Q8IVT5 (KSR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kinase suppressor of Ras 1

Gene names

Name:	KSR1
Synonyms:	KSR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	921 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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. Ref.11
Subcellular location	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. Ref.11
Domain	The protein kinase domain is predicted to be catalytically inactive.
Post-translational modification	Phosphorylated on Ser-309 and, to a higher extent, on Ser-404 by MARK3. Dephosphorylated on Ser-404 by PPP2CA. In resting cells, phosphorylated KSR1 is cytoplasmic and in stimulated cells, dephosphorylated KSR1 is membrane-associated By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Ras protein signal transduction Non-traceable author statement Ref.3. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell intracellular Non-traceable author statement. Source: UniProtKB
Molecular_function	ATP binding Non-traceable author statement. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase activity Non-traceable author statement Ref.3. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VRK2	Q86Y07	4	EBI-486984,EBI-1207615

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8IVT5-1)

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.

Isoform 2 (identifier: Q8IVT5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     502-524: VPSAGHCWKCLLIAESLKENAFN → D
     897-921: INSSKVVPRFERFGLGVLESSNPKM → L

Note: No experimental confirmation available.

Isoform 3 (identifier: Q8IVT5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-135: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 921	921	Kinase suppressor of Ras 1		PRO_0000086229
Regions
	Domain	611 – 881	271	Protein kinase
	Zinc finger	345 – 389	45	Phorbol-ester/DAG-type
	Compositional bias	17 – 21	5	Poly-Gly
	Compositional bias	287 – 290	4	Poly-Pro
Sites
	Metal binding	346	1	Zinc 1 By similarity
	Metal binding	358	1	Zinc 2 By similarity
	Metal binding	361	1	Zinc 2 By similarity
	Metal binding	371	1	Zinc 1 By similarity
	Metal binding	374	1	Zinc 1 By similarity
	Metal binding	379	1	Zinc 2 By similarity
	Metal binding	382	1	Zinc 2 By similarity
	Metal binding	389	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	268	1	Phosphothreonine Ref.6 Ref.7 Ref.8
	Modified residue	272	1	Phosphothreonine Ref.8
	Modified residue	309	1	Phosphoserine Ref.5 Ref.13
	Modified residue	332	1	Phosphoserine Ref.6 Ref.8
	Modified residue	404	1	Phosphoserine Ref.8 Ref.10
	Modified residue	567	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	1 – 135	135	Missing in isoform 3.		VSP_012229
	Alternative sequence	502 – 524	23	VPSAG…ENAFN → D in isoform 2.		VSP_012230
	Alternative sequence	897 – 921	25	INSSK…SNPKM → L in isoform 2.		VSP_012231
	Natural variant	225	1	S → P. Ref.14		VAR_040658
	Natural variant	357	1	V → A. Ref.14		VAR_046048
	Natural variant	661	1	Q → H. Ref.14		VAR_046049
Experimental info
	Sequence conflict	241 – 263	23	FSEGL…TPRAL → EFRHTSALTQHTAHTQHTSA HTQ Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 21, 2004. Version 2. Checksum: FBF2E4976215C313	FASTA	921	102,032
