ROM1_YEAST - dbPTM
ROM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ROM1_YEAST
UniProt AC P53046
Protein Name RHO1 GDP-GTP exchange protein 1
Gene Name ROM1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1155
Subcellular Localization
Protein Description Stimulates the exchange of RHO1 GDP-bound form into GTP-bound form..
Protein Sequence MNSNELDLRNKYFYEIFGKKRKSDTSTPTQLFSGSKVQTNINEISITNDEDEDSTEDENKASLKDYTLGHDTGARYRIAPDCSSHQLKASPVLHISTNLNSSPQSFTGDQISPTNKKISINDSTRQDKGNSCTTTSSPSQKRSNVLLPHVRKHSSPSLLSFSKNSGSHMGDPNQLSTPPTPKSAGHTMELHSSFNGKHSSSSTSSLFALESLKTQNRRSSNSSNHSSQYRRHTNQHQRHHSRSKSSPVSLTEISMIKGTPLVYPALLSLIAIKFKQTIKLSTHKKMGLLYRDSFTGKQAIDTLCLIIGSLDRNLGMLIGKSLEAQKLFHDVLYDHGVRDSVLEIYELSSESIFMAHQSQSSTSIANTFSSSSSSVNSLRTKTEIYGVFVPLTHCYSSTCSLEKLCYSISCPNRLQQQANLHLKLGGGLKRNISLALDKEDDERISWTNSVPKSVWESLSKQQIKRQEAIYELFTTEKKFVKSLEIIRDTFMKKLLETNIIPSDVRINFVKHVFAHINEIYSVNREFLKALAQRQSLSPICPGIADIFLQYLPFFDPFLSYIASRPYAKYLIETQRSVNPNFARFDDEVSNSSLRHGIDSFLSQGVSRPGRYSLLVREIIHFSDPVTDKDDLQMLMKVQDLLKDLMKRIDRASGAAQDRYDVKVLKQKILFKNEYVNLGLNNEKRKIKHEGLLSRKDVNKTDASFSGDIQFYLLDNMLLFLKSKAVNKWHQHTVFQRPIPLPLLFICPAEDMPPIKRYVTENPNCSAGVLLPQYQTSNPKNAIVFAYYGTKQQYQVTLYAPQPAGLQTLIEKVKQEQKRLLDETKHITFKQMVGQFFHSYINTNRVNDVLICHAGKILLVATNMGLFVLNYATSINQKPVHLLHKISISQISVLEEYKVMILLIDKKLYGCPLDVIDDAENADFLFRKNSKVLFKYVAMFKDGFCNGKRIIMIAHHFLHAVQLLIVNPLIFDFNSGNFKKNLKAGLVDFSVDSEPLSFSFLENKICIGCKKNIKILNVPEVCDKNGFKMRELLNLHDNKVLANMYKETFKVVSMFPIKNSTFACFPELCFFLNKQGKREETKGCFHWEGEPEQFACSYPYIVAINSNFIEIRHIENGELVRCVLGNKIRMLKSYAKKILYCYEDPQGFEIIELLNF
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 Orthologous
Protein Cluster
1Acetylation-------MNSNELDL
-------CCCCHHHH		50.0422814378
112PhosphorylationSFTGDQISPTNKKIS
CCCCCCCCCCCCEEE		21.7525752575
114PhosphorylationTGDQISPTNKKISIN
CCCCCCCCCCEEEEC		53.5321440633
134PhosphorylationDKGNSCTTTSSPSQK
CCCCCCCCCCCHHHH		29.0730377154
136PhosphorylationGNSCTTTSSPSQKRS
CCCCCCCCCHHHHCC		37.8530377154
137PhosphorylationNSCTTTSSPSQKRSN
CCCCCCCCHHHHCCC		26.8628889911
154PhosphorylationLPHVRKHSSPSLLSF
CCHHHCCCCCCHHCC		47.1628889911
155PhosphorylationPHVRKHSSPSLLSFS
CHHHCCCCCCHHCCC		20.4421440633
157PhosphorylationVRKHSSPSLLSFSKN
HHCCCCCCHHCCCCC		43.8424961812
165PhosphorylationLLSFSKNSGSHMGDP
HHCCCCCCCCCCCCH		45.4622369663
167PhosphorylationSFSKNSGSHMGDPNQ
CCCCCCCCCCCCHHH		15.3222369663
176PhosphorylationMGDPNQLSTPPTPKS
CCCHHHCCCCCCCCC		29.1522369663
177PhosphorylationGDPNQLSTPPTPKSA
CCHHHCCCCCCCCCC		41.7121440633
180PhosphorylationNQLSTPPTPKSAGHT
HHCCCCCCCCCCCCC		44.5522369663
183PhosphorylationSTPPTPKSAGHTMEL
CCCCCCCCCCCCEEE		40.4628889911
199PhosphorylationSSFNGKHSSSSTSSL
CCCCCCCCCCCHHHH		35.0922369663
200PhosphorylationSFNGKHSSSSTSSLF
