQS DVYAYGVVLY 500
ELMTGSLPYS HIGCRDQIIF MVGRGYLSPD LSKISSNCPK AMRRLLSDCL 550
KFQREERPLF PQILATIELL QRSLPKIERS ASEPSLHRTQ ADELPACLLS 600
AARLVP 606
Length:606
Mass (Da):67,585
Last modified:October 1, 1996 - v2
Checksum:iD23E5711304AA468
GO
Isoform 2 (identifier: P10398-2) [UniParc]FASTAAdd to Basket

Also known as: DA-Raf1

The sequence of this isoform differs from the canonical sequence as follows:
     186-186: S → R
     187-606: Missing.

Note: Has a wider tissue distribution than isoform 1, and acts as dominant-negative antagonist.

Show »
Length:186
Mass (Da):20,904
Checksum:i22710574E5D8A1B3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti98 – 981M → T.1 Publication
Corresponds to variant rs56197559 [ dbSNP | Ensembl ].
VAR_040375
Natural varianti331 – 3311G → C in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040376
Natural varianti578 – 5781E → D.1 Publication
Corresponds to variant rs55852926 [ dbSNP | Ensembl ].
VAR_040377

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei186 – 1861S → R in isoform 2. VSP_045609
Alternative sequencei187 – 606420Missing in isoform 2. VSP_045610Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 3681L → P in AAB08754. 1 Publication
Sequence conflicti378 – 3781F → V in AAB08754. 1 Publication
Sequence conflicti469 – 4691S → P in AAB08754. 1 Publication
Sequence conflicti478 – 4781I → T in AAB08754. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04790 mRNA. Translation: CAA28476.1.
L24038 Genomic DNA. Translation: AAA65219.1.
U01337 Genomic DNA. Translation: AAB03517.1.
AB158254 mRNA. Translation: BAE66645.1.
BT019864 mRNA. Translation: AAV38667.1.
AL542736 mRNA. No translation available.
Z84466 Genomic DNA. Translation: CAI42468.1.
Z84466 Genomic DNA. Translation: CAI42469.1.
BC002466 mRNA. Translation: AAH02466.1.
M13829 mRNA. Translation: AAB08754.1.
CCDSiCCDS35232.1. [P10398-1]
CCDS59164.1. [P10398-2]
PIRiA53026. TVHUAF.
RefSeqiNP_001243125.1. NM_001256196.1.
NP_001243126.1. NM_001256197.1. [P10398-2]
NP_001645.1. NM_001654.4. [P10398-1]
UniGeneiHs.446641.

Genome annotation databases

EnsembliENST00000377039; ENSP00000366238; ENSG00000078061. [P10398-2]
ENST00000377045; ENSP00000366244; ENSG00000078061. [P10398-1]
GeneIDi369.
KEGGihsa:369.
UCSCiuc011mlp.3. human. [P10398-1]
uc031tjj.1. human.

Polymorphism databases

DMDMi1730068.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04790 mRNA. Translation: CAA28476.1 .
L24038 Genomic DNA. Translation: AAA65219.1 .
U01337 Genomic DNA. Translation: AAB03517.1 .
AB158254 mRNA. Translation: BAE66645.1 .
BT019864 mRNA. Translation: AAV38667.1 .
AL542736 mRNA. No translation available.
Z84466 Genomic DNA. Translation: CAI42468.1 .
Z84466 Genomic DNA. Translation: CAI42469.1 .
BC002466 mRNA. Translation: AAH02466.1 .
M13829 mRNA. Translation: AAB08754.1 .
CCDSi CCDS35232.1. [P10398-1 ]
CCDS59164.1. [P10398-2 ]
PIRi A53026. TVHUAF.
RefSeqi NP_001243125.1. NM_001256196.1.
NP_001243126.1. NM_001256197.1. [P10398-2 ]
NP_001645.1. NM_001654.4. [P10398-1 ]
UniGenei Hs.446641.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WXM NMR - A 19-91 [» ]
ProteinModelPortali P10398.
SMRi P10398. Positions 20-91, 96-146, 273-576.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106864. 43 interactions.
DIPi DIP-31374N.
IntActi P10398. 37 interactions.
MINTi MINT-88835.
STRINGi 9606.ENSP00000366244.

