I12R1_HUMAN - dbPTM
I12R1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID I12R1_HUMAN
UniProt AC P42701
Protein Name Interleukin-12 receptor subunit beta-1
Gene Name IL12RB1
Organism Homo sapiens (Human).
Sequence Length 662
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Functions as an interleukin receptor which binds interleukin-12 with low affinity and is involved in IL12 transduction. Associated with IL12RB2 it forms a functional, high affinity receptor for IL12. Associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction probably through activation of the Jak-Stat signaling cascade..
Protein Sequence MEPLVTWVVPLLFLFLLSRQGAACRTSECCFQDPPYPDADSGSASGPRDLRCYRISSDRYECSWQYEGPTAGVSHFLRCCLSSGRCCYFAAGSATRLQFSDQAGVSVLYTVTLWVESWARNQTEKSPEVTLQLYNSVKYEPPLGDIKVSKLAGQLRMEWETPDNQVGAEVQFRHRTPSSPWKLGDCGPQDDDTESCLCPLEMNVAQEFQLRRRQLGSQGSSWSKWSSPVCVPPENPPQPQVRFSVEQLGQDGRRRLTLKEQPTQLELPEGCQGLAPGTEVTYRLQLHMLSCPCKAKATRTLHLGKMPYLSGAAYNVAVISSNQFGPGLNQTWHIPADTHTEPVALNISVGTNGTTMYWPARAQSMTYCIEWQPVGQDGGLATCSLTAPQDPDPAGMATYSWSRESGAMGQEKCYYITIFASAHPEKLTLWSTVLSTYHFGGNASAAGTPHHVSVKNHSLDSVSVDWAPSLLSTCPGVLKEYVVRCRDEDSKQVSEHPVQPTETQVTLSGLRAGVAYTVQVRADTAWLRGVWSQPQRFSIEVQVSDWLIFFASLGSFLSILLVGVLGYLGLNRAARHLCPPLPTPCASSAIEFPGGKETWQWINPVDFQEEASLQEALVVEMSWDKGERTEPLEKTELPEGAPELALDTELSLEDGDRCKAKM
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
121N-linked_GlycosylationWVESWARNQTEKSPE
HHHHHHCCCCCCCCC
45.43UniProtKB CARBOHYD
244PhosphorylationPQPQVRFSVEQLGQD
CCCCEEEEHHHCCCC
17.74-
300PhosphorylationCKAKATRTLHLGKMP
CCCEEEEEEECCCCC
17.74-
329N-linked_GlycosylationNQFGPGLNQTWHIPA
CCCCCCCCEEEECCC
43.05UniProtKB CARBOHYD
346N-linked_GlycosylationHTEPVALNISVGTNG
CCCCEEEEEEECCCC
18.10UniProtKB CARBOHYD
352N-linked_GlycosylationLNISVGTNGTTMYWP
EEEEECCCCCEEEEE
39.63UniProtKB CARBOHYD
375 (in isoform 3)Phosphorylation-26.92-
442N-linked_GlycosylationSTYHFGGNASAAGTP
EEEECCCCCCCCCCC
30.97UniProtKB CARBOHYD
456N-linked_GlycosylationPHHVSVKNHSLDSVS
CCEEEECCCCCCEEC
28.02UniProtKB CARBOHYD
508PhosphorylationTETQVTLSGLRAGVA
CCEEEEECCCCCCEE
26.8124719451

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 I12R1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of I12R1_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 I12R1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IL23R_HUMANIL23Rphysical
12023369
I12R2_HUMANIL12RB2genetic
8943050
SMD3_HUMANSNRPD3physical
21988832
TBB4A_HUMANTUBB4Aphysical
26186194
TBB3_HUMANTUBB3physical
26186194
TBB8_HUMANTUBB8physical
26186194
GRP78_HUMANHSPA5physical
26186194
TBA4A_HUMANTUBA4Aphysical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
CBWD1_HUMANCBWD1physical
26186194
TXNIP_HUMANTXNIPphysical
26186194
LOXL2_HUMANLOXL2physical
26186194
ISOC2_HUMANISOC2physical
26186194
RA51C_HUMANRAD51Cphysical
26186194
CREL2_HUMANCRELD2physical
26186194
TRM44_HUMANTRMT44physical
26186194
TXNIP_HUMANTXNIPphysical
28514442
ISOC2_HUMANISOC2physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
TBB3_HUMANTUBB3physical
28514442
LOXL2_HUMANLOXL2physical
28514442
CBWD1_HUMANCBWD1physical
28514442
NPTX1_HUMANNPTX1physical
28514442
GRP78_HUMANHSPA5physical
28514442
TBB8_HUMANTUBB8physical
28514442
TRM44_HUMANTRMT44physical
28514442
TBB4A_HUMANTUBB4Aphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of I12R1_HUMAN

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Related Literatures of Post-Translational Modification

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