RMI1_HUMAN - dbPTM
RMI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RMI1_HUMAN
UniProt AC Q9H9A7
Protein Name RecQ-mediated genome instability protein 1
Gene Name RMI1
Organism Homo sapiens (Human).
Sequence Length 625
Subcellular Localization Nucleus . Forms foci in response to DNA damage.
Protein Description Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability..
Protein Sequence MNVTSIALRAETWLLAAWHVKVPPMWLEACINWIQEENNNVNLSQAQMNKQVFEQWLLTDLRDLEHPLLPDGILEIPKGELNGFYALQINSLVDVSQPAYSQIQKLRGKNTTNDLVTAEAQVTPKPWEAKPSRMLMLQLTDGIVQIQGMEYQPIPILHSDLPPGTKILIYGNISFRLGVLLLKPENVKVLGGEVDALLEEYAQEKVLARLIGEPDLVVSVIPNNSNENIPRVTDVLDPALGPSDEELLASLDENDELTANNDTSSERCFTTGSSSNTIPTRQSSFEPEFVISPRPKEEPSNLSIHVMDGELDDFSLEEALLLEETVQKEQMETKELQPLTFNRNADRSIERFSHNPNTTNNFSLTCKNGNNNWSEKNVSEQMTNEDKSFGCPSVRDQNRSIFSVHCNVPLAHDFTNKEKNLETDNKIKQTSSSDSHSLNNKILNREVVNYVQKRNSQISNENDCNLQSCSLRSSENSINLSIAMDLYSPPFVYLSVLMASKPKEVTTVKVKAFIVTLTGNLSSSGGIWSITAKVSDGTAYLDVDFVDEILTSLIGFSVPEMKQSKKDPLQYQKFLEGLQKCQRDLIDLCCLMTISFNPSLSKAMVLALQDVNMEHLENLKKRLNK
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-------MNVTSIAL
-------CCHHHHHH		9.0922814378
4Phosphorylation----MNVTSIALRAE
----CCHHHHHHHHH		14.9324719451
109UbiquitinationQIQKLRGKNTTNDLV
HHHHHCCCCCCCCCE		44.6933845483
111PhosphorylationQKLRGKNTTNDLVTA
HHHCCCCCCCCCEEE		30.38-
112PhosphorylationKLRGKNTTNDLVTAE
HHCCCCCCCCCEEEE		35.81-
123PhosphorylationVTAEAQVTPKPWEAK
EEEEEECCCCCCCCC		17.3225159151
125UbiquitinationAEAQVTPKPWEAKPS
EEEECCCCCCCCCCC		54.0929967540
130UbiquitinationTPKPWEAKPSRMLML
CCCCCCCCCCCEEEE		31.82-
132PhosphorylationKPWEAKPSRMLMLQL
CCCCCCCCCEEEEEE		29.61-
174PhosphorylationILIYGNISFRLGVLL
EEEECEEEEEEEEEE		14.3324719451
183UbiquitinationRLGVLLLKPENVKVL
EEEEEEECHHHEEEC		50.70-
205UbiquitinationLEEYAQEKVLARLIG
HHHHHHHHHHHHHHC		30.3921906983
219PhosphorylationGEPDLVVSVIPNNSN
CCCCEEEEEECCCCC		13.5729255136
225PhosphorylationVSVIPNNSNENIPRV
EEEECCCCCCCCCCC		52.7629255136
233PhosphorylationNENIPRVTDVLDPAL
CCCCCCCEECCCCCC		22.9726074081
243PhosphorylationLDPALGPSDEELLAS
CCCCCCCCHHHHHHC		56.7230278072
250PhosphorylationSDEELLASLDENDEL
CHHHHHHCCCCCCCC		36.0028102081
258PhosphorylationLDENDELTANNDTSS
CCCCCCCCCCCCCCC		25.8728634120
270PhosphorylationTSSERCFTTGSSSNT
CCCCCEECCCCCCCC		33.6026074081
271PhosphorylationSSERCFTTGSSSNTI
CCCCEECCCCCCCCC		18.1426074081
273PhosphorylationERCFTTGSSSNTIPT
CCEECCCCCCCCCCC		28.6225159151
274PhosphorylationRCFTTGSSSNTIPTR
CEECCCCCCCCCCCC		29.0225159151
275PhosphorylationCFTTGSSSNTIPTRQ
EECCCCCCCCCCCCC		39.4225159151
277PhosphorylationTTGSSSNTIPTRQSS
CCCCCCCCCCCCCCC		30.2226074081
280PhosphorylationSSSNTIPTRQSSFEP
CCCCCCCCCCCCCCC		37.1726074081
283PhosphorylationNTIPTRQSSFEPEFV
CCCCCCCCCCCCCEE		33.4330266825
284PhosphorylationTIPTRQSSFEPEFVI
CCCCCCCCCCCCEEE		25.8730266825
292PhosphorylationFEPEFVISPRPKEEP
CCCCEEECCCCCCCC		15.0030266825
334SumoylationQKEQMETKELQPLTF
HHHHHCCCCCCCCCC		43.02-
334SumoylationQKEQMETKELQPLTF
HHHHHCCCCCCCCCC		43.0228112733
334UbiquitinationQKEQMETKELQPLTF
HHHHHCCCCCCCCCC		43.0229967540
348PhosphorylationFNRNADRSIERFSHN
CCCCCCCCEECCCCC		29.3728102081
359PhosphorylationFSHNPNTTNNFSLTC
CCCCCCCCCCEEEEE		34.5025159151
363PhosphorylationPNTTNNFSLTCKNGN
CCCCCCEEEEEECCC		25.5425159151
