RNF17_HUMAN - dbPTM
RNF17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF17_HUMAN
UniProt AC Q9BXT8
Protein Name RING finger protein 17
Gene Name RNF17
Organism Homo sapiens (Human).
Sequence Length 1623
Subcellular Localization Cytoplasm. Nucleus. Predominantly found in the cytoplasm. Component of a nuage in male germ cells (an electron-dense spherical cytoplasmic body present in late pachytene and diplotene spermatocytes and in elonging spermatids) (By similarity)..
Protein Description Seems to be involved in regulation of transcriptional activity of MYC. In vitro, inhibits DNA-binding activity of Mad-MAX heterodimers. Can recruit Mad transcriptional repressors (MXD1, MXD3, MXD4 and MXI1) to the cytoplasm. May be involved in spermiogenesis (By similarity)..
Protein Sequence MAAEASKTGPSRSSYQRMGRKSQPWGAAEIQCTRCGRRVSRSSGHHCELQCGHAFCELCLLMTEECTTIICPDCEVATAVNTRQRYYPMAGYIKEDSIMEKLQPKTIKNCSQDFKKTADQLTTGLERSASTDKTLLNSSAVMLDTNTAEEIDEALNTAHHSFEQLSIAGKALEHMQKQTIEERERVIEVVEKQFDQLLAFFDSRKKNLCEEFARTTDDYLSNLIKAKSYIEEKKNNLNAAMNIARALQLSPSLRTYCDLNQIIRTLQLTSDSELAQVSSPQLRNPPRLSVNCSEIICMFNNMGKIEFRDSTKCYPQENEIRQNVQKKYNNKKELSCYDTYPPLEKKKVDMSVLTSEAPPPPLQPETNDVHLEAKNFQPQKDVATASPKTIAVLPQMGSSPDVIIEEIIEDNVESSAELVFVSHVIDPCHFYIRKYSQIKDAKVLEKKVNEFCNRSSHLDPSDILELGARIFVSSIKNGMWCRGTITELIPIEGRNTRKPCSPTRLFVHEVALIQIFMVDFGNSEVLIVTGVVDTHVRPEHSAKQHIALNDLCLVLRKSEPYTEGLLKDIQPLAQPCSLKDIVPQNSNEGWEEEAKVEFLKMVNNKAVSMKVFREEDGVLIVDLQKPPPNKISSDMPVSLRDALVFMELAKFKSQSLRSHFEKNTTLHYHPPILPKEMTDVSVTVCHINSPGDFYLQLIEGLDILFLLKTIEEFYKSEDGENLEILCPVQDQACVAKFEDGIWYRAKVIGLPGHQEVEVKYVDFGNTAKITIKDVRKIKDEFLNAPEKAIKCKLAYIEPYKRTMQWSKEAKEKFEEKAQDKFMTCSVIKILEDNVLLVELFDSLGAPEMTTTSINDQLVKEGLASYEIGYILKDNSQKHIEVWDPSPEEIISNEVHNLNPVSAKSLPNENFQSLYNKELPVHICNVISPEKIYVQWLLTENLLNSLEEKMIAAYENSKWEPVKWENDMHCAVKIQDKNQWRRGQIIRMVTDTLVEVLLYDVGVELVVNVDCLRKLEENLKTMGRLSLECSLVDIRPAGGSDKWTATACDCLSLYLTGAVATIILQVDSEENNTTWPLPVKIFCRDEKGERVDVSKYLIKKGLALRERRINNLDNSHSLSEKSLEVPLEQEDSVVTNCIKTNFDPDKKTADIISEQKVSEFQEKILEPRTTRGYKPPAIPNMNVFEATVSCVGDDGTIFVVPKLSEFELIKMTNEIQSNLKCLGLLEPYFWKKGEACAVRGSDTLWYRGKVMEVVGGAVRVQYLDHGFTEKIPQCHLYPILLYPDIPQFCIPCQLHNTTPVGNVWQPDAIEVLQQLLSKRQVDIHIMELPKNPWEKLSIHLYFDGMSLSYFMAYYKYCTSEHTEEMLKEKPRSDHDKKYEEEQWEIRFEELLSAETDTPLLPPYLSSSLPSPGELYAVQVKHVVSPNEVYICLDSIETSNQSNQHSDTDDSGVSGESESESLDEALQRVNKKVEALPPLTDFRTEMPCLAEYDDGLWYRAKIVAIKEFNPLSILVQFVDYGSTAKLTLNRLCQIPSHLMRYPARAIKVLLAGFKPPLRDLGETRIPYCPKWSMEALWAMIDCLQGKQLYAVSMAPAPEQIVTLYDDEQHPVHMPLVEMGLADKDE
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
86PhosphorylationAVNTRQRYYPMAGYI
HCCCCCCCCCCCCCC		12.0025003641
87PhosphorylationVNTRQRYYPMAGYIK
CCCCCCCCCCCCCCC		6.6825463755