CCCCCCCCCCHHHHH		28.2021440633
201PhosphorylationFNGKHSSSSTSSLFA
CCCCCCCCCHHHHHH		40.4222369663
202PhosphorylationNGKHSSSSTSSLFAL
CCCCCCCCHHHHHHH		33.9722369663
203PhosphorylationGKHSSSSTSSLFALE
CCCCCCCHHHHHHHH		25.0422369663
204PhosphorylationKHSSSSTSSLFALES
CCCCCCHHHHHHHHH		27.3022369663
205PhosphorylationHSSSSTSSLFALESL
CCCCCHHHHHHHHHH		27.8222369663
220PhosphorylationKTQNRRSSNSSNHSS
HHCCCCCCCCCCCHH		38.6328889911
243PhosphorylationHQRHHSRSKSSPVSL
HHHHHCCCCCCCCCH		39.6530377154
245PhosphorylationRHHSRSKSSPVSLTE
HHHCCCCCCCCCHHH		40.9128152593
246PhosphorylationHHSRSKSSPVSLTEI
HHCCCCCCCCCHHHH		32.8125752575
249PhosphorylationRSKSSPVSLTEISMI
CCCCCCCCHHHHHCC		32.7229734811
433PhosphorylationGGLKRNISLALDKED
CHHHCEEEEEECCCC		15.9028889911
700PhosphorylationSRKDVNKTDASFSGD
CCCCCCCCCCCCCCC		31.4319779198
703PhosphorylationDVNKTDASFSGDIQF
CCCCCCCCCCCCCEE		23.8219779198
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 ROM1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ROM1_YEAST !!
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 ROM1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ROM2_YEASTROM2genetic
8641285
CSG2_YEASTCSG2genetic
20093466
YBQ6_YEASTYBR056Wgenetic
20093466
YBU0_YEASTYBR090Cgenetic
20093466
RL41A_YEASTRPL41Agenetic
20093466
RL41B_YEASTRPL41Agenetic
20093466
TRM3_YEASTTRM3genetic
20093466
PEX19_YEASTPEX19genetic
20093466
MSC2_YEASTMSC2genetic
20093466
LSM6_YEASTLSM6genetic
20093466
SNF6_YEASTSNF6genetic
20093466
SWI6_YEASTSWI6genetic
20093466
ROM2_YEASTROM2genetic
20093466
INO4_YEASTINO4genetic
20093466
BUD21_YEASTBUD21genetic
20093466
LRG1_YEASTLRG1genetic
19339687
SAC7_YEASTSAC7genetic
19339687
RHO1_YEASTRHO1genetic
19339687
TUS1_YEASTTUS1genetic
19339687
KPC1_YEASTPKC1genetic
11554924
ROM2_YEASTROM2genetic
22344253
LRG1_YEASTLRG1genetic
22344253
SNF5_YEASTSNF5genetic
27708008
YD338_YEASTYDR338Cgenetic
27708008
APN2_YEASTAPN2genetic
27708008
CSG2_YEASTCSG2genetic
27708008
YBQ6_YEASTYBR056Wgenetic
27708008
SGF29_YEASTSGF29genetic
27708008
GPR1_YEASTGPR1genetic
27708008
PEX19_YEASTPEX19genetic
27708008
TRM3_YEASTTRM3genetic
27708008
RL41A_YEASTRPL41Agenetic
27708008
RL41B_YEASTRPL41Agenetic
27708008
MSC2_YEASTMSC2genetic
27708008
SNF6_YEASTSNF6genetic
27708008
PTH_YEASTPTH1genetic
27708008
SRN2_YEASTSRN2genetic
27708008
ROM2_YEASTROM2genetic
27708008
IMP2_YEASTIMP2genetic
27708008
EAF7_YEASTEAF7genetic
27708008
INO4_YEASTINO4genetic
27708008
2ABA_YEASTCDC55genetic
26728856
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ROM1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-202; SER-245AND SER-433, AND MASS SPECTROMETRY.

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