374PhosphorylationKNGNNNWSEKNVSEQ
ECCCCCCCCCCHHHH		40.5921082442
376UbiquitinationGNNNWSEKNVSEQMT
CCCCCCCCCHHHHCC		58.0729967540
383PhosphorylationKNVSEQMTNEDKSFG
CCHHHHCCCCCHHCC		34.8429214152
387UbiquitinationEQMTNEDKSFGCPSV
HHCCCCCHHCCCCCH		41.3229967540
387SumoylationEQMTNEDKSFGCPSV
HHCCCCCHHCCCCCH		41.3228112733
388PhosphorylationQMTNEDKSFGCPSVR
HCCCCCHHCCCCCHH		38.9125159151
393PhosphorylationDKSFGCPSVRDQNRS
CHHCCCCCHHCCCCC		33.5826270265
400PhosphorylationSVRDQNRSIFSVHCN
CHHCCCCCEEEEECC		35.2230576142
403PhosphorylationDQNRSIFSVHCNVPL
CCCCCEEEEECCCCC		14.8528555341
415PhosphorylationVPLAHDFTNKEKNLE
CCCCCCCCCCCCCCC		51.98-
426SumoylationKNLETDNKIKQTSSS
CCCCCCCCCCCCCCC		54.8328112733
426UbiquitinationKNLETDNKIKQTSSS
CCCCCCCCCCCCCCC		54.8327667366
428UbiquitinationLETDNKIKQTSSSDS
CCCCCCCCCCCCCCC		49.4829967540
433PhosphorylationKIKQTSSSDSHSLNN
CCCCCCCCCCCCCHH		42.7925599653
435PhosphorylationKQTSSSDSHSLNNKI
CCCCCCCCCCCHHHH		19.5425599653
441UbiquitinationDSHSLNNKILNREVV
CCCCCHHHHHCHHHH		47.7127667366
450PhosphorylationLNREVVNYVQKRNSQ
HCHHHHHHHHHHCCC		7.8327642862
453AcetylationEVVNYVQKRNSQISN
HHHHHHHHHCCCCCC		43.4325953088
453UbiquitinationEVVNYVQKRNSQISN
HHHHHHHHHCCCCCC		43.4321906983
456PhosphorylationNYVQKRNSQISNEND
HHHHHHCCCCCCCCC		32.6830576142
459PhosphorylationQKRNSQISNENDCNL
HHHCCCCCCCCCCCC		30.3830576142
473PhosphorylationLQSCSLRSSENSINL
CCHHCCCCCCCCEEE		47.5030576142
474PhosphorylationQSCSLRSSENSINLS
CHHCCCCCCCCEEEH		34.0730576142
500PhosphorylationYLSVLMASKPKEVTT
EEEHHHCCCCCCCEE		35.2130576142
516PhosphorylationKVKAFIVTLTGNLSS
EEEEEEEEECCCCCC		17.4921406692
518PhosphorylationKAFIVTLTGNLSSSG
EEEEEEECCCCCCCC		18.0421406692
522PhosphorylationVTLTGNLSSSGGIWS
EEECCCCCCCCCEEE		26.8521406692
523PhosphorylationTLTGNLSSSGGIWSI
EECCCCCCCCCEEEE		35.8521406692
524PhosphorylationLTGNLSSSGGIWSIT
ECCCCCCCCCEEEEE		37.3521406692
529PhosphorylationSSSGGIWSITAKVSD
CCCCCEEEEEEEECC		14.2421406692
531PhosphorylationSGGIWSITAKVSDGT
CCCEEEEEEEECCCE		18.2121406692
535PhosphorylationWSITAKVSDGTAYLD
EEEEEEECCCEEEEC		29.6222210691
538PhosphorylationTAKVSDGTAYLDVDF
EEEECCCEEEECCHH		19.6721406692
540PhosphorylationKVSDGTAYLDVDFVD
EECCCEEEECCHHHH		11.8521406692
551PhosphorylationDFVDEILTSLIGFSV
HHHHHHHHHHHCCCH		27.4421406692
552PhosphorylationFVDEILTSLIGFSVP
HHHHHHHHHHCCCHH		17.9721406692
557PhosphorylationLTSLIGFSVPEMKQS
HHHHHCCCHHHHHHC		31.3922210691
566UbiquitinationPEMKQSKKDPLQYQK
HHHHHCCCCHHHHHH		70.5827667366
573UbiquitinationKDPLQYQKFLEGLQK
CCHHHHHHHHHHHHH		47.1629967540
580UbiquitinationKFLEGLQKCQRDLID
HHHHHHHHHHHHHHH		37.06-
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 RMI1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RMI1_HUMAN !!
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 RMI1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FANCM_HUMANFANCMphysical
20064461
BLM_HUMANBLMphysical
20064461
RMI2_HUMANRMI2physical
20064461
TOP3A_HUMANTOP3Aphysical
20064461
TOP3A_HUMANTOP3Aphysical
26186194
DCA15_HUMANDCAF15physical
26186194
DCA15_HUMANDCAF15physical
28514442
TOP3A_HUMANTOP3Aphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RMI1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND MASSSPECTROMETRY.

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