	10 20 30 40 50 60 MDRAALRAAA MGEKKEGGGG GDAAEGGAGA AASRALQQCG QLQKLIDISI GSLRGLRTKC 70 80 90 100 110 120 AVSNDLTQQE IRTLEAKLVR YICKQRQCKL SVAPGERTPE LNSYPRFSDW LYTFNVRPEV 130 140 150 160 170 180 VQEIPRDLTL DALLEMNEAK VKETLRRCGA SGDECGRLQY ALTCLRKVTG LGGEHKEDSS 190 200 210 220 230 240 WSSLDARRES GSGPSTDTLS AASLPWPPGS SQLGRAGNSA QGPRSISVSA LPASDSPTPS 250 260 270 280 290 300 FSEGLSDTCI PLHASGRLTP RALHSFITPP TTPQLRRHTK LKPPRTPPPP SRKVFQLLPS 310 320 330 340 350 360 FPTLTRSKSH ESQLGNRIDD VSSMRFDLSH GSPQMVRRDI GLSVTHRFST KSWLSQVCHV 370 380 390 400 410 420 CQKSMIFGVK CKHCRLKCHN KCTKEAPACR ISFLPLTRLR RTESVPSDIN NPVDRAAEPH 430 440 450 460 470 480 FGTLPKALTK KEHPPAMNHL DSSSNPSSTT SSTPSSPAPF PTSSNPSSAT TPPNPSPGQR 490 500 510 520 530 540 DSRFNFPAAY FIHHRQQFIF PVPSAGHCWK CLLIAESLKE NAFNISAFAH AAPLPEAADG 550 560 570 580 590 600 TRLDDQPKAD VLEAHEAEAE EPEAGKSEAE DDEDEVDDLP SSRRPWRGPI SRKASQTSVY 610 620 630 640 650 660 LQEWDIPFEQ VELGEPIGQG RWGRVHRGRW HGEVAIRLLE MDGHNQDHLK LFKKEVMNYR 670 680 690 700 710 720 QTRHENVVLF MGACMNPPHL AIITSFCKGR TLHSFVRDPK TSLDINKTRQ IAQEIIKGMG 730 740 750 760 770 780 YLHAKGIVHK DLKSKNVFYD NGKVVITDFG LFGISGVVRE GRRENQLKLS HDWLCYLAPE 790 800 810 820 830 840 IVREMTPGKD EDQLPFSKAA DVYAFGTVWY ELQARDWPLK NQAAEASIWQ IGSGEGMKRV 850 860 870 880 890 900 LTSVSLGKEV SEILSACWAF DLQERPSFSL LMDMLEKLPK LNRRLSHPGH FWKSAEINSS 910 920 KVVPRFERFG LGVLESSNPK M
	Isoform 2 [UniParc]. Checksum: 192D0A1F797EEE87	FASTA	875	96,973
	10 20 30 40 50 60 MDRAALRAAA MGEKKEGGGG GDAAEGGAGA AASRALQQCG QLQKLIDISI GSLRGLRTKC 70 80 90 100 110 120 AVSNDLTQQE IRTLEAKLVR YICKQRQCKL SVAPGERTPE LNSYPRFSDW LYTFNVRPEV 130 140 150 160 170 180 VQEIPRDLTL DALLEMNEAK VKETLRRCGA SGDECGRLQY ALTCLRKVTG LGGEHKEDSS 190 200 210 220 230 240 WSSLDARRES GSGPSTDTLS AASLPWPPGS SQLGRAGNSA QGPRSISVSA LPASDSPTPS 250 260 270 280 290 300 FSEGLSDTCI PLHASGRLTP RALHSFITPP TTPQLRRHTK LKPPRTPPPP SRKVFQLLPS 310 320 330 340 350 360 FPTLTRSKSH ESQLGNRIDD VSSMRFDLSH GSPQMVRRDI GLSVTHRFST KSWLSQVCHV 370 380 390 400 410 420 CQKSMIFGVK CKHCRLKCHN KCTKEAPACR ISFLPLTRLR RTESVPSDIN NPVDRAAEPH 430 440 450 460 470 480 FGTLPKALTK KEHPPAMNHL DSSSNPSSTT SSTPSSPAPF PTSSNPSSAT TPPNPSPGQR 490 500 510 520 530 540 DSRFNFPAAY FIHHRQQFIF PDISAFAHAA PLPEAADGTR LDDQPKADVL EAHEAEAEEP 550 560 570 580 590 600 EAGKSEAEDD EDEVDDLPSS RRPWRGPISR KASQTSVYLQ EWDIPFEQVE LGEPIGQGRW 610 620 630 640 650 660 GRVHRGRWHG EVAIRLLEMD GHNQDHLKLF KKEVMNYRQT RHENVVLFMG ACMNPPHLAI 670 680 690 700 710 720 ITSFCKGRTL HSFVRDPKTS LDINKTRQIA QEIIKGMGYL HAKGIVHKDL KSKNVFYDNG 730 740 750 760 770 780 KVVITDFGLF GISGVVREGR RENQLKLSHD WLCYLAPEIV REMTPGKDED QLPFSKAADV 790 800 810 820 830 840 YAFGTVWYEL QARDWPLKNQ AAEASIWQIG SGEGMKRVLT SVSLGKEVSE ILSACWAFDL 850 860 870 QERPSFSLLM DMLEKLPKLN RRLSHPGHFW KSAEL
	Isoform 3 [UniParc]. Checksum: 7BDC623DFE4B87BA	FASTA	786	87,358
	10 20 30 40 50 60 MNEAKVKETL RRCGASGDEC GRLQYALTCL RKVTGLGGEH KEDSSWSSLD ARRESGSGPS 70 80 90 100 110 120 TDTLSAASLP WPPGSSQLGR AGNSAQGPRS ISVSALPASD SPTPSFSEGL SDTCIPLHAS 130 140 150 160 170 180 GRLTPRALHS FITPPTTPQL RRHTKLKPPR TPPPPSRKVF QLLPSFPTLT RSKSHESQLG 190 200 210 220 230 240 NRIDDVSSMR FDLSHGSPQM VRRDIGLSVT HRFSTKSWLS QVCHVCQKSM IFGVKCKHCR 250 260 270 280 290 300 LKCHNKCTKE APACRISFLP LTRLRRTESV PSDINNPVDR AAEPHFGTLP KALTKKEHPP 310 320 330 340 350 360 AMNHLDSSSN PSSTTSSTPS SPAPFPTSSN PSSATTPPNP SPGQRDSRFN FPAAYFIHHR 370 380 390 400 410 420 QQFIFPVPSA GHCWKCLLIA ESLKENAFNI SAFAHAAPLP EAADGTRLDD QPKADVLEAH 430 440 450 460 470 480 EAEAEEPEAG