Saccharomyces cerevisiae (S288c)

PSK2

serine/threonine protein kinase PSK2, YOL045W

PAS-domain containing serine/threonine protein kinase; regulates sugar flux and translation in response to an unknown metabolite by phosphorylating Ugp1p and Gsy2p (sugar flux) and Caf20p, Tif11p and Sro9p (translation); PSK2 has a paralog, PSK1, that arose from the whole genome duplication

Kinome Project (Sc)

GO Process (3)

GO Function (1)

GO Component (2)

Gene Ontology Biological Process

negative regulation of glycogen biosynthetic process [IGI, IMP]

protein phosphorylation [IDA, IMP]

regulation of (1->6)-beta-D-glucan biosynthetic process [IGI]

Gene Ontology Molecular Function

protein serine/threonine kinase activity [IDA, IMP]

Gene Ontology Cellular Component

cytoplasm [IDA]

mitochondrion [IDA]

SGD Alliance of Genome Resources Entrez Gene RefSeq UniprotKB

Download Curated Data for this Protein

34357

559292

PTM statistics

Proteins

PTM Sites

Publications

Phosphorylation Sites (6)
Ubiquitination Sites (3)

Interactors 190
Interactions 300
Network
PTM Sites 9

Sites with Multi-PTMs

Displaying 1 protein 1 non-assigned with 9 total post translational modifications

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NP_014597

Psk2p

Length: 1101

1
MTYPVSAAAP ADISYSKNTP LVGLSKPPCL YQHASSSVDS FSSTFSDDDR
51
SDLVAVPNES PHAFSYNPIS PNSLGVRLTI LRRSLEIMVN SPDILHELKK
101
KAPVIAYPPS LRHTRNLTET ATLSASRDPL NGSLISPLVS NMPSPASRPV
151
IQRATSLMVL PDNDTASKLN PAKSELENLL FLLNLALENN SFERASDLHM
201
LSLLNIKKIN FDSDIQKSET LKKVLLDSLA EPFFENYKKF PHKDLGSKSQ
251
YNEYEEKHDD IVSLADIKPQ QDYSRILHPF TSAKNSGPEA IFTCSQQYPW
301
NFKAANDLAC LTFGISKNVI KALTLLDLIH TDSRNFVLEK IMNAEDDNQE
351
IVFTGETIPI VQPNSTSNNN VPNLIWASLW AKRKNGLLVC VFEKTPCDYI
401
DVMLNLRDFS VDSIIDTTHF LENFDKKKQQ ESTSPMTEKK TVKFANEIHD
451
IGSVSHSLSK LIDDVRFGKV FSADDDLLPL SIRVANHVNE ERYFTLNCLS
501
ENIPCAVTTS VLENEIKLKI HSLPYQAGLF IVDSHTLSLL SFNKSVAKNM
551
FGLRLHELAG SSVTKLVPSL ADMISYINKT YPMLNITLPE NKGLVLTEHF
601
FRKIEAEMHH DKDSFYTSIG LDGCHKDGNL IKVDVQLRVL NTNAVLLWIT
651
HSRDVVIENY TTVPSQLPML KENEIDVVGS RGSSSASSKK SSEKIPVNTL
701
KAMADLSISS AETISNSDDE VDLNQVNEKL RETSCGKVRG IESNDNNNYD
751
DDMTMVDDPE LKHKIELTKM YTQDKSKFVK DDNFKVDEKF IMRIIEPING
801
EEIKKETNEL DKRNSTLKAT YLTTPEANIG SQKRIKKFSD FTILQVMGEG
851
AYGKVNLCIH NREHYIVVIK MIFKERILVD TWVRDRKLGT IPSEIQIMAT
901
LNKNSQENIL KLLDFFEDDD YYYIETPVHG ETGSIDLFDV IEFKKDMVEH
951
EAKLVFKQVV ASIKHLHDQG IVHRDIKDEN VIVDSHGFVK LIDFGSAAYI
1001
KSGPFDVFVG TMDYAAPEVL GGSSYKGKPQ DIWALGVLLY TIIYKENPYY
1051
NIDEILEGEL RFDKSEHVSE ECISLIKRIL TREVDKRPTI DEIYEDKWLK
1101
I

Location	PTM	Residue	Source(s)	Note(s)
118	Phosphorylation	T	Albuquerque CP (2008)	-
			Breitkreutz A (2010)	-
			Holt LJ (2009)	-
155	Phosphorylation	T	Albuquerque CP (2008)	eyJOT1RFUyI6WyJQTUlEIDIxMTI2MzM2OiBQcmVkaWN0ZWQgcHJvdGVpbiBraW5hc2UgPSBQS0MxIl19
155	Phosphorylation	T	Helbig AO (2010)	eyJOT1RFUyI6WyJQTUlEIDIxMTI2MzM2OiBQcmVkaWN0ZWQgcHJvdGVpbiBraW5hc2UgPSBQS0MxIl19
156	Phosphorylation	S	Albuquerque CP (2008)	-
222	Ubiquitination	K	Mayor T (2005)	-
223	Ubiquitination	K	Mayor T (2005)	-
434	Phosphorylation	S	Smolka MB (2007)	-
680	Phosphorylation	S	Albuquerque CP (2008)	-
			Breitkreutz A (2010)	-
			Holt LJ (2009)	-
717	Phosphorylation	S	Albuquerque CP (2008)	-
717	Phosphorylation	S	Breitkreutz A (2010)	-

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Non-Assigned PTMs

Post translational modifications that are currently unassigned to a specific residue location.

Location	PTM	Residue	Source(s)	Note(s)
-	Ubiquitination	K	Kolawa NJ (2013)	eyJOT1RFUyI6WyJUYWJsZSBTMTsgVmFsaWQgU3Vic3RyYXRlIiwibGlrZWx5IHViaXF1aXRpbiBjb25qdWdhdGUiXSwiUkVMQVRJT05TSElQUyI6eyJVQkk0IjoiPHNwYW4+PGEgaHJlZj0naHR0cHM6XC9cL3RoZWJpb2dyaWQub3JnXC8zMTIxNVwvc3VtbWFyeVwvc2FjY2hhcm9teWNlcy1jZXJldmlzaWFlXC91Ymk0Lmh0bWwnIGFsdD0nVUJJNCc+VUJJNDxcL2E+PFwvc3Bhbj4ifX0=

Relationships

Protein	Relationship	Location	PTM	Residue	Identity	Source(s)
UBI4	Conjugate	-	Ubiquitination	K	PTM	Kolawa NJ (2013)

Result Summary