| UniProt ID | ACRBP_HUMAN | |
|---|---|---|
| UniProt AC | Q8NEB7 | |
| Protein Name | Acrosin-binding protein | |
| Gene Name | ACRBP {ECO:0000312|EMBL:AAH33010.1} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 543 | |
| Subcellular Localization | Secreted . Cytoplasmic vesicle, secretory vesicle, acrosome . | |
| Protein Description | May be involved in packaging and condensation of the acrosin zymogen in the acrosomal matrix via its association with proacrosin.. | |
| Protein Sequence | MRKPAAGFLPSLLKVLLLPLAPAAAQDSTQASTPGSPLSPTEYERFFALLTPTWKAETTCRLRATHGCRNPTLVQLDQYENHGLVPDGAVCSNLPYASWFESFCQFTHYRCSNHVYYAKRVLCSQPVSILSPNTLKEIEASAEVSPTTMTSPISPHFTVTERQTFQPWPERLSNNVEELLQSSLSLGGQEQAPEHKQEQGVEHRQEPTQEHKQEEGQKQEEQEEEQEEEGKQEEGQGTKEGREAVSQLQTDSEPKFHSESLSSNPSSFAPRVREVESTPMIMENIQELIRSAQEIDEMNEIYDENSYWRNQNPGSLLQLPHTEALLVLCYSIVENTCIITPTAKAWKYMEEEILGFGKSVCDSLGRRHMSTCALCDFCSLKLEQCHSEASLQRQQCDTSHKTPFVSPLLASQSLSIGNQVGSPESGRFYGLDLYGGLHMDFWCARLATKGCEDVRVSGWLQTEFLSFQDGDFPTKICDTDYIQYPNYCSFKSQQCLMRNRNRKVSRMRCLQNETYSALSPGKSEDVVLRWSQEFSTLTLGQFG | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 11 | Phosphorylation | PAAGFLPSLLKVLLL CCCCCHHHHHHHHHH | 48.78 | 24719451 | |
| 128 | Phosphorylation | VLCSQPVSILSPNTL EHHCCCEEECCCCHH | 25.21 | 25693802 | |
| 141 | Phosphorylation | TLKEIEASAEVSPTT HHHHHHHCCCCCCCC | 16.51 | 22252499 | |
| 145 | Phosphorylation | IEASAEVSPTTMTSP HHHCCCCCCCCCCCC | 14.18 | 22252507 | |
| 260 | Phosphorylation | EPKFHSESLSSNPSS CCCCCCHHHCCCCCC | 36.24 | 28961369 | |
| 277 | Phosphorylation | PRVREVESTPMIMEN CCCEECCCCHHHHHH | 42.88 | 24275569 | |
| 291 | Phosphorylation | NIQELIRSAQEIDEM HHHHHHHHHHHHHHH | 27.58 | 30622161 | |
| 302 | Phosphorylation | IDEMNEIYDENSYWR HHHHHHHCCCCCCCC | 15.83 | 30622161 | |
| 347 | Acetylation | TPTAKAWKYMEEEIL CCCHHHHHHHHHHHH | 39.31 | 25038526 | |
| 370 | Phosphorylation | SLGRRHMSTCALCDF HHCCHHCCHHHHHHH | 17.76 | 25693802 | |
| 371 | Phosphorylation | LGRRHMSTCALCDFC HCCHHCCHHHHHHHH | 8.33 | 25693802 | |
| 381 | Acetylation | LCDFCSLKLEQCHSE HHHHHHCCHHHHCCH | 33.41 | 25038526 | |
| 387 | Phosphorylation | LKLEQCHSEASLQRQ CCHHHHCCHHHHHHH | 42.35 | 30622161 | |
| 390 | Phosphorylation | EQCHSEASLQRQQCD HHHCCHHHHHHHHCC | 22.45 | 30622161 | |
| 402 | Phosphorylation | QCDTSHKTPFVSPLL HCCCCCCCCCCHHHH | 19.28 | 25693802 | |
| 406 | Phosphorylation | SHKTPFVSPLLASQS CCCCCCCHHHHHCCC | 15.37 | 25693802 | |
| 411 | Phosphorylation | FVSPLLASQSLSIGN CCHHHHHCCCCCCCC | 21.92 | 25693802 | |
| 413 | Phosphorylation | SPLLASQSLSIGNQV HHHHHCCCCCCCCCC | 22.91 | 25693802 | |
| 415 | Phosphorylation | LLASQSLSIGNQVGS HHHCCCCCCCCCCCC | 33.43 | 25693802 | |
| 491 | Acetylation | YPNYCSFKSQQCLMR CCCCCCHHHHHHHHH | 30.94 | 25038526 | |
| 519 | Phosphorylation | NETYSALSPGKSEDV CCCCCCCCCCCCHHH | 31.18 | 24719451 | |
| 523 | Phosphorylation | SALSPGKSEDVVLRW CCCCCCCCHHHHHEE | 44.97 | 22210691 |
| 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 ACRBP_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACRBP_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 ACRBP_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ACRBP_HUMAN !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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