ANPRB_HUMAN - dbPTM
ANPRB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANPRB_HUMAN
UniProt AC P20594
Protein Name Atrial natriuretic peptide receptor 2
Gene Name NPR2
Organism Homo sapiens (Human).
Sequence Length 1047
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth..
Protein Sequence MALPSLLLLVAALAGGVRPPGARNLTLAVVLPEHNLSYAWAWPRVGPAVALAVEALGRALPVDLRFVSSELEGACSEYLAPLSAVDLKLYHDPDLLLGPGCVYPAASVARFASHWRLPLLTAGAVASGFSAKNDHYRTLVRTGPSAPKLGEFVVTLHGHFNWTARAALLYLDARTDDRPHYFTIEGVFEALQGSNLSVQHQVYAREPGGPEQATHFIRANGRIVYICGPLEMLHEILLQAQRENLTNGDYVFFYLDVFGESLRAGPTRATGRPWQDNRTREQAQALREAFQTVLVITYREPPNPEYQEFQNRLLIRAREDFGVELGPSLMNLIAGCFYDGILLYAEVLNETIQEGGTREDGLRIVEKMQGRRYHGVTGLVVMDKNNDRETDFVLWAMGDLDSGDFQPAAHYSGAEKQIWWTGRPIPWVKGAPPSDNPPCAFDLDDPSCDKTPLSTLAIVALGTGITFIMFGVSSFLIFRKLMLEKELASMLWRIRWEELQFGNSERYHKGAGSRLTLSLRGSSYGSLMTAHGKYQIFANTGHFKGNVVAIKHVNKKRIELTRQVLFELKHMRDVQFNHLTRFIGACIDPPNICIVTEYCPRGSLQDILENDSINLDWMFRYSLINDLVKGMAFLHNSIISSHGSLKSSNCVVDSRFVLKITDYGLASFRSTAEPDDSHALYAKKLWTAPELLSGNPLPTTGMQKADVYSFGIILQEIALRSGPFYLEGLDLSPKEIVQKVRNGQRPYFRPSIDRTQLNEELVLLMERCWAQDPAERPDFGQIKGFIRRFNKEGGTSILDNLLLRMEQYANNLEKLVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAIIDNFDVYKVETIGDAYMVVSGLPGRNGQRHAPEIARMALALLDAVSSFRIRHRPHDQLRLRIGVHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGQALKIHVSSTTKDALDELGCFQLELRGDVEMKGKGKMRTYWLLGERKGPPGLL
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
24N-linked_GlycosylationVRPPGARNLTLAVVL
CCCCCCCCEEEEEEE		36.52UniProtKB CARBOHYD
35N-linked_GlycosylationAVVLPEHNLSYAWAW
EEEECCCCCCEECCC		29.08UniProtKB CARBOHYD
142PhosphorylationHYRTLVRTGPSAPKL
CHHEEEECCCCCCCC		46.0627251275
145PhosphorylationTLVRTGPSAPKLGEF
EEEECCCCCCCCCEE		59.5627251275
161N-linked_GlycosylationVTLHGHFNWTARAAL
EEECCCCCHHHEEHH		29.52UniProtKB CARBOHYD
163PhosphorylationLHGHFNWTARAALLY
ECCCCCHHHEEHHHH		13.84113307035
195N-linked_GlycosylationFEALQGSNLSVQHQV
HHHHCCCCCEEEEEE		43.06UniProtKB CARBOHYD
244N-linked_GlycosylationLLQAQRENLTNGDYV
HHHHHHHCCCCCCEE		55.12UniProtKB CARBOHYD
250PhosphorylationENLTNGDYVFFYLDV
HCCCCCCEEEEEEEC		10.6822617229
277N-linked_GlycosylationTGRPWQDNRTREQAQ
CCCCCCCCCHHHHHH		31.93UniProtKB CARBOHYD
323UbiquitinationRAREDFGVELGPSLM
HHHHHHCCCCCHHHH		5.7623000965
326UbiquitinationEDFGVELGPSLMNLI
HHHCCCCCHHHHHHH		9.0323000965
349N-linked_GlycosylationLLYAEVLNETIQEGG
HHHHHHHHHHHHCCC		49.92UniProtKB CARBOHYD
462UbiquitinationTLAIVALGTGITFIM
HHHHHHHCCCCHHHH		16.5023000965
465UbiquitinationIVALGTGITFIMFGV
HHHHCCCCHHHHCCH		2.6023000965
489PhosphorylationMLEKELASMLWRIRW
HHHHHHHHHHHHHHH		27.3422590601
505UbiquitinationELQFGNSERYHKGAG
HHHCCCCCCCCCCCC		62.3522817900
508UbiquitinationFGNSERYHKGAGSRL
CCCCCCCCCCCCCCE		28.4422817900
513PhosphorylationRYHKGAGSRLTLSLR
CCCCCCCCCEEEEEC		24.4720977274
