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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Phosphorylation | -----MKSLSLLLAV -----CCHHHHHHHH | 23.15 | 18187866 | |
5 | Phosphorylation | ---MKSLSLLLAVAL ---CCHHHHHHHHHH | 24.86 | 18187866 | |
40 | Ubiquitination | ASGKGLAKRPGALLL CCCCCCCCCCCEEEE | 65.26 | 21890473 | |
40 (in isoform 2) | Ubiquitination | - | 65.26 | 21890473 | |
40 (in isoform 1) | Ubiquitination | - | 65.26 | 21890473 | |
40 | Ubiquitination | ASGKGLAKRPGALLL CCCCCCCCCCCEEEE | 65.26 | 21890473 | |
40 (in isoform 3) | Ubiquitination | - | 65.26 | 21890473 | |
102 | Phosphorylation | RFVPLPASAKWASGL CCCCCCCCCHHHCCC | 28.57 | - | |
104 (in isoform 2) | Ubiquitination | - | 40.57 | 21890473 | |
104 (in isoform 1) | Ubiquitination | - | 40.57 | 21890473 | |
104 (in isoform 3) | Ubiquitination | - | 40.57 | 21890473 | |
104 | Ubiquitination | VPLPASAKWASGLTP CCCCCCCHHHCCCCC | 40.57 | 2189047 | |
136 | Phosphorylation | SSPVLSLSSLLRPQP CCCCCCHHHHCCCCC | 18.63 | 24945436 | |
137 | Phosphorylation | SPVLSLSSLLRPQPE CCCCCHHHHCCCCCC | 36.39 | 24719451 | |
181 | Phosphorylation | QDALLDLSFAYMPPT CCEEEECCEEECCCC | 13.90 | 26074081 | |
184 | Phosphorylation | LLDLSFAYMPPTSEA EEECCEEECCCCHHH | 14.24 | 26074081 | |
188 | Phosphorylation | SFAYMPPTSEAASSL CEEECCCCHHHHHHC | 33.07 | 26074081 | |
189 | Phosphorylation | FAYMPPTSEAASSLA EEECCCCHHHHHHCC | 30.89 | 26074081 | |
193 | Phosphorylation | PPTSEAASSLAPGPP CCCHHHHHHCCCCCC | 32.69 | 26074081 | |
194 | Phosphorylation | PTSEAASSLAPGPPP CCHHHHHHCCCCCCC | 24.67 | 26074081 | |
253 | N-linked_Glycosylation | PWGPWTGNGTFWLPR CCCCCCCCCCEEECC | 38.67 | 19119025 | |
253 | N-linked_Glycosylation | PWGPWTGNGTFWLPR CCCCCCCCCCEEECC | 38.67 | 9271576 | |
295 | Phosphorylation | VYKPPKVSLMPATLA EECCCCCCCCCHHHH | 25.69 | 20068231 | |
300 | Phosphorylation | KVSLMPATLARAAPG CCCCCCHHHHHHCCC | 18.32 | 20068231 | |
356 | Phosphorylation | LSALRHHSDGSVSLS HHHHHHCCCCCEEEC | 37.23 | 27080861 | |
359 | Phosphorylation | LRHHSDGSVSLSGHL HHHCCCCCEEECCCC | 17.33 | 27080861 | |
361 | Phosphorylation | HHSDGSVSLSGHLQP HCCCCCEEECCCCCC | 20.65 | 27080861 | |
363 | Phosphorylation | SDGSVSLSGHLQPPP CCCCEEECCCCCCCC | 19.36 | 27080861 | |
388 (in isoform 2) | Phosphorylation | - | 42.50 | 22210691 | |
436 | Phosphorylation | ALGWAAVYLSTCKDS HHHHHHHHHHHCCCH | 7.10 | 29083192 | |
438 | Phosphorylation | GWAAVYLSTCKDSKK HHHHHHHHHCCCHHH | 17.67 | 29083192 | |
439 | Phosphorylation | WAAVYLSTCKDSKKK HHHHHHHHCCCHHHH | 22.45 | 29083192 | |
441 | Acetylation | AVYLSTCKDSKKKAE HHHHHHCCCHHHHCC | 66.19 | 16916647 | |
445 | Acetylation | STCKDSKKKAE---- HHCCCHHHHCC---- | 62.26 | 16916647 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TPSN_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TAP1_HUMAN | TAP1 | physical | 12213826 | |
TAP2_HUMAN | TAP2 | physical | 12213826 | |
COPB_HUMAN | COPB1 | physical | 11884415 | |
COPG1_HUMAN | COPG1 | physical | 11884415 | |
TAP1_HUMAN | TAP1 | physical | 11884415 | |
1A02_HUMAN | HLA-A | physical | 11884415 | |
1A03_HUMAN | HLA-A | physical | 11884415 | |
1A01_HUMAN | HLA-A | physical | 11884415 | |
1A26_HUMAN | HLA-A | physical | 11884415 |
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. |
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N-linked Glycosylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |