| UniProt ID | ANXA7_HUMAN | |
|---|---|---|
| UniProt AC | P20073 | |
| Protein Name | Annexin A7 | |
| Gene Name | ANXA7 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 488 | |
| Subcellular Localization | ||
| Protein Description | Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.. | |
| Protein Sequence | MSYPGYPPTGYPPFPGYPPAGQESSFPPSGQYPYPSGFPPMGGGAYPQVPSSGYPGAGGYPAPGGYPAPGGYPGAPQPGGAPSYPGVPPGQGFGVPPGGAGFSGYPQPPSQSYGGGPAQVPLPGGFPGGQMPSQYPGGQPTYPSQINTDSFSSYPVFSPVSLDYSSEPATVTQVTQGTIRPAANFDAIRDAEILRKAMKGFGTDEQAIVDVVANRSNDQRQKIKAAFKTSYGKDLIKDLKSELSGNMEELILALFMPPTYYDAWSLRKAMQGAGTQERVLIEILCTRTNQEIREIVRCYQSEFGRDLEKDIRSDTSGHFERLLVSMCQGNRDENQSINHQMAQEDAQRLYQAGEGRLGTDESCFNMILATRSFPQLRATMEAYSRMANRDLLSSVSREFSGYVESGLKTILQCALNRPAFFAERLYYAMKGAGTDDSTLVRIVVTRSEIDLVQIKQMFAQMYQKTLGTMIAGDTSGDYRRLLLAIVGQ | |
| 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 |
|---|---|---|---|---|---|
| 177 (in isoform 2) | Ubiquitination | - | 17.47 | 21906983 | |
| 196 | Acetylation | RDAEILRKAMKGFGT HHHHHHHHHHCCCCC | 49.76 | 156479 | |
| 199 (in isoform 1) | Ubiquitination | - | 56.82 | 22053931 | |
| 199 | Ubiquitination | EILRKAMKGFGTDEQ HHHHHHHCCCCCCHH | 56.82 | 21906983 | |
| 211 (in isoform 2) | Acetylation | - | 2.80 | - | |
| 211 | Acetylation | DEQAIVDVVANRSND CHHHHHHHHHCCCHH | 2.80 | 19608861 | |
| 215 (in isoform 2) | Ubiquitination | - | 27.40 | 21906983 | |
| 216 | Phosphorylation | VDVVANRSNDQRQKI HHHHHCCCHHHHHHH | 44.56 | 24719451 | |
| 224 | Ubiquitination | NDQRQKIKAAFKTSY HHHHHHHHHHHHHHH | 40.47 | - | |
| 228 | Malonylation | QKIKAAFKTSYGKDL HHHHHHHHHHHHHHH | 31.66 | 26320211 | |
| 228 | Acetylation | QKIKAAFKTSYGKDL HHHHHHHHHHHHHHH | 31.66 | 26051181 | |
| 228 | Ubiquitination | QKIKAAFKTSYGKDL HHHHHHHHHHHHHHH | 31.66 | - | |
| 233 | Malonylation | AFKTSYGKDLIKDLK HHHHHHHHHHHHHHH | 40.92 | 26320211 | |
| 233 | Acetylation | AFKTSYGKDLIKDLK HHHHHHHHHHHHHHH | 40.92 | 19608861 | |
| 233 | Ubiquitination | AFKTSYGKDLIKDLK HHHHHHHHHHHHHHH | 40.92 | 19608861 | |
| 237 | Malonylation | SYGKDLIKDLKSELS HHHHHHHHHHHHHHC | 65.39 | 26320211 | |
| 237 | Acetylation | SYGKDLIKDLKSELS HHHHHHHHHHHHHHC | 65.39 | 25953088 | |
| 237 (in isoform 1) | Ubiquitination | - | 65.39 | 22053931 | |
| 237 | Ubiquitination | SYGKDLIKDLKSELS HHHHHHHHHHHHHHC | 65.39 | - | |
| 240 | Acetylation | KDLIKDLKSELSGNM HHHHHHHHHHHCCCH | 52.60 | 26051181 | |
| 265 | Phosphorylation | PTYYDAWSLRKAMQG CCHHHHHHHHHHHCC | 21.73 | 24719451 | |
| 268 | Ubiquitination | YDAWSLRKAMQGAGT HHHHHHHHHHCCCCC | 54.20 | - | |
| 270 | Sulfoxidation | AWSLRKAMQGAGTQE HHHHHHHHCCCCCCH | 4.18 | 30846556 | |
| 286 | Phosphorylation | VLIEILCTRTNQEIR HHHHHHHHCCCHHHH | 36.76 | 21406692 | |
| 298 | S-nitrosocysteine | EIREIVRCYQSEFGR HHHHHHHHHHHHHCC | 2.22 | - | |
| 298 | S-nitrosylation | EIREIVRCYQSEFGR HHHHHHHHHHHHHCC | 2.22 | 19483679 | |
| 299 | Phosphorylation | IREIVRCYQSEFGRD HHHHHHHHHHHHCCC | 12.43 | 28152594 | |
| 309 | Acetylation | EFGRDLEKDIRSDTS HHCCCHHHHHHCCCC | 66.79 | 26051181 | |
| 309 | Ubiquitination | EFGRDLEKDIRSDTS HHCCCHHHHHHCCCC | 66.79 | - | |
