STE20/SPS1-related proline-alanine-rich protein kinase

Details

Name
STE20/SPS1-related proline-alanine-rich protein kinase
Synonyms
  • 2.7.11.1
  • DCHT
  • Serine/threonine-protein kinase 39
  • SPAK
  • Ste-20-related kinase
Gene Name
STK39
Organism
Humans
Amino acid sequence
>lcl|BSEQ0051660|STE20/SPS1-related proline-alanine-rich protein kinase
MAEPSGSPVHVQLPQQAAPVTAAAAAAPAAATAAPAPAAPAAPAPAPAPAAQAVGWPICR
DAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPN
VVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGL
DYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKTFVGTPCWMA
PEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDK
EMMKKYGKSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEKLLTRTPDIAQR
AKKVRRVPGSSGHLHKTEDGDWEWSDDEMDEKSEEGKAAFSQEKSRRVKEENPEIAVSAS
TIPEQIQSLSVHDSQGPPNANEDYREASSCAVNLVLRLRNSRKELNDIRFEFTPGRDTAD
GVSQELFSAGLVDGHDVVIVAANLQKIVDDPKALKTLTFKLASGCDGSEIPDEVKLIGFA
QLSVS
Number of residues
545
Molecular Weight
59473.46
Theoretical pI
Not Available
GO Classification
Functions
ATP binding / kinase activity / protein kinase binding / protein serine/threonine kinase activity
Processes
activation of MAPK activity / activation of protein kinase activity / cellular hypotonic response / intracellular signal transduction / maintenance of lens transparency / negative regulation of creatine transmembrane transporter activity / negative regulation of pancreatic juice secretion / negative regulation of potassium ion transmembrane transport / negative regulation of potassium ion transmembrane transporter activity / negative regulation of protein phosphorylation / negative regulation of sodium ion transmembrane transporter activity / peptidyl-serine phosphorylation / peptidyl-threonine phosphorylation / positive regulation of ion transmembrane transporter activity / positive regulation of potassium ion transport / protein autophosphorylation / protein phosphorylation / regulation of apoptotic process / regulation of blood pressure / regulation of inflammatory response / regulation of ion homeostasis / regulation of mitotic cell cycle / signal transduction by protein phosphorylation / signal transduction by trans-phosphorylation / stress-activated protein kinase signaling cascade
Components
apical plasma membrane / basolateral plasma membrane / cytoplasm / cytoskeleton / cytosol / extrinsic component of membrane / intracellular membrane-bounded organelle / nucleoplasm
General Function
May act as a mediator of stress-activated signals. Mediates the inhibition of SLC4A4, SLC26A6 as well as CFTR activities by the WNK scaffolds, probably through phosphorylation.
Specific Function
Atp binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0051661|STE20/SPS1-related proline-alanine-rich protein kinase (STK39)
ATGGCGGAGCCGAGCGGCTCGCCCGTGCACGTCCAGCTTCCCCAGCAGGCGGCCCCGGTG
ACAGCGGCGGCGGCGGCGGCCCCGGCGGCCGCGACAGCAGCGCCGGCCCCGGCAGCTCCC
GCGGCCCCGGCCCCGGCCCCGGCCCCGGCGGCACAGGCTGTCGGCTGGCCCATCTGCAGG
GACGCGTACGAGCTGCAGGAGGTTATCGGCAGTGGAGCTACTGCTGTGGTTCAGGCAGCC
CTATGCAAACCCAGGCAAGAACGTGTAGCAATAAAACGGATCAACTTGGAAAAATGCCAG
