UniProt ID | RECK_HUMAN | |
---|---|---|
UniProt AC | O95980 | |
Protein Name | Reversion-inducing cysteine-rich protein with Kazal motifs | |
Gene Name | RECK | |
Organism | Homo sapiens (Human). | |
Sequence Length | 971 | |
Subcellular Localization |
Cell membrane Lipid-anchor, GPI-anchor. |
|
Protein Description | Negatively regulates matrix metalloproteinase-9 (MMP-9) by suppressing MMP-9 secretion and by direct inhibition of its enzymatic activity. RECK down-regulation by oncogenic signals may facilitate tumor invasion and metastasis. Appears to also regulate MMP-2 and MT1-MMP, which are involved in cancer progression.. | |
Protein Sequence | MATVRASLRGALLLLLAVAGVAEVAGGLAPGSAGALCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLQRAPDYCPETMVEIWNCMNSSLPGVFKKSDGWVGLGCCELAIALECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREYCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQEFDRFCEYNPVEVSMLTCLADVREPCQLGCRNLTYCTNFNNRPTELFRSCNAQSDQGAMNDMKLWEKGSIKMPFINIPVLDIKKCQPEMWKAIACSLQIKPCHSKSRGSIICKSDCVEILKKCGDQNKFPEDHTAESICELLSPTDDLKNCIPLDTYLRPSTLGNIVEEVTHPCNPNPCPANELCEVNRKGCPSGDPCLPYFCVQGCKLGEASDFIVRQGTLIQVPSSAGEVGCYKICSCGQSGLLENCMEMHCIDLQKSCIVGGKRKSHGTSFSIDCNVCSCFAGNLVCSTRLCLSEHSSEDDRRTFTGLPCNCADQFVPVCGQNGRTYPSACIARCVGLQDHQFEFGSCMSKDPCNPNPCQKNQRCIPKPQVCLTTFDKFGCSQYECVPRQLACDQVQDPVCDTDHMEHNNLCTLYQRGKSLSYKGPCQPFCRATEPVCGHNGETYSSVCAAYSDRVAVDYYGDCQAVGVLSEHSSVAECASVKCPSLLAAGCKPIIPPGACCPLCAGMLRVLFDKEKLDTIAKVTNKKPITVLEILQKIRMHVSVPQCDVFGYFSIESEIVILIIPVDHYPKALQIEACNKEAEKIESLINSDSPTLASHVPLSALIISQVQVSSSVPSAGVRARPSCHSLLLPLSLGLALHLLWTYN | |
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 |
---|---|---|---|---|---|
39 | N-linked_Glycosylation | SAGALCCNHSKDNQM CCCHHHCCCCCCCHH | 41.28 | UniProtKB CARBOHYD | |
56 | Phosphorylation | DVCEQIFSSKSESRL HHHHHHHCCCCHHHH | 38.19 | 26471730 | |
86 | N-linked_Glycosylation | VEIWNCMNSSLPGVF HHHHHHHHCCCCCCE | 30.55 | UniProtKB CARBOHYD | |
154 | Phosphorylation | MGSVCCSYAGHHTNC CCCCHHHHCCCCCCH | 11.59 | 22817900 | |
164 | Phosphorylation | HHTNCREYCQAIFRT CCCCHHHHHHHHHCC | 3.15 | 22817900 | |
200 | N-linked_Glycosylation | QLIHCVNNYTQSYPM HHHHHHHCCCCCCCC | 22.34 | UniProtKB CARBOHYD | |
276 | O-linked_Glycosylation | QSVHPGVTVHPPPST CCCCCCCEECCCCCC | 21.00 | OGP | |
294 | Phosphorylation | GAKLHCCSKANTSTC CCEEEECCCCCHHHH | 39.95 | - | |
297 | N-linked_Glycosylation | LHCCSKANTSTCREL EEECCCCCHHHHHHH | 38.00 | UniProtKB CARBOHYD | |
298 | Phosphorylation | HCCSKANTSTCRELC EECCCCCHHHHHHHH | 30.21 | - | |
299 | Phosphorylation | CCSKANTSTCRELCT ECCCCCHHHHHHHHH | 25.89 | - | |
300 | Phosphorylation | CSKANTSTCRELCTK CCCCCHHHHHHHHHH | 17.34 | - | |
352 | N-linked_Glycosylation | PCQLGCRNLTYCTNF HHHCCCCCCCEEECC | 40.59 | UniProtKB CARBOHYD | |
454 | Phosphorylation | NKFPEDHTAESICEL CCCCCCCHHHHHHHH | 44.43 | 22210691 | |
457 | Phosphorylation | PEDHTAESICELLSP CCCCHHHHHHHHHCC | 30.03 | 22210691 | |
476 | Phosphorylation | KNCIPLDTYLRPSTL HCCCCCCCCCCHHHC | 31.94 | 22210691 | |
477 | Phosphorylation | NCIPLDTYLRPSTLG CCCCCCCCCCHHHCC | 10.61 | 22210691 | |
617 | Phosphorylation | CSTRLCLSEHSSEDD EEEEEEECCCCCCCC | 32.06 | 23312004 | |
620 | Phosphorylation | RLCLSEHSSEDDRRT EEEECCCCCCCCCCC | 31.22 | 23312004 | |
621 | Phosphorylation | LCLSEHSSEDDRRTF EEECCCCCCCCCCCC | 47.13 | 24505115 | |
684 | Sumoylation | CNPNPCQKNQRCIPK CCCCCCCCCCCCCCC | 62.86 | - | |
843 | Phosphorylation | FDKEKLDTIAKVTNK CCHHHHHHHHHHCCC | 33.02 | - | |
848 | Phosphorylation | LDTIAKVTNKKPITV HHHHHHHCCCCCCCH | 40.38 | - | |
942 | GPI-anchor | QVSSSVPSAGVRARP EECCCCCCCCCCCCC | 35.18 | - | |
969 | Phosphorylation | LALHLLWTYN----- HHHHHHHHCC----- | 17.10 | - | |
970 | Phosphorylation | ALHLLWTYN------ HHHHHHHCC------ | 13.80 | - |
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 RECK_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RECK_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 RECK_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
KEAP1_HUMAN | KEAP1 | physical | 25416956 | |
TRI39_HUMAN | TRIM39 | physical | 25416956 | |
USBP1_HUMAN | USHBP1 | physical | 25416956 | |
K1C40_HUMAN | KRT40 | physical | 25416956 | |
TRI69_HUMAN | TRIM69 | physical | 25416956 | |
TEKT4_HUMAN | TEKT4 | physical | 25416956 | |
NT2NL_HUMAN | NOTCH2NL | physical | 25416956 | |
MCCB_HUMAN | MCCC2 | physical | 28514442 | |
IFNA4_HUMAN | IFNA4 | physical | 28514442 | |
ACOX1_HUMAN | ACOX1 | physical | 28514442 |
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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