CNNM4_HUMAN - dbPTM
CNNM4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNNM4_HUMAN
UniProt AC Q6P4Q7
Protein Name Metal transporter CNNM4
Gene Name CNNM4
Organism Homo sapiens (Human).
Sequence Length 775
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Probable metal transporter. The interaction with the metal ion chaperone COX11 suggests that it may play a role in sensory neuron functions (By similarity). May play a role in biomineralization and retinal function..
Protein Sequence MAPVGGGGRPVGGPARGRLLLAAPVLLVLLWALGARGQGSPQQGTIVGMRLASCNKSCGTNPDGIIFVSEGSTVNLRLYGYSLGNISSNLISFTEVDDAETLHKSTSCLELTKDLVVQQLVNVSRGNTSGVLVVLTKFLRRSESMKLYALCTRAQPDGPWLKWTDKDSLLFMVEEPGRFLPLWLHILLITVLLVLSGIFSGLNLGLMALDPMELRIVQNCGTEKERRYARKIEPIRRKGNYLLCSLLLGNVLVNTSLTILLDNLIGSGLMAVASSTIGIVIFGEILPQALCSRHGLAVGANTILLTKFFMLLTFPLSFPISKLLDFFLGQEIRTVYNREKLMEMLKVTEPYNDLVKEELNMIQGALELRTKTVEDIMTQLQDCFMIRSDAILDFNTMSEIMESGYTRIPVFEDEQSNIVDILYVKDLAFVDPDDCTPLKTITRFYNHPVHFVFHDTKLDAMLEEFKKGKSHLAIVQKVNNEGEGDPFYEVLGLVTLEDVIEEIIKSEILDESDMYTDNRSRKRVSEKNKRDFSAFKDADNELKVKISPQLLLAAHRFLATEVSQFSPSLISEKILLRLLKYPDVIQELKFDEHNKYYARHYLYTRNKPADYFILILQGKVEVEAGKENMKFETGAFSYYGTMALTSVPSDRSPAHPTPLSRSASLSYPDRTDVSTAATLAGSSNQFGSSVLGQYISDFSVRALVDLQYIKITRQQYQNGLLASRMENSPQFPIDGCTTHMENLAEKSELPVVDETTTLLNERNSLLHKASHENAI
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
85N-linked_GlycosylationLYGYSLGNISSNLIS
EEEEECCCCCCCEEC		35.94UniProtKB CARBOHYD
122N-linked_GlycosylationLVVQQLVNVSRGNTS
HHHHHHHHHCCCCCH		34.34UniProtKB CARBOHYD
127N-linked_GlycosylationLVNVSRGNTSGVLVV
HHHHCCCCCHHHHHH		29.93-
127N-linked_GlycosylationLVNVSRGNTSGVLVV
HHHHCCCCCHHHHHH		29.9319349973
148PhosphorylationRSESMKLYALCTRAQ
HCCCCHHHHHHHHCC		7.63-
224UbiquitinationVQNCGTEKERRYARK
HHCCCCHHHHHHHHC		57.2533845483
2242-HydroxyisobutyrylationVQNCGTEKERRYARK
HHCCCCHHHHHHHHC		57.25-
340UbiquitinationRTVYNREKLMEMLKV
HHHHCHHHHHHHHHC		50.3129901268
346UbiquitinationEKLMEMLKVTEPYND
HHHHHHHHCCCCHHH		45.8932015554
351PhosphorylationMLKVTEPYNDLVKEE
HHHCCCCHHHHHHHH		18.3128796482
356UbiquitinationEPYNDLVKEELNMIQ
CCHHHHHHHHHHHHH		53.4129967540
398PhosphorylationILDFNTMSEIMESGY
CCCCCCHHHHHHHCC		23.1827251275
403PhosphorylationTMSEIMESGYTRIPV
CHHHHHHHCCCEEEE		21.5127251275
406PhosphorylationEIMESGYTRIPVFED
HHHHHCCCEEEECCC		26.1627251275
416PhosphorylationPVFEDEQSNIVDILY
EECCCCCCCEEEEEE		26.8628348404
423PhosphorylationSNIVDILYVKDLAFV
CCEEEEEEEEECEEC		13.0427762562
439UbiquitinationPDDCTPLKTITRFYN
CCCCCCCHHHHHHHC		38.8029901268
440PhosphorylationDDCTPLKTITRFYNH
CCCCCCHHHHHHHCC		34.9527762562
442PhosphorylationCTPLKTITRFYNHPV
CCCCHHHHHHHCCCE		21.6927762562
466UbiquitinationDAMLEEFKKGKSHLA
HHHHHHHHCCCCEEE		64.99-
469UbiquitinationLEEFKKGKSHLAIVQ
HHHHHCCCCEEEEEE		43.5129901268
470PhosphorylationEEFKKGKSHLAIVQK
HHHHCCCCEEEEEEC		32.1924114839
512PhosphorylationKSEILDESDMYTDNR
HCCCCCHHHCCCCCH		27.6121815630
515PhosphorylationILDESDMYTDNRSRK
CCCHHHCCCCCHHHH		18.8729978859
516PhosphorylationLDESDMYTDNRSRKR
CCHHHCCCCCHHHHC		21.8429978859
520PhosphorylationDMYTDNRSRKRVSEK
HCCCCCHHHHCHHHH		48.7025849741
533PhosphorylationEKNKRDFSAFKDADN
HHHHHCCHHHCCCCC		36.76-
536UbiquitinationKRDFSAFKDADNELK