| 309 | Malonylation | EFGRDLEKDIRSDTS HHCCCHHHHHHCCCC | 66.79 | 26320211 | |
| 313 | Phosphorylation | DLEKDIRSDTSGHFE CHHHHHHCCCCCHHH | 45.64 | 26437602 | |
| 315 | Phosphorylation | EKDIRSDTSGHFERL HHHHHCCCCCHHHHH | 37.54 | 26437602 | |
| 316 | Phosphorylation | KDIRSDTSGHFERLL HHHHCCCCCHHHHHH | 34.95 | 28348404 | |
| 326 | Sulfoxidation | FERLLVSMCQGNRDE HHHHHHHHHHCCCCC | 1.22 | 30846556 | |
| 336 | Phosphorylation | GNRDENQSINHQMAQ CCCCCCCCCCHHHHH | 36.62 | 28348404 | |
| 341 | Sulfoxidation | NQSINHQMAQEDAQR CCCCCHHHHHHHHHH | 3.02 | 21406390 | |
| 366 | Sulfoxidation | TDESCFNMILATRSF CCHHHHHHHHHCCCC | 1.02 | 21406390 | |
| 380 | Sulfoxidation | FPQLRATMEAYSRMA CHHHHHHHHHHHHHH | 2.43 | 30846556 | |
| 393 | Phosphorylation | MANRDLLSSVSREFS HHCHHHHHHHHHHHH | 35.67 | 21406692 | |
| 394 | Phosphorylation | ANRDLLSSVSREFSG HCHHHHHHHHHHHHH | 24.87 | 21406692 | |
| 396 | Phosphorylation | RDLLSSVSREFSGYV HHHHHHHHHHHHHHH | 28.21 | 21406692 | |
| 400 | Phosphorylation | SSVSREFSGYVESGL HHHHHHHHHHHHHHH | 25.18 | 113306939 | |
| 402 | Phosphorylation | VSREFSGYVESGLKT HHHHHHHHHHHHHHH | 10.39 | 14583609 | |
| 408 (in isoform 2) | Ubiquitination | - | 36.72 | 21906983 | |
| 426 | Phosphorylation | AFFAERLYYAMKGAG HHHHHHHHHHHHCCC | 8.73 | 23663014 | |
| 427 | Phosphorylation | FFAERLYYAMKGAGT HHHHHHHHHHHCCCC | 12.57 | 23663014 | |
| 430 | Malonylation | ERLYYAMKGAGTDDS HHHHHHHHCCCCCCC | 37.12 | 26320211 | |
| 430 | Acetylation | ERLYYAMKGAGTDDS HHHHHHHHCCCCCCC | 37.12 | 25953088 | |
| 430 (in isoform 1) | Ubiquitination | - | 37.12 | 22053931 | |
| 430 | Ubiquitination | ERLYYAMKGAGTDDS HHHHHHHHCCCCCCC | 37.12 | - | |
| 434 | Phosphorylation | YAMKGAGTDDSTLVR HHHHCCCCCCCCEEE | 35.78 | 23663014 | |
| 437 | Phosphorylation | KGAGTDDSTLVRIVV HCCCCCCCCEEEEEE | 26.84 | 23663014 | |
| 438 | Phosphorylation | GAGTDDSTLVRIVVT CCCCCCCCEEEEEEE | 35.95 | 23663014 | |
| 446 (in isoform 2) | Phosphorylation | - | 22.23 | - | |
| 447 | Phosphorylation | VRIVVTRSEIDLVQI EEEEEECCCCCHHHH | 29.54 | 63743355 | |
| 455 | Ubiquitination | EIDLVQIKQMFAQMY CCCHHHHHHHHHHHH | 20.72 | - | |
| 462 | Phosphorylation | KQMFAQMYQKTLGTM HHHHHHHHHHHHCHH | 8.52 | 21406692 | |
| 465 | Phosphorylation | FAQMYQKTLGTMIAG HHHHHHHHHCHHHCC | 18.20 | 21406692 | |
| 468 | Phosphorylation | MYQKTLGTMIAGDTS HHHHHHCHHHCCCCC | 14.44 | 20068231 | |
| 474 | Phosphorylation | GTMIAGDTSGDYRRL CHHHCCCCCHHHHHH | 33.42 | 21406692 | |
| 475 | Phosphorylation | TMIAGDTSGDYRRLL HHHCCCCCHHHHHHH | 34.11 | 110742291 | |
| 478 | Phosphorylation | AGDTSGDYRRLLLAI CCCCCHHHHHHHHHH | 10.93 | 20068231 |
| 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 ANXA7_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ANXA7_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 ANXA7_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| 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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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-233, AND MASS SPECTROMETRY. | |