516PhosphorylationKGAGSRLTLSLRGSS
CCCCCCEEEEECCCC		17.1220977274
518PhosphorylationAGSRLTLSLRGSSYG
CCCCEEEEECCCCCC		15.7020977274
522PhosphorylationLTLSLRGSSYGSLMT
EEEEECCCCCCCCEE		17.6020639409
523PhosphorylationTLSLRGSSYGSLMTA
EEEECCCCCCCCEEC		36.0220977274
526PhosphorylationLRGSSYGSLMTAHGK
ECCCCCCCCEECCEE		13.5120977274
529PhosphorylationSSYGSLMTAHGKYQI
CCCCCCEECCEEEEE		22.3122870295
561PhosphorylationNKKRIELTRQVLFEL
CHHHHHHHHHHHHHH		13.28113307043
621PhosphorylationNLDWMFRYSLINDLV
CHHHHHHHHHHHHHH		9.1422210691
622PhosphorylationLDWMFRYSLINDLVK
HHHHHHHHHHHHHHH		20.6522210691
644UbiquitinationSIISSHGSLKSSNCV
HHHHCCCCCCCCCEE		27.4822817900
647UbiquitinationSSHGSLKSSNCVVDS
HCCCCCCCCCEEEEC		31.8822817900
667PhosphorylationITDYGLASFRSTAEP
ECCCCCCCCCCCCCC		26.6624719451
684UbiquitinationSHALYAKKLWTAPEL
CHHHHHHHCCCCHHH		40.8830230243
687UbiquitinationLYAKKLWTAPELLSG
HHHHHCCCCHHHHCC		42.6530230243
739UbiquitinationSPKEIVQKVRNGQRP
CHHHHHHHHHCCCCC		32.0632142685
742UbiquitinationEIVQKVRNGQRPYFR
HHHHHHHCCCCCCCC		54.6732142685
747PhosphorylationVRNGQRPYFRPSIDR
HHCCCCCCCCCCCCC		17.897348343
791UbiquitinationGFIRRFNKEGGTSIL
HHHHHHCCCCCCCHH		55.8323000965
794UbiquitinationRRFNKEGGTSILDNL
HHHCCCCCCCHHHHH		19.8523000965
796PhosphorylationFNKEGGTSILDNLLL
HCCCCCCCHHHHHHH		25.1617081983
808PhosphorylationLLLRMEQYANNLEKL
HHHHHHHHHHHHHHH		9.6755861427
820PhosphorylationEKLVEERTQAYLEEK
HHHHHHHHHHHHHHH		22.34-
912PhosphorylationVETIGDAYMVVSGLP
EEEECCEEEEECCCC		8.65-
973UbiquitinationCAGVVGLKMPRYCLF
EEEECCCCCCCEEEE		40.7122817900
976UbiquitinationVVGLKMPRYCLFGDT
ECCCCCCCEEEECCC		31.1622817900
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 ANPRB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANPRB_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 ANPRB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANFC_HUMANNPPCphysical
1309330
ANFB_HUMANNPPBphysical
1309330
ANF_HUMANNPPAphysical
1309330
ANF_HUMANNPPAphysical
1660465
ANFB_HUMANNPPBphysical
1660465
ANFC_HUMANNPPCphysical
1660465
ANF_HUMANNPPAphysical
1672777
ANFB_HUMANNPPBphysical
1672777
ANFC_HUMANNPPCphysical
1672777
Drug and Disease Associations
Kegg Disease
H00470 Acromesomelic dysplasia, Maroteaux type
OMIM Disease
602875Acromesomelic dysplasia, Maroteaux type (AMDM)
615923Epiphyseal chondrodysplasia, Miura type (ECDM)
Kegg Drug
D10063 Cenderitide (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANPRB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Mass spectrometric identification of phosphorylation sites inguanylyl cyclase A and B.";
Yoder A.R., Stone M.D., Griffin T.J., Potter L.R.;
Biochemistry 49:10137-10145(2010).
Cited for: PHOSPHORYLATION AT SER-513; THR-516; SER-518; SER-523; SER-526 ANDTHR-529.

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