ITM2B_HUMAN - dbPTM
ITM2B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITM2B_HUMAN
UniProt AC Q9Y287
Protein Name Integral membrane protein 2B
Gene Name ITM2B
Organism Homo sapiens (Human).
Sequence Length 266
Subcellular Localization Integral membrane protein 2B: Golgi apparatus membrane
Single-pass type II membrane protein . Immature BRI2 (imBRI2) is cleaved by furin in the Golgi into mBRI2 and a Bri23 peptide. mBRI2 is transported to the plasma membrane and Bri23 peptide is s
Protein Description Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites.; Mature BRI2 (mBRI2) functions as a modulator of the amyloid-beta A4 precursor protein (APP) processing leading to a strong reduction in the secretion of secretase-processed amyloid-beta protein 40 and amyloid-beta protein 42.; Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers..
Protein Sequence MVKVTFNSALAQKEAKKDEPKSGEEALIIPPDAVAVDCKDPDDVVPVGQRRAWCWCMCFGLAFMLAGVILGGAYLYKYFALQPDDVYYCGIKYIKDDVILNEPSADAPAALYQTIEENIKIFEEEEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKLQRRETIKGIQKREASNCFAIRHFENKFAVETLICS
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
3Ubiquitination-----MVKVTFNSAL
-----CCEEEECHHH		33.97-
3Ubiquitination-----MVKVTFNSAL
-----CCEEEECHHH		33.97-
5Phosphorylation---MVKVTFNSALAQ
---CCEEEECHHHHH		16.0427050516
8PhosphorylationMVKVTFNSALAQKEA
CCEEEECHHHHHHHH		22.0725159151
13UbiquitinationFNSALAQKEAKKDEP
ECHHHHHHHHCCCCC		54.7721890473
13UbiquitinationFNSALAQKEAKKDEP
ECHHHHHHHHCCCCC		54.7721890473
13UbiquitinationFNSALAQKEAKKDEP
ECHHHHHHHHCCCCC		54.7721906983
16UbiquitinationALAQKEAKKDEPKSG
HHHHHHHCCCCCCCC		62.9521906983
17UbiquitinationLAQKEAKKDEPKSGE
HHHHHHCCCCCCCCC		74.5021906983
21UbiquitinationEAKKDEPKSGEEALI
HHCCCCCCCCCCCEE		69.88-
38S-palmitoylationPDAVAVDCKDPDDVV
CCCEEECCCCHHHCC		4.2929575903
39UbiquitinationDAVAVDCKDPDDVVP
CCEEECCCCHHHCCC		68.7621906983
76PhosphorylationILGGAYLYKYFALQP
HHHHHHHHHHHCCCC		7.32-
78 (in isoform 2)Phosphorylation-4.7820068231
85 (in isoform 2)Phosphorylation-36.6820068231
86 (in isoform 2)Phosphorylation-4.8420068231
90 (in isoform 2)Phosphorylation-11.8720068231
91 (in isoform 2)Phosphorylation-2.4620068231
100 (in isoform 2)Phosphorylation-6.2820068231
104O-linked_GlycosylationDVILNEPSADAPAAL
CEECCCCCCCCCHHH		32.38OGP
114 (in isoform 2)Phosphorylation-19.4620068231
114O-linked_GlycosylationAPAALYQTIEENIKI
CCHHHHHHHHHHHCC		19.46OGP
165PhosphorylationDLNLDKCYVIPLNTS
ECCCCCEEEEECCCC		13.73-
170N-linked_GlycosylationKCYVIPLNTSIVMPP
CEEEEECCCCEECCC		26.8221752865
191PhosphorylationLINIKAGTYLPQSYL
HHHCCCCCCCCHHHE		27.0922210691
192PhosphorylationINIKAGTYLPQSYLI
HHCCCCCCCCHHHEE		18.5722210691
206PhosphorylationIHEHMVITDRIENID
ECEEEEECCCCCCCC		14.0722210691
228PhosphorylationRLCHDKETYKLQRRE
HHHCCHHHHHHHHHH		31.5323532336
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 ITM2B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
170NGlycosylation

21752865
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 ITM2B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCL2_HUMANBCL2physical
12082633
KASH5_HUMANCCDC155physical
25416956
SYNE4_HUMANSYNE4physical
25416956
NADL2_HUMANNAALADL2physical
25416956
1A02_HUMANHLA-Aphysical
26186194
1A03_HUMANHLA-Aphysical
26186194
1A01_HUMANHLA-Aphysical
26186194
1A26_HUMANHLA-Aphysical
26186194
UBR1_HUMANUBR1physical
26186194
DCBD2_HUMANDCBLD2physical
26186194
HMR1_HUMANMR1physical
26186194
BT2A2_HUMANBTN2A2physical
26186194
SEM4F_HUMANSEMA4Fphysical
26186194
ATF6B_HUMANATF6Bphysical
26186194
CHSTC_HUMANCHST12physical
26186194
TM59L_HUMANTMEM59Lphysical
26186194
TM219_HUMANTMEM219physical
26186194
H6ST1_HUMANHS6ST1physical
26186194
PGAP1_HUMANPGAP1physical
26186194
GSLG1_HUMANGLG1physical
26186194
SEM6A_HUMANSEMA6Aphysical
26186194
CA2D1_HUMANCACNA2D1physical
26186194
B4GN1_HUMANB4GALNT1physical
26186194
TGBR3_HUMANTGFBR3physical
26186194
LRFN3_HUMANLRFN3physical
26186194
F234B_HUMANKIAA1467physical
26186194
AMGO1_HUMANAMIGO1physical
26186194
SEM6A_HUMANSEMA6Aphysical
28514442
TM219_HUMANTMEM219physical
28514442
DCBD2_HUMANDCBLD2physical
28514442
TM59L_HUMANTMEM59Lphysical
28514442
BT2A2_HUMANBTN2A2physical
28514442
TGBR3_HUMANTGFBR3physical
28514442
AMGO1_HUMANAMIGO1physical
28514442
UBR1_HUMANUBR1physical
28514442
CHSTC_HUMANCHST12physical
28514442
B4GN1_HUMANB4GALNT1physical
28514442
SEM4F_HUMANSEMA4Fphysical
28514442
Drug and Disease Associations
Kegg Disease
H01184 Familial dementia, including: Familial British dementia (FBD); Familial Danish dementia (FDD)
OMIM Disease
176500Cerebral amyloid angiopathy, ITM2B-related 1 (CAA-ITM2B1)
117300Cerebral amyloid angiopathy, ITM2B-related 2 (CAA-ITM2B2)
616079Retinal dystrophy with inner retinal dysfunction and ganglion cell abnormalities (RDGCA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITM2B_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycosylation of BRI2 on asparagine 170 is involved in itstrafficking to the cell surface but not in its processing by furin orADAM10.";
Tsachaki M., Serlidaki D., Fetani A., Zarkou V., Rozani I., Ghiso J.,Efthimiopoulos S.;
Glycobiology 21:1382-1388(2011).
Cited for: CLEAVAGE BY ADAM10; FURIN AND SPPL2B, GLYCOSYLATION AT ASN-170,SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-170.

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