UniProt ID | ZPBP1_HUMAN | |
---|---|---|
UniProt AC | Q9BS86 | |
Protein Name | Zona pellucida-binding protein 1 | |
Gene Name | ZPBP | |
Organism | Homo sapiens (Human). | |
Sequence Length | 351 | |
Subcellular Localization |
Cytoplasmic vesicle, secretory vesicle, acrosome membrane Peripheral membrane protein . Secreted . First localized in acrosome granule, later migrates to the inner and outer acrosomal membrane. Released after the acrosomal reaction. |
|
Protein Description | Plays a role in acrosome compaction and sperm morphogenesis. [PubMed: 21911476 Is implicated in sperm-oocyte interaction during fertilization (By similarity] | |
Protein Sequence | MEAFALGPARRGRRRTRAAGSLLSRAAILLFISAFLVRVPSSVGHLVRLPRAFRLTKDSVKIVGSTSFPVKAYVMLHQKSPHVLCVTQQLRNAELIDPSFQWYGPKGKVVSVENRTAQITSTGSLVFQNFEESMSGIYTCFLEYKPTVEEIVKRLQLKYAIYAYREPHYYYQFTARYHAAPCNSIYNISFEKKLLQILSKLLLDLSCEISLLKSECHRVKMQRAGLQNELFFAFSVSSLDTEKGPKRCTDHNCEPYKRLFKAKNLIERFFNQQVEILGRRAEQLPQIYYIEGTLQMVWINRCFPGYGMNVQQHPKCPECCVICSPGSYNPRDGIHCLQCNSSLVYGAKTCL | |
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 |
---|---|---|---|---|---|
16 | Phosphorylation | ARRGRRRTRAAGSLL CCCCHHHHHHHHHHH | 23.89 | 22210691 | |
21 | Phosphorylation | RRTRAAGSLLSRAAI HHHHHHHHHHHHHHH | 22.78 | 24719451 | |
24 | Phosphorylation | RAAGSLLSRAAILLF HHHHHHHHHHHHHHH | 25.76 | 24719451 | |
42 | Phosphorylation | FLVRVPSSVGHLVRL HHHCCCCHHHHHHCC | 26.50 | 24114839 | |
65 | Phosphorylation | DSVKIVGSTSFPVKA CCEEEEECCCCCEEE | 15.24 | 30622161 | |
66 | Phosphorylation | SVKIVGSTSFPVKAY CEEEEECCCCCEEEE | 28.58 | 28787133 | |
67 | Phosphorylation | VKIVGSTSFPVKAYV EEEEECCCCCEEEEE | 29.29 | 30622161 | |
114 | N-linked_Glycosylation | GKVVSVENRTAQITS CCEEEEECCEEEEEC | 44.43 | UniProtKB CARBOHYD | |
133 | Phosphorylation | VFQNFEESMSGIYTC EECCHHHHHCCEEEE | 15.85 | 22468782 | |
138 | Phosphorylation | EESMSGIYTCFLEYK HHHHCCEEEEHHEEC | 10.86 | 22468782 | |
139 | Phosphorylation | ESMSGIYTCFLEYKP HHHCCEEEEHHEECC | 8.55 | 22468782 | |
158 | Acetylation | IVKRLQLKYAIYAYR HHHHHCHHHHHEECC | 21.48 | 25038526 | |
187 | N-linked_Glycosylation | APCNSIYNISFEKKL CCCCCEEECCHHHHH | 23.04 | UniProtKB CARBOHYD | |
199 | Phosphorylation | KKLLQILSKLLLDLS HHHHHHHHHHHHHHH | 23.92 | 24719451 | |
210 | Phosphorylation | LDLSCEISLLKSECH HHHHHHHHHHHHHHH | 12.83 | 24719451 | |
249 | Phosphorylation | EKGPKRCTDHNCEPY CCCCCCCCCCCCHHH | 44.31 | 24719451 | |
324 | Phosphorylation | PECCVICSPGSYNPR CCCEEEECCCCCCCC | 22.60 | 29978859 | |
328 | Phosphorylation | VICSPGSYNPRDGIH EEECCCCCCCCCCCE | 34.79 | 29978859 | |
340 | N-linked_Glycosylation | GIHCLQCNSSLVYGA CCEEEECCCEEEEEC | 22.98 | UniProtKB CARBOHYD | |
341 | Phosphorylation | IHCLQCNSSLVYGAK CEEEECCCEEEEECC | 32.45 | 29978859 | |
342 | Phosphorylation | HCLQCNSSLVYGAKT EEEECCCEEEEECCC | 14.09 | 29978859 | |
345 | Phosphorylation | QCNSSLVYGAKTCL- ECCCEEEEECCCCC- | 19.36 | 29978859 | |
349 | Phosphorylation | SLVYGAKTCL----- EEEEECCCCC----- | 20.64 | 29978859 |
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 ZPBP1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZPBP1_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 ZPBP1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ZPBP1_HUMAN !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...