dbPTM

ROCK_CAEEL - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ROCK_CAEEL
UniProt AC	P92199
Protein Name	Rho-associated protein kinase let-502 {ECO:0000250\|UniProtKB:Q13464, ECO:0000303\|PubMed:9042856}
Gene Name	let-502
Organism	Caenorhabditis elegans.
Sequence Length	1173
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton . Cleavage furrow . Colocalizes with nmy-2 myosin thick filaments at the cleavage furrow.
Protein Description	Negatively regulates mel-11 to relieve the inhibition of mlc-4, allowing contraction of the circumferentially oriented microfilaments in epidermal cells and thereby regulating myosin II contractility during spermathecal contraction, cleavage furrow contraction in early embryos, and embryonic elongation and morphogenesis. Required for P-cell migration. May also play a role in oocyte cellularization..
Protein Sequence	MEQDELRDQLVDPKSPINIESLLDTITALVNDCKIPVLMRMKSVDNFISRYERVVESLAALRMKAADFRQLKVIGRGAFGEVHLVRHTRTNTVYAMKMLNKDDMIKRADSAFFWEERDIMAHANSEWIVRLQYAFQDPRHLYMVMEYMPGGDLVNLMTSYEVSEKWTRFYTAEIVEALAALHSMGYIHRDVKPDNMLISISGHIKLADFGTCVKMNANGVVRCSTAVGTPDYISPEVLRNQGQDAEFGKEVDWWSVGVFIYEMLVGETPFYAEALVSTYTNIMNHKTSLKFPDEPLISTQAKDIIKKFLSAAPDRLGRNSVDDIRNHKFFVNDEWTFATLREASPPVIPSLKSDDDTTHFEEIETRDRDNAGDFQLPKTFNGNQLPFIGFTYSNEYSPVKNLLKGHGAGSKQNGIEQHKPQTVVEQPLTNGHASGVPEEKYEAVKMELDSKNREFELLKDSIARNEIRAKMIENEKNSLSTKISDLERELKDNKDKLRHGADSDAKVNELAVELRMSKEYNSEMESELSKFRDKCEQLKEDLRKKSGELAQEKNETQRVFQQKKDADEAFAEIKRDYELLQTRENEKSVQLKKALDERKENGAYQQSVAKATDAEWERKMQFYEKQLEHANDERKREEQKRTAAEFDQSRVARKLAGIEANYELLQNDYKSMKEARKDLERDLQDVITEKRRLEIRVEQLMDSRNTDERVLSLCQDELVESQEEAKYKEDGLRGKIDGFKHELENEKMKTQTLEENLLVADKERGMLKMEVQELMQRHKWEITNKDQTLKHLETQLDEIKQQSKIESSEQESNDKQTIADLRKKLDLEKAHKKAVINKLEEEMAKRQPLKKGEKGVTKSALIKKEREIMALEQERDTMSKRIAALFYENDKQAEHFNIAIQDMQTTQDALRDELKECKEELANRNVNTRYEDKRSLDSREGIPSSLSNQHIQMEGWLSLRDNTKKSRKPKWTNCFVALNEYSFTIYVDEKAVSVILLIEAGAMAHVRHVTAADLRNVDDSQLPKIFHIMYDDASCNSSRHASNSDLSMIESFREESWKRHDFQELSYHIRTFCDVCNKKLSDIIRPTPAFECKNCHFKTHKDHVAQGSLPMCRYNTGLSRELVLMAPQTDNCNKWVSQLRRFIESSRSAAVSVSRVSSRRHAPGSSNSSTIYQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1037	Phosphorylation	YDDASCNSSRHASNS ECCCCCCCCCCCCCC	32.83	19530675
1038	Phosphorylation	DDASCNSSRHASNSD CCCCCCCCCCCCCCC	17.69	19530675
1042	Phosphorylation	CNSSRHASNSDLSMI CCCCCCCCCCCHHHH	30.64	28854356
1044	Phosphorylation	SSRHASNSDLSMIES CCCCCCCCCHHHHHH	37.12	19530675
1047	Phosphorylation	HASNSDLSMIESFRE CCCCCCHHHHHHHHH	23.78	19530675

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
Oops, there are no upstream regulatory protein records of ROCK_CAEEL !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ROCK_CAEEL !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ROCK_CAEEL !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ROCK_CAEEL !!

Drug and Disease Associations

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

Regulatory Network of ROCK_CAEEL

Related Literatures of Post-Translational Modification