TPSN_HUMAN - dbPTM
TPSN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPSN_HUMAN
UniProt AC O15533
Protein Name Tapasin
Gene Name TAPBP
Organism Homo sapiens (Human).
Sequence Length 448
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein .
Protein Description Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading)..
Protein Sequence MKSLSLLLAVALGLATAVSAGPAVIECWFVEDASGKGLAKRPGALLLRQGPGEPPPRPDLDPELYLSVHDPAGALQAAFRRYPRGAPAPHCEMSRFVPLPASAKWASGLTPAQNCPRALDGAWLMVSISSPVLSLSSLLRPQPEPQQEPVLITMATVVLTVLTHTPAPRVRLGQDALLDLSFAYMPPTSEAASSLAPGPPPFGLEWRRQHLGKGHLLLAATPGLNGQMPAAQEGAVAFAAWDDDEPWGPWTGNGTFWLPRVQPFQEGTYLATIHLPYLQGQVTLELAVYKPPKVSLMPATLARAAPGEAPPELLCLVSHFYPSGGLEVEWELRGGPGGRSQKAEGQRWLSALRHHSDGSVSLSGHLQPPPVTTEQHGARYACRIHHPSLPASGRSAEVTLEVAGLSGPSLEDSVGLFLSAFLLLGLFKALGWAAVYLSTCKDSKKKAE
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
3Phosphorylation-----MKSLSLLLAV
-----CCHHHHHHHH
23.1518187866
5Phosphorylation---MKSLSLLLAVAL
---CCHHHHHHHHHH
24.8618187866
40UbiquitinationASGKGLAKRPGALLL
CCCCCCCCCCCEEEE
65.2621890473
40 (in isoform 2)Ubiquitination-65.2621890473
40 (in isoform 1)Ubiquitination-65.2621890473
40UbiquitinationASGKGLAKRPGALLL
CCCCCCCCCCCEEEE
65.2621890473
40 (in isoform 3)Ubiquitination-65.2621890473
102PhosphorylationRFVPLPASAKWASGL
CCCCCCCCCHHHCCC
28.57-
104 (in isoform 2)Ubiquitination-40.5721890473
104 (in isoform 1)Ubiquitination-40.5721890473
104 (in isoform 3)Ubiquitination-40.5721890473
104UbiquitinationVPLPASAKWASGLTP
CCCCCCCHHHCCCCC
40.572189047
136PhosphorylationSSPVLSLSSLLRPQP
CCCCCCHHHHCCCCC
18.6324945436
137PhosphorylationSPVLSLSSLLRPQPE
CCCCCHHHHCCCCCC
36.3924719451
181PhosphorylationQDALLDLSFAYMPPT
CCEEEECCEEECCCC
13.9026074081
184PhosphorylationLLDLSFAYMPPTSEA
EEECCEEECCCCHHH
14.2426074081
188PhosphorylationSFAYMPPTSEAASSL
CEEECCCCHHHHHHC
33.0726074081
189PhosphorylationFAYMPPTSEAASSLA
EEECCCCHHHHHHCC
30.8926074081
193PhosphorylationPPTSEAASSLAPGPP
CCCHHHHHHCCCCCC
32.6926074081
194PhosphorylationPTSEAASSLAPGPPP
CCHHHHHHCCCCCCC
24.6726074081
253N-linked_GlycosylationPWGPWTGNGTFWLPR
CCCCCCCCCCEEECC
38.6719119025
253N-linked_GlycosylationPWGPWTGNGTFWLPR
CCCCCCCCCCEEECC
38.679271576
295PhosphorylationVYKPPKVSLMPATLA
EECCCCCCCCCHHHH
25.6920068231
300PhosphorylationKVSLMPATLARAAPG
CCCCCCHHHHHHCCC
18.3220068231
356PhosphorylationLSALRHHSDGSVSLS
HHHHHHCCCCCEEEC
37.2327080861
359PhosphorylationLRHHSDGSVSLSGHL
HHHCCCCCEEECCCC
17.3327080861
361PhosphorylationHHSDGSVSLSGHLQP
HCCCCCEEECCCCCC
20.6527080861
363PhosphorylationSDGSVSLSGHLQPPP
CCCCEEECCCCCCCC
19.3627080861
388 (in isoform 2)Phosphorylation-42.5022210691
436PhosphorylationALGWAAVYLSTCKDS
HHHHHHHHHHHCCCH
7.1029083192
438PhosphorylationGWAAVYLSTCKDSKK
HHHHHHHHHCCCHHH
17.6729083192
439PhosphorylationWAAVYLSTCKDSKKK
HHHHHHHHCCCHHHH
22.4529083192
441AcetylationAVYLSTCKDSKKKAE
HHHHHHCCCHHHHCC
66.1916916647
445AcetylationSTCKDSKKKAE----
HHCCCHHHHCC----
62.2616916647

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 TPSN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPSN_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 TPSN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAP1_HUMANTAP1physical
12213826
TAP2_HUMANTAP2physical
12213826
COPB_HUMANCOPB1physical
11884415
COPG1_HUMANCOPG1physical
11884415
TAP1_HUMANTAP1physical
11884415
1A02_HUMANHLA-Aphysical
11884415
1A03_HUMANHLA-Aphysical
11884415
1A01_HUMANHLA-Aphysical
11884415
1A26_HUMANHLA-Aphysical
11884415

Drug and Disease Associations
Kegg Disease
H00984 Bare lymphocyte syndrome (BLS) type1
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPSN_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Insights into MHC class I peptide loading from the structure of thetapasin-ERp57 thiol oxidoreductase heterodimer.";
Dong G., Wearsch P.A., Peaper D.R., Cresswell P., Reinisch K.M.;
Immunity 30:21-32(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-401 IN COMPLEX WITH PDIA3,SUBUNIT, INTERACTION WITH PDIA3, GLYCOSYLATION AT ASN-253, ANDDISULFIDE BONDS.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-5, AND MASSSPECTROMETRY.

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