ACCAGTATGGATGAACTATTAAAAGAAATTCAAGCCATGAGTCAGTGCAGCCATCCCAAC
GTAGTGACCTATTACACCTCTTTTGTGGTCAAAGATGAACTTTGGCTGGTCATGAAATTA
CTAAGTGGAGGTTCAATGTTGGATATCATAAAATACATTGTCAACCGAGGAGAACACAAG
AATGGAGTTCTGGAAGAGGCAATAATAGCAACAATTCTTAAAGAGGTTTTGGAAGGCTTA
GACTATCTACACAGAAACGGTCAGATTCACAGGGATTTGAAAGCTGGTAATATTCTTCTG
GGTGAGGATGGTTCAGTACAAATAGCAGATTTTGGGGTAAGTGCGTTCCTAGCAACAGGG
GGTGATGTTACCCGAAATAAAGTAAGAAAAACATTCGTTGGCACCCCATGTTGGATGGCT
CCTGAAGTCATGGAACAGGTGAGAGGCTATGACTTCAAGGCTGACATGTGGAGTTTTGGA
ATAACTGCCATTGAATTAGCAACAGGAGCAGCGCCTTATCACAAATATCCTCCCATGAAA
GTGTTAATGTTGACTTTGCAAAATGATCCACCCACTTTGGAAACAGGGGTAGAGGATAAA
GAAATGATGAAAAAGTACGGCAAGTCCTTTAGAAAATTACTTTCACTGTGTCTTCAGAAA
GATCCTTCCAAAAGGCCCACAGCAGCAGAACTTTTAAAATGCAAATTCTTCCAGAAAGCC
AAGAACAGAGAGTACCTGATTGAGAAGCTGCTTACAAGAACACCAGACATAGCCCAAAGA
GCCAAAAAGGTAAGAAGAGTTCCTGGGTCAAGTGGTCACCTTCATAAAACCGAAGACGGG
GACTGGGAGTGGAGTGACGACGAGATGGATGAGAAGAGCGAAGAAGGGAAAGCAGCTTTT
TCTCAGGAAAAGTCACGAAGAGTAAAAGAAGAAAATCCAGAGATTGCAGTGAGTGCCAGC
ACCATCCCCGAACAAATACAGTCCCTCTCTGTGCACGACTCTCAGGGCCCACCCAATGCT
AATGAAGACTACAGAGAAGCTTCTTCTTGTGCCGTGAACCTCGTTTTGAGATTAAGAAAC
TCCAGAAAGGAACTTAATGACATACGATTTGAGTTTACTCCAGGAAGAGATACAGCAGAT
GGTGTATCTCAGGAGCTCTTCTCTGCTGGCTTGGTGGATGGTCACGATGTAGTTATAGTG
GCTGCTAATTTACAGAAGATTGTAGATGATCCCAAAGCTTTAAAAACATTGACATTTAAG
TTGGCTTCTGGCTGTGATGGGTCGGAGATTCCTGATGAAGTGAAGCTGATTGGGTTTGCT
CAGTTGAGTGTCAGCTGA
Chromosome Location
2
Locus
2q24.3
External Identifiers
ResourceLink
UniProtKB IDQ9UEW8
UniProtKB Entry NameSTK39_HUMAN
HGNC IDHGNC:17717
General References
  1. Johnston AM, Naselli G, Gonez LJ, Martin RM, Harrison LC, DeAizpurua HJ: SPAK, a STE20/SPS1-related kinase that activates the p38 pathway. Oncogene. 2000 Aug 31;19(37):4290-7. [Article]
  2. Corominas R, Yang X, Lin GN, Kang S, Shen Y, Ghamsari L, Broly M, Rodriguez M, Tam S, Trigg SA, Fan C, Yi S, Tasan M, Lemmens I, Kuang X, Zhao N, Malhotra D, Michaelson JJ, Vacic V, Calderwood MA, Roth FP, Tavernier J, Horvath S, Salehi-Ashtiani K, Korkin D, Sebat J, Hill DE, Hao T, Vidal M, Iakoucheva LM: Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism. Nat Commun. 2014 Apr 11;5:3650. doi: 10.1038/ncomms4650. [Article]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [Article]
  4. Li Y, Hu J, Vita R, Sun B, Tabata H, Altman A: SPAK kinase is a substrate and target of PKCtheta in T-cell receptor-induced AP-1 activation pathway. EMBO J. 2004 Mar 10;23(5):1112-22. Epub 2004 Feb 26. [Article]
  5. Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [Article]
  6. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [Article]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [Article]
  10. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  11. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  12. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. [Article]
  13. Zhou H, Di Palma S, Preisinger C, Peng M, Polat AN, Heck AJ, Mohammed S: Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71. doi: 10.1021/pr300630k. Epub 2012 Dec 18. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails