TAP2_HUMAN - dbPTM
TAP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAP2_HUMAN
UniProt AC Q03519
Protein Name Antigen peptide transporter 2
Gene Name TAP2
Organism Homo sapiens (Human).
Sequence Length 686
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein. The transmembrane segments seem to form a pore in the membrane.
Protein Description Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association..
Protein Sequence MRLPDLRPWTSLLLVDAALLWLLQGPLGTLLPQGLPGLWLEGTLRLGGLWGLLKLRGLLGFVGTLLLPLCLATPLTVSLRALVAGASRAPPARVASAPWSWLLVGYGAAGLSWSLWAVLSPPGAQEKEQDQVNNKVLMWRLLKLSRPDLPLLVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDRQPNLPSPGTLAPTTLQGVVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQALQDWNSRGDRTVLVIAHRLQTVQRAHQILVLQEGKLQKLAQL
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
54UbiquitinationGGLWGLLKLRGLLGF
CHHHHHHHHHHHHHH
40.9821906983
135UbiquitinationEQDQVNNKVLMWRLL
HHHHHHHHHHHHHHH
31.3821890473
135UbiquitinationEQDQVNNKVLMWRLL
HHHHHHHHHHHHHHH
31.3821890473
135UbiquitinationEQDQVNNKVLMWRLL
HHHHHHHHHHHHHHH
31.3821890473
135UbiquitinationEQDQVNNKVLMWRLL
HHHHHHHHHHHHHHH
31.3821890473
135UbiquitinationEQDQVNNKVLMWRLL
HHHHHHHHHHHHHHH
31.3821890473
216PhosphorylationCRGGCFTYTMSRINL
CCCCCCHHHHHHHHH
4.7224719451
217PhosphorylationRGGCFTYTMSRINLR
CCCCCHHHHHHHHHH
12.9524719451
219PhosphorylationGCFTYTMSRINLRIR
CCCHHHHHHHHHHHH
23.3924719451
232PhosphorylationIREQLFSSLLRQDLG
HHHHHHHHHHHHHCC
24.8824719451
245UbiquitinationLGFFQETKTGELNSR
CCCCCCCCCCCCCCC
54.5021890473
245UbiquitinationLGFFQETKTGELNSR
CCCCCCCCCCCCCCC
54.5021890473
245UbiquitinationLGFFQETKTGELNSR
CCCCCCCCCCCCCCC
54.5021890473
245 (in isoform 2)Ubiquitination-54.50-
245UbiquitinationLGFFQETKTGELNSR
CCCCCCCCCCCCCCC
54.5021890473
245UbiquitinationLGFFQETKTGELNSR
CCCCCCCCCCCCCCC
54.5021906983
282PhosphorylationLVKVVGLYGFMLSIS
HHHHHHHHHHHHCCC
11.4622210691
287PhosphorylationGLYGFMLSISPRLTL
HHHHHHHCCCHHHHH
14.8326074081
289PhosphorylationYGFMLSISPRLTLLS
HHHHHCCCHHHHHHH
10.6926074081
293PhosphorylationLSISPRLTLLSLLHM
HCCCHHHHHHHHHCC
27.2526074081
296PhosphorylationSPRLTLLSLLHMPFT
CHHHHHHHHHCCCHH
31.8126074081
308UbiquitinationPFTIAAEKVYNTRHQ
CHHHHHHHHHCHHHH
45.34-
356UbiquitinationEHEVCRYKEALEQCR
HHHHHHHHHHHHHHH
19.7021890473
3562-HydroxyisobutyrylationEHEVCRYKEALEQCR
HHHHHHHHHHHHHHH
19.70-
455PhosphorylationDRQPNLPSPGTLAPT
CCCCCCCCCCCCCCC
38.8426657352
458PhosphorylationPNLPSPGTLAPTTLQ
CCCCCCCCCCCCEEE
24.1126657352
469UbiquitinationTTLQGVVKFQDVSFA
CEEECEEEEEEEEEE
34.60-
492PhosphorylationVLKGLTFTLRPGEVT
EEEECEEEECCCEEE
19.3424719451
597PhosphorylationQEMEHGIYTDVGEKG
HHHHCCCCCCCCHHH
11.0728796482
598PhosphorylationEMEHGIYTDVGEKGS
HHHCCCCCCCCHHHC
23.4528796482
603 (in isoform 2)Ubiquitination-58.91-
603UbiquitinationIYTDVGEKGSQLAAG
CCCCCCHHHCCCCHH
58.9121906983
6122-HydroxyisobutyrylationSQLAAGQKQRLAIAR
CCCCHHHHHHHHHHH
36.15-
612 (in isoform 2)Ubiquitination-36.15-
612UbiquitinationSQLAAGQKQRLAIAR
CCCCHHHHHHHHHHH
36.1521906983
679UbiquitinationILVLQEGKLQKLAQL
HHHCCCCHHHHHHCC
47.1721890473
682UbiquitinationLQEGKLQKLAQL---
CCCCHHHHHHCC---
57.1121890473
682UbiquitinationLQEGKLQKLAQL---
CCCCHHHHHHCC---
57.1121890473
682UbiquitinationLQEGKLQKLAQL---
CCCCHHHHHHCC---
57.1121890473
682UbiquitinationLQEGKLQKLAQL---
CCCCHHHHHHCC---
57.11-
693PhosphorylationL--------------
C--------------
-

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 TAP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAP2_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 TAP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HLAG_HUMANHLA-Gphysical
9103419
1C07_HUMANHLA-Cphysical
9551969
A4_HUMANAPPphysical
21832049
B2MG_HUMANB2Mphysical
8805302
1A02_HUMANHLA-Aphysical
8805302
1A03_HUMANHLA-Aphysical
8805302
1A01_HUMANHLA-Aphysical
8805302
1A26_HUMANHLA-Aphysical
8805302
HLAE_HUMANHLA-Ephysical
9427624
TAP1_HUMANTAP1physical
28514442

Drug and Disease Associations
Kegg Disease
H00093 Combined immunodeficiencies (CIDs), including the following nine diseases: X-linked hyper IgM syndro
H00984 Bare lymphocyte syndrome (BLS) type1
OMIM Disease
604571Bare lymphocyte syndrome 1 (BLS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TAP2_HUMAN

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Related Literatures of Post-Translational Modification

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