HHCCHHHCCCCCCCE		52.2933845483
543UbiquitinationKDADNELKVKISPQL
CCCCCCCEEECCHHH		34.9933845483
547PhosphorylationNELKVKISPQLLLAA
CCCEEECCHHHHHHH		10.8123312004
560PhosphorylationAAHRFLATEVSQFSP
HHHHHHHHHHHHCCH		38.7820068231
563PhosphorylationRFLATEVSQFSPSLI
HHHHHHHHHCCHHHH		21.1920068231
566PhosphorylationATEVSQFSPSLISEK
HHHHHHCCHHHHCHH		13.1228348404
568PhosphorylationEVSQFSPSLISEKIL
HHHHCCHHHHCHHHH		36.8220068231
571PhosphorylationQFSPSLISEKILLRL
HCCHHHHCHHHHHHH		37.8220068231
596PhosphorylationKFDEHNKYYARHYLY
CCCCCCCCCHHHHHH		14.0028152594
597PhosphorylationFDEHNKYYARHYLYT
CCCCCCCCHHHHHHH		9.9628152594
601PhosphorylationNKYYARHYLYTRNKP
CCCCHHHHHHHCCCC		8.89-
603PhosphorylationYYARHYLYTRNKPAD
CCHHHHHHHCCCCCC		9.11-
607UbiquitinationHYLYTRNKPADYFIL
HHHHHCCCCCCEEEE		37.9933845483
611PhosphorylationTRNKPADYFILILQG
HCCCCCCEEEEEEEC		8.47-
645PhosphorylationYYGTMALTSVPSDRS
ECEEEEEECCCCCCC		20.38-
646PhosphorylationYGTMALTSVPSDRSP
CEEEEEECCCCCCCC		32.64-
652PhosphorylationTSVPSDRSPAHPTPL
ECCCCCCCCCCCCCC		31.2823663014
657PhosphorylationDRSPAHPTPLSRSAS
CCCCCCCCCCCCCCC		27.3128348404
660PhosphorylationPAHPTPLSRSASLSY
CCCCCCCCCCCCCCC		25.9523401153
662PhosphorylationHPTPLSRSASLSYPD
CCCCCCCCCCCCCCC		20.8730266825
664PhosphorylationTPLSRSASLSYPDRT
CCCCCCCCCCCCCCC		21.0623401153
666PhosphorylationLSRSASLSYPDRTDV
CCCCCCCCCCCCCCC		31.9330266825
667PhosphorylationSRSASLSYPDRTDVS
CCCCCCCCCCCCCCC		17.9129396449
671PhosphorylationSLSYPDRTDVSTAAT
CCCCCCCCCCCHHHH		48.4028102081
674PhosphorylationYPDRTDVSTAATLAG
CCCCCCCCHHHHHCC		18.3528102081
675PhosphorylationPDRTDVSTAATLAGS
CCCCCCCHHHHHCCC		21.8428102081
682PhosphorylationTAATLAGSSNQFGSS
HHHHHCCCCCCCCCH		22.1028348404
683PhosphorylationAATLAGSSNQFGSSV
HHHHCCCCCCCCCHH		33.4624719451
688PhosphorylationGSSNQFGSSVLGQYI
CCCCCCCCHHHHHHH		20.6829802988
689PhosphorylationSSNQFGSSVLGQYIS
CCCCCCCHHHHHHHC		23.0328348404
696PhosphorylationSVLGQYISDFSVRAL
HHHHHHHCCCCHHHH		27.8922210691
699PhosphorylationGQYISDFSVRALVDL
HHHHCCCCHHHHEEH		18.7122210691
708PhosphorylationRALVDLQYIKITRQQ
HHHEEHHEEEEEHHH		16.1022210691
728PhosphorylationLASRMENSPQFPIDG
HHHHCCCCCCCCCCC		13.5325159151
737PhosphorylationQFPIDGCTTHMENLA
CCCCCCHHHHHHHHH		25.8427251275
738PhosphorylationFPIDGCTTHMENLAE
CCCCCHHHHHHHHHH		24.2527251275
755PhosphorylationELPVVDETTTLLNER
CCCCCCHHHHHHHHH		22.1830108239
756PhosphorylationLPVVDETTTLLNERN
CCCCCHHHHHHHHHH		17.2530108239
757PhosphorylationPVVDETTTLLNERNS
CCCCHHHHHHHHHHH		36.3530266825
764PhosphorylationTLLNERNSLLHKASH
HHHHHHHHHHHHHHH		38.2330266825
768UbiquitinationERNSLLHKASHENAI
HHHHHHHHHHHHCCC		52.1029967540
770PhosphorylationNSLLHKASHENAI--
HHHHHHHHHHCCC--		35.8228348404
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 CNNM4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNNM4_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 CNNM4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CNNM4_HUMAN !!
Drug and Disease Associations
Kegg Disease
H01015 Jalili syndrome
OMIM Disease
217080Jalili syndrome (JALIS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNNM4_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory