TAP1_HUMAN - dbPTM
TAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAP1_HUMAN
UniProt AC Q03518
Protein Name Antigen peptide transporter 1
Gene Name TAP1
Organism Homo sapiens (Human).
Sequence Length 808
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. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-10 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules..
Protein Sequence MAELLASAGSACSWDFPRAPPSFPPPAASRGGLGGTRSFRPHRGAESPRPGRDRDGVRVPMASSRCPAPRGCRCLPGASLAWLGTVLLLLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGSKSENAGAQGWLAALKPLAAALGLALPGLALFRELISWGAPGSADSTRLLHWGSHPTAFVVSYAAALPAAALWHKLGSLWVPGGQGGSGNPVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQAPADAPE
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
30MethylationFPPPAASRGGLGGTR
CCCCCHHCCCCCCCC
38.1754559851
37MethylationRGGLGGTRSFRPHRG
CCCCCCCCCCCCCCC
36.7554559855
47PhosphorylationRPHRGAESPRPGRDR
CCCCCCCCCCCCCCC
26.1920860994
63O-linked_GlycosylationGVRVPMASSRCPAPR
CCCCCCCCCCCCCCC
16.4430379171
63PhosphorylationGVRVPMASSRCPAPR
CCCCCCCCCCCCCCC
16.4428102081
64PhosphorylationVRVPMASSRCPAPRG
CCCCCCCCCCCCCCC
28.5028102081
229PhosphorylationVPGGQGGSGNPVRRL
CCCCCCCCCCHHHHH
42.0722210691
422UbiquitinationQVRESLAKSSQVAIE
HHHHHHHHHCHHHHH
56.80-
423PhosphorylationVRESLAKSSQVAIEA
HHHHHHHHCHHHHHH
22.0128857561
424PhosphorylationRESLAKSSQVAIEAL
HHHHHHHCHHHHHHH
28.1530108239
434SulfoxidationAIEALSAMPTVRSFA
HHHHHHCCHHHHHHC
2.2821406390
436PhosphorylationEALSAMPTVRSFANE
HHHHCCHHHHHHCCC
18.5724719451
439PhosphorylationSAMPTVRSFANEEGE
HCCHHHHHHCCCCHH
25.1130108239
4492-HydroxyisobutyrylationNEEGEAQKFREKLQE
CCCHHHHHHHHHHHH
54.13-
449UbiquitinationNEEGEAQKFREKLQE
CCCHHHHHHHHHHHH
54.1321890473
453UbiquitinationEAQKFREKLQEIKTL
HHHHHHHHHHHHHCC
51.74-
458UbiquitinationREKLQEIKTLNQKEA
HHHHHHHHCCCHHHH
46.3221890473
4582-HydroxyisobutyrylationREKLQEIKTLNQKEA
HHHHHHHHCCCHHHH
46.32-
5302-HydroxyisobutyrylationSIYPRVQKAVGSSEK
HHHHHHHHHHCCHHH
42.03-
537UbiquitinationKAVGSSEKIFEYLDR
HHHCCHHHHHHHHHC
55.4321890473
541PhosphorylationSSEKIFEYLDRTPRC
CHHHHHHHHHCCCCC
11.8023403867
545PhosphorylationIFEYLDRTPRCPPSG
HHHHHHCCCCCCCCC
18.1022617229
587PhosphorylationVLQGLTFTLRPGEVT
EEECEEEEECCCEEE
19.3424719451
627UbiquitinationGQLLLDGKPLPQYEH
CEEEECCEECCCCCH
42.94-
666UbiquitinationIAYGLTQKPTMEEIT
HHCCCCCCCCHHHHH
36.9021890473
668PhosphorylationYGLTQKPTMEEITAA
CCCCCCCCHHHHHHH
44.2228348404
679PhosphorylationITAAAVKSGAHSFIS
HHHHHHHCCCCHHHC
34.3127080861
683PhosphorylationAVKSGAHSFISGLPQ
HHHCCCCHHHCCCCC
24.6027080861
694PhosphorylationGLPQGYDTEVDEAGS
CCCCCCCCCCCHHHH
29.44-

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 TAP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAP1_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 TAP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR412_HUMANKRTAP4-12physical
16189514
HLAG_HUMANHLA-Gphysical
9103419
PDIA3_HUMANPDIA3physical
9545232
TAP2_HUMANTAP2physical
11381133
COPB_HUMANCOPB1physical
11884415
COPG1_HUMANCOPG1physical
11884415
TPSN_HUMANTAPBPphysical
11884415
1A02_HUMANHLA-Aphysical
11884415
1A03_HUMANHLA-Aphysical
11884415
1A01_HUMANHLA-Aphysical
11884415
1A26_HUMANHLA-Aphysical
11884415
TAP2_HUMANTAP2physical
17055437
CALR_HUMANCALRphysical
17055437
PDIA3_HUMANPDIA3physical
17055437
PDIA2_HUMANPDIA2physical
17055437
TPSN_HUMANTAPBPphysical
17055437
B2MG_HUMANB2Mphysical
17055437
1A02_HUMANHLA-Aphysical
17055437
1A03_HUMANHLA-Aphysical
17055437
1A01_HUMANHLA-Aphysical
17055437
1A26_HUMANHLA-Aphysical
17055437
PSB8_HUMANPSMB8physical
15488952
TYDP2_HUMANTDP2physical
21988832
CALR_HUMANCALRphysical
11823531
PDIA3_HUMANPDIA3physical
11823531
1B07_HUMANHLA-Bphysical
11823531
1B18_HUMANHLA-Bphysical
11823531
TPSN_HUMANTAPBPphysical
11823531
CALX_HUMANCANXphysical
11823531

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
DB01259Lapatinib
Regulatory Network of TAP1_HUMAN

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Related Literatures of Post-Translational Modification

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