F5H5U8 (F5H5U8_HUMAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase RuleBase RU003492
EC=2.7.10.2 RuleBase RU003492

Gene names

Name:

JAK2 Ensembl ENSP00000443103

Organism

Homo sapiens (Human) [Reference proteome] Ensembl ENSP00000443103

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	983 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. RuleBase RU003492 SAAS SAAS008266
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. JAK subfamily. RuleBase RU003492 Contains 1 SH2 domain. RuleBase RU003492
Caution	The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSP00000443103

Ontologies

Keywords
Domain	SH2 domain RuleBase RU003492
Ligand	ATP-binding SAAS SAAS008266 Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase SAAS SAAS008266
PTM	Phosphoprotein RuleBase RU003493
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara STAT protein import into nucleus Inferred from electronic annotation. Source: Compara activation of MAPKK activity Inferred from electronic annotation. Source: Compara axon regeneration Inferred from electronic annotation. Source: Compara elevation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Compara hormone-mediated signaling pathway Inferred from electronic annotation. Source: Compara interferon-gamma-mediated signaling pathway Inferred from electronic annotation. Source: Compara intrinsic apoptotic signaling pathway in response to oxidative stress Inferred from electronic annotation. Source: Compara mammary gland epithelium development Inferred from electronic annotation. Source: Compara mineralocorticoid receptor signaling pathway Inferred from electronic annotation. Source: Compara myeloid cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of DNA binding Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of cell-cell adhesion Inferred from electronic annotation. Source: Compara negative regulation of heart contraction Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara platelet-derived growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of DNA binding Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell activation Inferred from electronic annotation. Source: Compara positive regulation of cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of inflammatory response Inferred from electronic annotation. Source: Compara positive regulation of insulin secretion Inferred from electronic annotation. Source: Compara positive regulation of interleukin-1 beta production Inferred from electronic annotation. Source: Compara positive regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of nitric-oxide synthase biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of phosphoprotein phosphatase activity Inferred from electronic annotation. Source: Compara positive regulation of protein import into nucleus, translocation Inferred from electronic annotation. Source: Compara positive regulation of sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara response to hydroperoxide Inferred from electronic annotation. Source: Compara tyrosine phosphorylation of Stat1 protein Inferred from electronic annotation. Source: Compara tyrosine phosphorylation of Stat3 protein Inferred from electronic annotation. Source: Compara tyrosine phosphorylation of Stat5 protein Inferred from electronic annotation. Source: Compara
Cellular_component	caveola Inferred from electronic annotation. Source: Compara cytoskeleton Inferred from electronic annotation. Source: InterPro cytosol Inferred from electronic annotation. Source: Compara nuclear matrix Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	F5H5U8 [UniParc]. Last modified June 28, 2011. Version 1. Checksum: F9C99B39A8A9D345	FASTA	983	113,766
	10 20 30 40 50 60 MSYLFAQWRH DFVHGWIKVP VTHETQEECL GMAVLDMMRI AKENDQTPLA IYNSISYKTF 70 80 90 100 110 120 LPKCIRAKIQ DYHILTRKRI RYRFRRFIQQ FSQCKATARN LKLKYLINLE TLQSAFYTEK 130 140 150 160 170 180 FEVKEPGSGP SGEEIFATII ITGNGGIQWS RGKHKESETL TEQDLQLYCD FPNIIDVSIK 190 200 210 220 230 240 QANQEGSNES RVVTIHKQDG KNLEIELSSL REALSFVSLI DGYYRLTADA HHYLCKEVAP 250 260 270 280 290 300 PAVLENIQSN CHGPISMDFA ISKLKKAGNQ TGLYVLRCSP KDFNKYFLTF AVERENVIEY 310 320 330 340 350 360 KHCLITKNEN EEYNLSGTKK NFSSLKDLLN CYQMETVRSD NIIFQFTKCC PPKPKDKSNL 370 380 390 400 410 420 LVFRTNGVSD VPTSPTLQRP THMNQMVFHK IRNEDLIFNE SLGQGTFTKI FKGVRREVGD 430 440 450 460 470 480 YGQLHETEVL LKVLDKAHRN YSESFFEAAS MMSKLSHKHL VLNYGVCVCG DENILVQEFV 490 500 510 520 530 540 KFGSLDTYLK KNKNCINILW KLEVAKQLAW AMHFLEENTL IHGNVCAKNI LLIREEDRKT 550 560 570 580 590 600 GNPPFIKLSD PGISITVLPK DILQERIPWV PPECIENPKN LNLATDKWSF GTTLWEICSG 610 620 630 640 650 660 GDKPLSALDS QRKLQFYEDR HQLPAPKWAE LANLINNCMD YEPDFRPSFR AIIRDLNSLF 670 680 690 700 710 720 TPDYELLTEN DMLPNMRIGA LGFSGAFEDR DPTQFEERHL KFLQQLGKGN FGSVEMCRYD 730 740 750 760 770 780 PLQDNTGEVV AVKKLQHSTE EHLRDFEREI EILKSLQHDN IVKYKGVCYS AGRRNLKLIM 790 800 810 820 830 840 EYLPYGSLRD YLQKHKERID HIKLLQYTSQ ICKGMEYLGT KRYIHRDLAT RNILVENENR 850 860 870 880 890 900 VKIGDFGLTK VLPQDKEYYK VKEPGESPIF WYAPESLTES KFSVASDVWS FGVVLYELFT 910 920 930 940 950 960 YIEKSKSPPA EFMRMIGNDK QGQMIVFHLI ELLKNNGRLP RPDGCPDEIY MIMTECWNNN 970 980 VNQRPSFRDL ALRVDQIRDN MAG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	Ensembl Submitted (JUL-2011) to UniProtKB Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL158147 Genomic DNA. No translation available. AL161450 Genomic DNA. No translation available. AL513350 Genomic DNA. No translation available.
IPI	IPI01013665.
3D structure databases
ProteinModelPortal	F5H5U8.
SMR	F5H5U8. Positions 252-982.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000544510; ENSP00000443103; ENSG00000096968.
Organism-specific databases
HGNC	HGNC:6192. JAK2.
GenAtlas	Search...
Gene expression databases
ArrayExpress	F5H5U8.
Bgee	F5H5U8.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR000299. FERM_domain. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR000980. SH2. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. IPR016251. Tyr_kinase_non-rcpt_Jak/Tyk2. IPR020693. Tyr_kinase_non-rcpt_Jak2. [Graphical view]
Pfam	PF07714. Pkinase_Tyr. 2 hits. PF00017. SH2. 1 hit. [Graphical view]
PRINTS	PR01823. JANUSKINASE. PR01825. JANUSKINASE2. PR00109. TYRKINASE.
SMART	SM00252. SH2. 1 hit. SM00219. TyrKc. 2 hits. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 2 hits.
PROSITE	PS50057. FERM_3. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 2 hits. PS00109. PROTEIN_KINASE_TYR. 1 hit. PS50001. SH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	JAK2. human.
NextBio	35509070.

Entry information

Entry name

F5H5U8_HUMAN

Accession

Primary (citable) accession number: F5H5U8

Entry history

Integrated into UniProtKB/TrEMBL:	June 28, 2011
Last sequence update:	June 28, 2011
Last modified:	May 1, 2013
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

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.