ROCK2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ROCK2_MOUSE
• UniProt AC: P70336
• Protein Name: Rho-associated protein kinase 2
• Gene Name: Rock2
• Organism: Mus musculus (Mouse).
• Sequence Length: 1388
• Subcellular Localization: Isoform 1: Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic, and associated with actin microfilaments and the plasma membrane..; Isoform 2: Cytoplasm. Cell
• Protein Description: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays a role in placental homeostasis during the perinatal period. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation..
• Protein Sequence: MSRPPPTGKMPGAPEAAPGDGAGAGRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDTEISKHAKNLICAFLTDREVRLGRNGVEEIKQHPFFKNDQWNWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYFRENLLLSDSPPCRENDAIQTRKSEESQEIQKKLYALEEHLSSEVQAKEELEQKCKSINTRLEKTAKELEEEITLRKSVESTLRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQSSQISTEKVNQLQKQLDEANALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKEFINLQSALESERRDRTHGSEIINDLQGRISGLEEDLKTGKALLAKVELEKRQLQEKLTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKTTKARLADKNKIYESIEEAKSEAMKEMEKKLLEERSLKQKVENLLLEAEKRCSILDCDLKQSQQKLNELLKQKDVLNEDVRNLTLKIEQETQKRCLMQNDLKMQTQQVNTLKMSEKQIKQENNHLMEMKMNLEKQNTELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEENEEKTKLCKELQQKKQDLQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDTTIASLEETNRTLTSDVANLANEKEELNNKLKDSQEQLSKLKDEEMSAAAIKAQFEKQLLNERTLKTQAVNKLAEIMNRKEPVKRGSDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGMDSSSIGSGPGDAEPDDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEPEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISSAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAPNKPS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSRPPPTGK ------CCCCCCCCC	65.87	19854140
7	Phosphorylation	-MSRPPPTGKMPGAP -CCCCCCCCCCCCCC	56.03	22817900
253	Phosphorylation	HCDTAVGTPDYISPE ECCCCCCCCCCCCHH	13.34	-
298	Phosphorylation	DTPFYADSLVGTYSK CCCCCCCHHHHHHHH	19.45	-
414	Phosphorylation	QLPFIGFTYFRENLL CCCCCEEEEEHHCCC	19.28	-
423	Phosphorylation	FRENLLLSDSPPCRE EHHCCCCCCCCCCCC	35.69	28066266
425	Phosphorylation	ENLLLSDSPPCREND HCCCCCCCCCCCCCC	27.63	29233185
436	Phosphorylation	RENDAIQTRKSEESQ CCCCCCCCCCCHHHH	33.67	20415495
439	Phosphorylation	DAIQTRKSEESQEIQ CCCCCCCCHHHHHHH	43.22	26824392
442	Phosphorylation	QTRKSEESQEIQKKL CCCCCHHHHHHHHHH	29.12	29550500
625	Phosphorylation	KEFINLQSALESERR HHHHCHHHHHHHHHC	37.68	30635358
629	Phosphorylation	NLQSALESERRDRTH CHHHHHHHHHCCCCC	36.93	30635358
691	Phosphorylation	SNMEIDMTYQLKVIQ HCCCCCHHHHHHHHH	12.36	-
692	Phosphorylation	NMEIDMTYQLKVIQQ CCCCCHHHHHHHHHH	12.76	-
