ADA33_HUMAN - dbPTM
ADA33_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADA33_HUMAN
UniProt AC Q9BZ11
Protein Name Disintegrin and metalloproteinase domain-containing protein 33
Gene Name ADAM33
Organism Homo sapiens (Human).
Sequence Length 813
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description
Protein Sequence MGWRPRRARGTPLLLLLLLLLLWPVPGAGVLQGHIPGQPVTPHWVLDGQPWRTVSLEEPVSKPDMGLVALEAEGQELLLELEKNHRLLAPGYIETHYGPDGQPVVLAPNHTDHCHYQGRVRGFPDSWVVLCTCSGMSGLITLSRNASYYLRPWPPRGSKDFSTHEIFRMEQLLTWKGTCGHRDPGNKAGMTSLPGGPQSRGRREARRTRKYLELYIVADHTLFLTRHRNLNHTKQRLLEVANYVDQLLRTLDIQVALTGLEVWTERDRSRVTQDANATLWAFLQWRRGLWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGCCVEAAAESGGCVMAAATGHPFPRVFSACSRRQLRAFFRKGGGACLSNAPDPGLPVPPALCGNGFVEAGEECDCGPGQECRDLCCFAHNCSLRPGAQCAHGDCCVRCLLKPAGALCRQAMGDCDLPEFCTGTSSHCPPDVYLLDGSPCARGSGYCWDGACPTLEQQCQQLWGPGSHPAPEACFQVVNSAGDAHGNCGQDSEGHFLPCAGRDALCGKLQCQGGKPSLLAPHMVPVDSTVHLDGQEVTCRGALALPSAQLDLLGLGLVEPGTQCGPRMVCQSRRCRKNAFQELQRCLTACHSHGVCNSNHNCHCAPGWAPPFCDKPGFGGSMDSGPVQAENHDTFLLAMLLSVLLPLLPGAGLAWCCYRLPGAHLQRCSWGCRRDPACSGPKDGPHRDHPLGGVHPMELGPTATGQPWPLDPENSHEPSSHPEKPLPAVSPDPQADQVQMPRSCLW
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
109N-linked_GlycosylationQPVVLAPNHTDHCHY
CEEEECCCCCCCCCC
45.12UniProtKB CARBOHYD
145N-linked_GlycosylationGLITLSRNASYYLRP
CEEEEECCCEEEECC
29.84UniProtKB CARBOHYD
187MethylationGHRDPGNKAGMTSLP
CCCCCCCCCCCCCCC
52.83-
192PhosphorylationGNKAGMTSLPGGPQS
CCCCCCCCCCCCCCC
24.5528509920
231N-linked_GlycosylationLTRHRNLNHTKQRLL
HHHCCCCCHHHHHHH
44.31UniProtKB CARBOHYD
243PhosphorylationRLLEVANYVDQLLRT
HHHHHHHHHHHHHHH
8.8222817900
269PhosphorylationVWTERDRSRVTQDAN
EECHHHHHHHCCHHH
35.0817081983
276N-linked_GlycosylationSRVTQDANATLWAFL
HHHCCHHHHHHHHHH
41.57UniProtKB CARBOHYD
448N-linked_GlycosylationDLCCFAHNCSLRPGA
HHHHHCCCCCCCCCC
17.40UniProtKB CARBOHYD
489PhosphorylationCDLPEFCTGTSSHCP
CCCCHHHCCCCCCCC
49.1468707401
746PhosphorylationCRRDPACSGPKDGPH
CCCCCCCCCCCCCCC
61.3050563475

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 ADA33_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADA33_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 ADA33_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASB7_HUMANASB7physical
28514442
ZDHC6_HUMANZDHHC6physical
28514442
HMOX1_HUMANHMOX1physical
28514442
SOAT1_HUMANSOAT1physical
28514442
TM39B_HUMANTMEM39Bphysical
28514442
DYR2_HUMANDHFRL1physical
28514442
S27A3_HUMANSLC27A3physical
28514442
NOTC3_HUMANNOTCH3physical
28514442
MKS3_HUMANTMEM67physical
28514442
EGFL7_HUMANEGFL7physical
28514442
1A02_HUMANHLA-Aphysical
28514442
1A03_HUMANHLA-Aphysical
28514442
1A01_HUMANHLA-Aphysical
28514442
1A26_HUMANHLA-Aphysical
28514442
TTC17_HUMANTTC17physical
28514442
ITB5_HUMANITGB5physical
28514442
LRP12_HUMANLRP12physical
28514442
FBX2_HUMANFBXO2physical
28514442
1C07_HUMANHLA-Cphysical
28514442
BI1_HUMANTMBIM6physical
28514442
MANEL_HUMANMANEALphysical
28514442
TOR3A_HUMANTOR3Aphysical
28514442
IDD_HUMANDGCR2physical
28514442
LSR_HUMANLSRphysical
28514442
FSTL1_HUMANFSTL1physical
28514442
SDF2L_HUMANSDF2L1physical
28514442
CISD3_HUMANCISD3physical
28514442
LRP6_HUMANLRP6physical
28514442
GLT12_HUMANGALNT12physical
28514442
AMGO1_HUMANAMIGO1physical
28514442
LRP5_HUMANLRP5physical
28514442
CSTN1_HUMANCLSTN1physical
28514442
TYW1_HUMANTYW1physical
28514442
KCNJ8_HUMANKCNJ8physical
28514442
ANR46_HUMANANKRD46physical
28514442
SEM4F_HUMANSEMA4Fphysical
28514442
ADA15_HUMANADAM15physical
28514442
DEFM_HUMANPDFphysical
28514442
NETO2_HUMANNETO2physical
28514442

Drug and Disease Associations
Kegg Disease
H00079 Asthma
OMIM Disease
600807Asthma (ASTHMA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADA33_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND MASSSPECTROMETRY.

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