KSEAEDDEDE VDDLPSSRRP WRGPISRKAS QTSVYLQEWD IPFEQVELGE 490 500 510 520 530 540 PIGQGRWGRV HRGRWHGEVA IRLLEMDGHN QDHLKLFKKE VMNYRQTRHE NVVLFMGACM 550 560 570 580 590 600 NPPHLAIITS FCKGRTLHSF VRDPKTSLDI NKTRQIAQEI IKGMGYLHAK GIVHKDLKSK 610 620 630 640 650 660 NVFYDNGKVV ITDFGLFGIS GVVREGRREN QLKLSHDWLC YLAPEIVREM TPGKDEDQLP 670 680 690 700 710 720 FSKAADVYAF GTVWYELQAR DWPLKNQAAE ASIWQIGSGE GMKRVLTSVS LGKEVSEILS 730 740 750 760 770 780 ACWAFDLQER PSFSLLMDML EKLPKLNRRL SHPGHFWKSA EINSSKVVPR FERFGLGVLE SSNPKM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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] (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 241-897 (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-309, MASS SPECTROMETRY. 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-268 AND SER-332, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268, MASS SPECTROMETRY. Tissue: Platelet.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; THR-272; SER-332; SER-404 AND SER-567, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] 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-404, MASS SPECTROMETRY. 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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-309, MASS SPECTROMETRY.
[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-225; ALA-357 AND HIS-661.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC069366 Genomic DNA. No translation available. AC015688 Genomic DNA. No translation available. BC042106 mRNA. Translation: AAH42106.1. U43586 mRNA. Translation: AAC50354.1.
IPI	IPI00013384. IPI00217124. IPI01015914.
RefSeq	NP_055053.1. NM_014238.1.
UniGene	Hs.133534.
3D structure databases
ProteinModelPortal	Q8IVT5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IVT5. 9 interactions.
STRING	9606.ENSP00000268763.
PTM databases
PhosphoSite	Q8IVT5.
Polymorphism databases
DMDM	56749095.
Proteomic databases
PaxDb	Q8IVT5.
PRIDE	Q8IVT5.
Protocols and materials databases
DNASU	8844.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000268763; ENSP00000268763; ENSG00000141068.
GeneID	8844.
KEGG	hsa:8844.
UCSC	uc002gzm.3. human.
Organism-specific databases
CTD	8844.
GeneCards	GC17P025783.
H-InvDB	HIX0018394. HIX0025516. HIX0029273.
HGNC	HGNC:6465. KSR1.
HPA	CAB009623. HPA011215.
MIM	601132. gene.
neXtProt	NX_Q8IVT5.
PharmGKB	PA30254.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000113263.
HOVERGEN	HBG052293.
InParanoid	Q8IVT5.
KO	K14958.
Enzyme and pathway databases
Pathway_Interaction_DB	ceramidepathway. Ceramide signaling pathway.
Gene expression databases
ArrayExpress	Q8IVT5.
Bgee	Q8IVT5.
CleanEx	HS_KSR1.
Genevestigator	Q8IVT5.
GermOnline	ENSG00000141068. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR025561. KSR_SAM-like_dom. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR000719. Prot_kinase_cat_dom. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF13543. KSR1-SAM. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view]
SMART	SM00109. C1. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1938215.
ChiTaRS	KSR1. human.
GenomeRNAi	8844.
NextBio	33204.
SOURCE	Search...

Entry information

Entry name

KSR1_HUMAN

Accession

Primary (citable) accession number: Q8IVT5
Secondary accession number(s): Q13476

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.