722	Phosphorylation	LADKNKIYESIEEAK HHCHHHHHHHHHHHH	12.77	20826462
724	Phosphorylation	DKNKIYESIEEAKSE CHHHHHHHHHHHHHH	20.52	25367039
814	Phosphorylation	QNDLKMQTQQVNTLK HCCHHHHHHHHHHHH	19.92	29514104
819	Phosphorylation	MQTQQVNTLKMSEKQ HHHHHHHHHHHCHHH	28.97	29514104
828	Ubiquitination	KMSEKQIKQENNHLM HHCHHHHHHHHHHHH	49.41	-
937	Phosphorylation	SIAEEQYSDLEKEKI HHHHHHHCHHHHHHH	35.10	26525534
1007	Acetylation	QEQLSKLKDEEMSAA HHHHHHHCHHHHHHH	67.82	15607995
1022	Acetylation	AIKAQFEKQLLNERT HHHHHHHHHHHCCHH	47.75	15608007
1022	Ubiquitination	AIKAQFEKQLLNERT HHHHHHHHHHHCCHH	47.75	-
1037	Ubiquitination	LKTQAVNKLAEIMNR HHHHHHHHHHHHHCC	42.34	-
1052	Phosphorylation	KEPVKRGSDTDVRRK CCCCCCCCHHHHHHH	41.17	25521595
1054	Phosphorylation	PVKRGSDTDVRRKEK CCCCCCHHHHHHHHH	37.78	29550500
1072	Phosphorylation	KLHMELKSEREKLTQ HHHHHHHHHHHHHHH	55.28	25338131
1121	Phosphorylation	SDIEQLRSQLQALHI CHHHHHHHHHHHHHC	43.78	23984901
1132	Phosphorylation	ALHIGMDSSSIGSGP HHHCCCCHHHCCCCC	19.66	24759943
1133	Phosphorylation	LHIGMDSSSIGSGPG HHCCCCHHHCCCCCC	23.01	21183079
1134	Phosphorylation	HIGMDSSSIGSGPGD HCCCCHHHCCCCCCC	34.61	27087446
1137	Phosphorylation	MDSSSIGSGPGDAEP CCHHHCCCCCCCCCC	39.89	27087446
1169 (in isoform 2)	Phosphorylation	-	36.83	28464351
1194	Phosphorylation	SEQDKEQSNPYMVLD CCCCHHHCCCEEEEE	40.64	29899451
1197	Phosphorylation	DKEQSNPYMVLDIDK CHHHCCCEEEEEHHH	12.24	29899451
1212	Phosphorylation	LFHVRPVTQTDVYRA HCCCEECCCCCEECC	28.56	-
1318	Phosphorylation	IIAPCKVYYDISSAK EEECCEEEEECCCHH	4.86	29514104
1319	Phosphorylation	IAPCKVYYDISSAKN EECCEEEEECCCHHH	15.13	29514104
1322	Phosphorylation	CKVYYDISSAKNLLL CEEEEECCCHHHHHH	22.73	28285833
1323	Phosphorylation	KVYYDISSAKNLLLL EEEEECCCHHHHHHH	43.53	28285833
1361	Phosphorylation	APDPFARSSPRTSMK CCCCCCCCCCCCCHH	41.06	26239621
1362	Phosphorylation	PDPFARSSPRTSMKI CCCCCCCCCCCCHHH	16.91	26824392
1365	Phosphorylation	FARSSPRTSMKIQQN CCCCCCCCCHHHHHC	36.24	22324799
1366	Phosphorylation	ARSSPRTSMKIQQNQ CCCCCCCCHHHHHCC	21.25	22324799
1374	Phosphorylation	MKIQQNQSIRRPSRQ HHHHHCCCCCCCCCC	26.13	25521595
1379	Phosphorylation	NQSIRRPSRQLAPNK CCCCCCCCCCCCCCC	30.74	26060331
1388	Phosphorylation	QLAPNKPS------- CCCCCCCC-------	55.23	-
1431 (in isoform 2)	Phosphorylation	-		29514104
1436 (in isoform 2)	Phosphorylation	-		29514104

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
414	T	Phosphorylation	Kinase	ROCK2	P70336	Uniprot
722	Y	Phosphorylation	Kinase	SRC	P12931	PSP
722	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ROCK2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ROCK2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NPM_MOUSE	Npm1	physical	17015463
VIME_MOUSE	Vim	physical	17015463

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.