RECK_HUMAN - dbPTM
RECK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
39N-linked_GlycosylationSAGALCCNHSKDNQM
CCCHHHCCCCCCCHH
41.28UniProtKB CARBOHYD
56PhosphorylationDVCEQIFSSKSESRL
HHHHHHHCCCCHHHH
38.1926471730
86N-linked_GlycosylationVEIWNCMNSSLPGVF
HHHHHHHHCCCCCCE
30.55UniProtKB CARBOHYD
154PhosphorylationMGSVCCSYAGHHTNC
CCCCHHHHCCCCCCH
11.5922817900
164PhosphorylationHHTNCREYCQAIFRT
CCCCHHHHHHHHHCC
3.1522817900
200N-linked_GlycosylationQLIHCVNNYTQSYPM
HHHHHHHCCCCCCCC
22.34UniProtKB CARBOHYD
276O-linked_GlycosylationQSVHPGVTVHPPPST
CCCCCCCEECCCCCC
21.00OGP
294PhosphorylationGAKLHCCSKANTSTC
CCEEEECCCCCHHHH
39.95-
297N-linked_GlycosylationLHCCSKANTSTCREL
EEECCCCCHHHHHHH
38.00UniProtKB CARBOHYD
298PhosphorylationHCCSKANTSTCRELC
EECCCCCHHHHHHHH
30.21-
299PhosphorylationCCSKANTSTCRELCT
ECCCCCHHHHHHHHH
25.89-
300PhosphorylationCSKANTSTCRELCTK
CCCCCHHHHHHHHHH
17.34-
352N-linked_GlycosylationPCQLGCRNLTYCTNF
HHHCCCCCCCEEECC
40.59UniProtKB CARBOHYD
454PhosphorylationNKFPEDHTAESICEL
CCCCCCCHHHHHHHH
44.4322210691
457PhosphorylationPEDHTAESICELLSP
CCCCHHHHHHHHHCC
30.0322210691
476PhosphorylationKNCIPLDTYLRPSTL
HCCCCCCCCCCHHHC
31.9422210691
477PhosphorylationNCIPLDTYLRPSTLG
CCCCCCCCCCHHHCC
10.6122210691
617PhosphorylationCSTRLCLSEHSSEDD
EEEEEEECCCCCCCC
32.0623312004
620PhosphorylationRLCLSEHSSEDDRRT
EEEECCCCCCCCCCC
31.2223312004
621PhosphorylationLCLSEHSSEDDRRTF
EEECCCCCCCCCCCC
47.1324505115
684SumoylationCNPNPCQKNQRCIPK
CCCCCCCCCCCCCCC
62.86-
843PhosphorylationFDKEKLDTIAKVTNK
CCHHHHHHHHHHCCC
33.02-
848PhosphorylationLDTIAKVTNKKPITV
HHHHHHHCCCCCCCH
40.38-
942GPI-anchorQVSSSVPSAGVRARP
EECCCCCCCCCCCCC
35.18-
969PhosphorylationLALHLLWTYN-----
HHHHHHHHCC-----
17.10-
970PhosphorylationALHLLWTYN------
HHHHHHHCC------
13.80-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RECK_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KEAP1_HUMANKEAP1physical
25416956
TRI39_HUMANTRIM39physical
25416956
USBP1_HUMANUSHBP1physical
25416956
K1C40_HUMANKRT40physical
25416956
TRI69_HUMANTRIM69physical
25416956
TEKT4_HUMANTEKT4physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
MCCB_HUMANMCCC2physical
28514442
IFNA4_HUMANIFNA4physical
28514442
ACOX1_HUMANACOX1physical
28514442

Drug and Disease Associations
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.
Regulatory Network of RECK_HUMAN

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Related Literatures of Post-Translational Modification

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