I12R2_HUMAN - dbPTM
I12R2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID I12R2_HUMAN
UniProt AC Q99665
Protein Name Interleukin-12 receptor subunit beta-2
Gene Name IL12RB2
Organism Homo sapiens (Human).
Sequence Length 862
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Receptor for interleukin-12. This subunit is the signaling component coupling to the JAK2/STAT4 pathway. Promotes the proliferation of T-cells as well as NK cells. Induces the promotion of T-cells towards the Th1 phenotype by strongly enhancing IFN-gamma production..
Protein Sequence MAHTFRGCSLAFMFIITWLLIKAKIDACKRGDVTVKPSHVILLGSTVNITCSLKPRQGCFHYSRRNKLILYKFDRRINFHHGHSLNSQVTGLPLGTTLFVCKLACINSDEIQICGAEIFVGVAPEQPQNLSCIQKGEQGTVACTWERGRDTHLYTEYTLQLSGPKNLTWQKQCKDIYCDYLDFGINLTPESPESNFTAKVTAVNSLGSSSSLPSTFTFLDIVRPLPPWDIRIKFQKASVSRCTLYWRDEGLVLLNRLRYRPSNSRLWNMVNVTKAKGRHDLLDLKPFTEYEFQISSKLHLYKGSWSDWSESLRAQTPEEEPTGMLDVWYMKRHIDYSRQQISLFWKNLSVSEARGKILHYQVTLQELTGGKAMTQNITGHTSWTTVIPRTGNWAVAVSAANSKGSSLPTRINIMNLCEAGLLAPRQVSANSEGMDNILVTWQPPRKDPSAVQEYVVEWRELHPGGDTQVPLNWLRSRPYNVSALISENIKSYICYEIRVYALSGDQGGCSSILGNSKHKAPLSGPHINAITEEKGSILISWNSIPVQEQMGCLLHYRIYWKERDSNSQPQLCEIPYRVSQNSHPINSLQPRVTYVLWMTALTAAGESSHGNEREFCLQGKANWMAFVAPSICIAIIMVGIFSTHYFQQKVFVLLAALRPQWCSREIPDPANSTCAKKYPIAEEKTQLPLDRLLIDWPTPEDPEPLVISEVLHQVTPVFRHPPCSNWPQREKGIQGHQASEKDMMHSASSPPPPRALQAESRQLVDLYKVLESRGSDPKPENPACPWTVLPAGDLPTHDGYLPSNIDDLPSHEAPLADSLEELEPQHISLSVFPSSSLHPLTFSCGDKLTLDQLKMRCDSLML
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
48N-linked_GlycosylationILLGSTVNITCSLKP
EEECCEEEEEEECCC
24.76UniProtKB CARBOHYD
129N-linked_GlycosylationVAPEQPQNLSCIQKG
ECCCCCCCEECEECC
40.37UniProtKB CARBOHYD
166N-linked_GlycosylationLQLSGPKNLTWQKQC
EEECCCCCCCHHHHC
45.92UniProtKB CARBOHYD
195N-linked_GlycosylationTPESPESNFTAKVTA
CCCCCCCCCEEEEEE
36.30UniProtKB CARBOHYD
271N-linked_GlycosylationSRLWNMVNVTKAKGR
CCHHHHHEEEECCCC
25.60UniProtKB CARBOHYD
347N-linked_GlycosylationQISLFWKNLSVSEAR
HHHHHEECCCHHHHH
28.30UniProtKB CARBOHYD
376N-linked_GlycosylationGGKAMTQNITGHTSW
CCCCEEEECCCCCCE
25.32UniProtKB CARBOHYD
390PhosphorylationWTTVIPRTGNWAVAV
EEEEECCCCCEEEEE
29.52-
406PhosphorylationAANSKGSSLPTRINI
EECCCCCCCCCCCCH
47.2224719451
480N-linked_GlycosylationWLRSRPYNVSALISE
HHHCCCCCHHHHHCC
24.77UniProtKB CARBOHYD
565PhosphorylationIYWKERDSNSQPQLC
EEECCCCCCCCCCEE
44.6022210691
607PhosphorylationALTAAGESSHGNERE
HHHHCCCCCCCCCCE
27.0722210691
630PhosphorylationWMAFVAPSICIAIIM
HHHHHHHHHHHHHHH
21.98-
749PhosphorylationDMMHSASSPPPPRAL
HHCCCCCCCCCCHHH
40.9420058876
767PhosphorylationSRQLVDLYKVLESRG
HHHHHHHHHHHHHCC
8.4528111955
768UbiquitinationRQLVDLYKVLESRGS
HHHHHHHHHHHHCCC
47.87-
772PhosphorylationDLYKVLESRGSDPKP
HHHHHHHHCCCCCCC
37.4728111955
800PhosphorylationDLPTHDGYLPSNIDD
CCCCCCCCCCCCCCC
22.849890938
859PhosphorylationQLKMRCDSLML----
HHHHHHHHHCC----
21.21-

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 I12R2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of I12R2_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 I12R2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JAK2_HUMANJAK2physical
10198225
SOCS3_HUMANSOCS3physical
14559241

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 I12R2_HUMAN

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Related Literatures of Post-Translational Modification

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