Chemistry

ChEMBLi CHEMBL1169596.
DrugBanki DB00171. Adenosine triphosphate.
GuidetoPHARMACOLOGYi 1933.

PTM databases

PhosphoSitei P10398.

Polymorphism databases

DMDMi 1730068.

Proteomic databases

MaxQBi P10398.
PaxDbi P10398.
PRIDEi P10398.

Protocols and materials databases

DNASUi 369.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377039 ; ENSP00000366238 ; ENSG00000078061 . [P10398-2 ]
ENST00000377045 ; ENSP00000366244 ; ENSG00000078061 . [P10398-1 ]
GeneIDi 369.
KEGGi hsa:369.
UCSCi uc011mlp.3. human. [P10398-1 ]
uc031tjj.1. human.

Organism-specific databases

CTDi 369.
GeneCardsi GC0XP047429.
HGNCi HGNC:646. ARAF.
MIMi 311010. gene.
neXtProti NX_P10398.
PharmGKBi PA24928.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000252972.
HOVERGENi HBG001886.
KOi K08845.
OMAi LFHTTRL.
OrthoDBi EOG7F5128.
PhylomeDBi P10398.
TreeFami TF317006.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
SignaLinki P10398.

Miscellaneous databases

EvolutionaryTracei P10398.
GeneWikii ARAF.
GenomeRNAii 369.
NextBioi 1545.
PROi P10398.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10398.
Bgeei P10398.
CleanExi HS_ARAF.
Genevestigatori P10398.

Family and domain databases

InterProi IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR003116. Raf-like_ras-bd.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00130. C1_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF02196. RBD. 1 hit.
[Graphical view ]
PRINTSi PR00008. DAGPEDOMAIN.
SMARTi SM00109. C1. 1 hit.
SM00455. RBD. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50898. RBD. 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. "The complete coding sequence of the human A-raf-1 oncogene and transforming activity of a human A-raf carrying retrovirus."
    Beck T.W., Huleihel M., Gunnell M., Bonner T.I., Rapp U.R.
    Nucleic Acids Res. 15:595-609(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The complete sequence and promoter activity of the human A-raf-1 gene (ARAF1)."
    Lee J.-E., Beck T.W., Brennscheidt U., DeGennaro L.J., Rapp U.R.
    Genomics 20:43-55(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  3. "DA-Raf1, a competent intrinsic dominant-negative antagonist of the Ras-ERK pathway, is required for myogenic differentiation."
    Yokoyama T., Takano K., Yoshida A., Katada F., Sun P., Takenawa T., Andoh T., Endo T.
    J. Cell Biol. 177:781-793(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), ALTERNATIVE SPLICING.
  4. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  6. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Kidney.
  8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 292-589 (ISOFORM 1).
  9. "Identification of TH1 as an interaction partner of A-Raf kinase."
    Yin X.L., Chen S., Gu J.X.
    Mol. Cell. Biochem. 231:69-74(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NELFD.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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 THR-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "PRR5L degradation promotes mTORC2-mediated PKC-delta phosphorylation and cell migration downstream of Galpha12."
    Gan X., Wang J., Wang C., Sommer E., Kozasa T., Srinivasula S., Alessi D., Offermanns S., Simon M.I., Wu D.
    Nat. Cell Biol. 14:686-696(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TOR SIGNALING.
  20. "Solution structure of the N-terminal RAS-binding domain (RBD) in human A-RAF kinase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 19-91.
  21. "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] THR-98; CYS-331 AND ASP-578.

Entry informationi

Entry nameiARAF_HUMAN
AccessioniPrimary (citable) accession number: P10398
Secondary accession number(s): P07557, Q5H9B2, Q5H9B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 174 of the entry and version 2 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 X
    Human chromosome X: 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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