97PhosphorylationAGYIKEDSIMEKLQP
CCCCCHHHHHHHHCC		25.5625003641
122PhosphorylationKKTADQLTTGLERSA
HHHHHHHHHHHHHCC		17.1228192239
130PhosphorylationTGLERSASTDKTLLN
HHHHHCCCCCCHHHC		38.0828192239
179PhosphorylationLEHMQKQTIEERERV
HHHHHHHCHHHHHHH		37.0726091039
203PhosphorylationQLLAFFDSRKKNLCE
HHHHHHHHHCCHHHH		40.62-
215PhosphorylationLCEEFARTTDDYLSN
HHHHHHHCCHHHHHH		31.0224719451
219PhosphorylationFARTTDDYLSNLIKA
HHHCCHHHHHHHHHH		18.1624719451
234AcetylationKSYIEEKKNNLNAAM
HHHHHHHHCHHHHHH		55.11-
250PhosphorylationIARALQLSPSLRTYC
HHHHHHCCHHHHHHC		10.2429396449
252PhosphorylationRALQLSPSLRTYCDL
HHHHCCHHHHHHCCH		27.4029396449
436 (in isoform 2)Phosphorylation-28.5925849741
484PhosphorylationNGMWCRGTITELIPI
CCCEECCEEEEEEEC		12.8422210691
486PhosphorylationMWCRGTITELIPIEG
CEECCEEEEEEECCC		25.2822210691
496PhosphorylationIPIEGRNTRKPCSPT
EECCCCCCCCCCCCC		38.4122210691
600AcetylationEAKVEFLKMVNNKAV
HHHHHHHHHHCCCEE		46.232520689
632PhosphorylationKPPPNKISSDMPVSL
CCCCCCCCCCCCCCH		23.1528348404
633PhosphorylationPPPNKISSDMPVSLR
CCCCCCCCCCCCCHH		41.2124719451
760PhosphorylationHQEVEVKYVDFGNTA
CCEEEEEEEECCCEE		15.49-
770PhosphorylationFGNTAKITIKDVRKI
CCCEEEEEHHHHHHH		22.6724719451
806PhosphorylationYKRTMQWSKEAKEKF
CHHHHHCCHHHHHHH		12.0622210691
1147PhosphorylationNFDPDKKTADIISEQ
CCCCCCCHHHHHCHH		34.9930622161
1152PhosphorylationKKTADIISEQKVSEF
CCHHHHHCHHHHHHH		34.0223532336
1157PhosphorylationIISEQKVSEFQEKIL
HHCHHHHHHHHHHHC		39.4630622161
1240PhosphorylationEACAVRGSDTLWYRG
CCCEECCCCCEEECC		19.50-
1242PhosphorylationCAVRGSDTLWYRGKV
CEECCCCCEEECCEE		22.38-
1245PhosphorylationRGSDTLWYRGKVMEV
CCCCCEEECCEEEEE		16.7618083107
1281PhosphorylationHLYPILLYPDIPQFC
CEEEEEECCCCCCCC		8.73-
1316PhosphorylationEVLQQLLSKRQVDIH
HHHHHHHHHCCCEEE		34.0924719451
1336PhosphorylationKNPWEKLSIHLYFDG
CCHHHHCEEEEEECC		21.0124260401
1340PhosphorylationEKLSIHLYFDGMSLS
HHCEEEEEECCCCHH		5.8625884760
1345PhosphorylationHLYFDGMSLSYFMAY
EEEECCCCHHHHHHH		21.5024260401
1348PhosphorylationFDGMSLSYFMAYYKY
ECCCCHHHHHHHHHH		11.5825884760
1561PhosphorylationPLRDLGETRIPYCPK
CHHHCCCCCCCCCCC		31.91-
1602PhosphorylationPEQIVTLYDDEQHPV
CHHEEEEECCCCCCC		16.3918083107
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 RNF17_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF17_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 RNF17_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RNF17_HUMAN !!
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNF17_HUMAN

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Related Literatures of Post-Translational Modification

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