AMPQ_HUMAN - dbPTM
AMPQ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMPQ_HUMAN
UniProt AC Q6Q4G3
Protein Name Aminopeptidase Q {ECO:0000305}
Gene Name LVRN {ECO:0000312|HGNC:HGNC:26904}
Organism Homo sapiens (Human).
Sequence Length 990
Subcellular Localization Membrane
Single-pass type II membrane protein .
Protein Description Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C..
Protein Sequence MGPPSSSGFYVSRAVALLLAGLVAALLLALAVLAALYGHCERVPPSELPGLRDLEAESSPPLRQKPTPTPKPSSARELAVTTTPSNWRPPGPWDQLRLPPWLVPLHYDLELWPQLRPDELPAGSLPFTGRVNITVRCTVATSRLLLHSLFQDCERAEVRGPLSPGTGNATVGRVPVDDVWFALDTEYMVLELSEPLKPGSSYELQLSFSGLVKEDLREGLFLNVYTDQGERRALLASQLEPTFARYVFPCFDEPALKATFNITMIHHPSYVALSNMPKLGQSEKEDVNGSKWTVTTFSTTPHMPTYLVAFVICDYDHVNRTERGKEIRIWARKDAIANGSADFALNITGPIFSFLEDLFNISYSLPKTDIIALPSFDNHAMENWGLMIFDESGLLLEPKDQLTEKKTLISYVVSHEIGHQWFGNLVTMNWWNNIWLNEGFASYFEFEVINYFNPKLPRNEIFFSNILHNILREDHALVTRAVAMKVENFKTSEIQELFDIFTYSKGASMARMLSCFLNEHLFVSALKSYLKTFSYSNAEQDDLWRHFQMAIDDQSTVILPATIKNIMDSWTHQSGFPVITLNVSTGVMKQEPFYLENIKNRTLLTSNDTWIVPILWIKNGTTQPLVWLDQSSKVFPEMQVSDSDHDWVILNLNMTGYYRVNYDKLGWKKLNQQLEKDPKAIPVIHRLQLIDDAFSLSKNNYIEIETALELTKYLAEEDEIIVWHTVLVNLVTRDLVSEVNIYDIYSLLKRYLLKRLNLIWNIYSTIIRENVLALQDDYLALISLEKLFVTACWLGLEDCLQLSKELFAKWVDHPENEIPYPIKDVVLCYGIALGSDKEWDILLNTYTNTTNKEEKIQLAYAMSCSKDPWILNRYMEYAISTSPFTSNETNIIEVVASSEVGRYVAKDFLVNNWQAVSKRYGTQSLINLIYTIGRTVTTDLQIVELQQFFSNMLEEHQRIRVHANLQTIKNENLKNKKLSARIAAWLRRNT
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
46PhosphorylationHCERVPPSELPGLRD
HHHCCCHHHCCCCCC		45.7726270265
58PhosphorylationLRDLEAESSPPLRQK
CCCCCCCCCCCCCCC		56.0126699800
59PhosphorylationRDLEAESSPPLRQKP
CCCCCCCCCCCCCCC		23.2626699800
132N-linked_GlycosylationLPFTGRVNITVRCTV
CCCCCCEEEEEEEEE		23.89UniProtKB CARBOHYD
168N-linked_GlycosylationPLSPGTGNATVGRVP
CCCCCCCCCEEECEE		32.07UniProtKB CARBOHYD
237PhosphorylationERRALLASQLEPTFA
HHHHHHHHHCCCHHH		34.9625690035
242PhosphorylationLASQLEPTFARYVFP
HHHHCCCHHHHHHCC		22.1325690035
261N-linked_GlycosylationPALKATFNITMIHHP
HHHHEEEEEEEECCH		25.19UniProtKB CARBOHYD
288N-linked_GlycosylationQSEKEDVNGSKWTVT
CCCCCCCCCCCEEEE		62.43UniProtKB CARBOHYD
319N-linked_GlycosylationICDYDHVNRTERGKE
EECCCCCCCCCCCCE		41.56UniProtKB CARBOHYD
325AcetylationVNRTERGKEIRIWAR
CCCCCCCCEEEEEEE		57.0730590197
346N-linked_GlycosylationGSADFALNITGPIFS
CCCCEEEECCHHHHH		26.75UniProtKB CARBOHYD
508PhosphorylationFTYSKGASMARMLSC
HHHCCHHHHHHHHHH		22.9526552605
514PhosphorylationASMARMLSCFLNEHL
HHHHHHHHHHHCHHH		8.0926552605
524PhosphorylationLNEHLFVSALKSYLK
HCHHHHHHHHHHHHH		22.1326552605
607N-linked_GlycosylationNRTLLTSNDTWIVPI
CCEEECCCCCEEEEE		45.56UniProtKB CARBOHYD
653N-linked_GlycosylationDWVILNLNMTGYYRV
CEEEEEEECEEEEEC		25.54UniProtKB CARBOHYD
701PhosphorylationFSLSKNNYIEIETAL
HHCCCCCCEEHHHHH		14.8827067055
706PhosphorylationNNYIEIETALELTKY
CCCEEHHHHHHHHHH		42.0527067055
745PhosphorylationEVNIYDIYSLLKRYL
CCCHHHHHHHHHHHH		7.1424719451
746PhosphorylationVNIYDIYSLLKRYLL
CCHHHHHHHHHHHHH		27.7924719451
765PhosphorylationLIWNIYSTIIRENVL
HHHHHHHHHHHHHHH		11.94-
845PhosphorylationEWDILLNTYTNTTNK
HHHHHEEEECCCCCH		31.5229888752
846PhosphorylationWDILLNTYTNTTNKE
HHHHEEEECCCCCHH		9.2729888752
847PhosphorylationDILLNTYTNTTNKEE
HHHEEEECCCCCHHH		24.8529888752
849PhosphorylationLLNTYTNTTNKEEKI
HEEEECCCCCHHHHH		24.7629888752
850PhosphorylationLNTYTNTTNKEEKIQ
EEEECCCCCHHHHHH		46.4929888752
920PhosphorylationWQAVSKRYGTQSLIN
HHHHHHHHCHHHHHH		28.4125072903
922PhosphorylationAVSKRYGTQSLINLI
HHHHHHCHHHHHHHH		13.1725072903
924PhosphorylationSKRYGTQSLINLIYT
HHHHCHHHHHHHHHH		30.9325072903
930PhosphorylationQSLINLIYTIGRTVT
HHHHHHHHHCCCCCC		8.7525072903
931PhosphorylationSLINLIYTIGRTVTT
HHHHHHHHCCCCCCC		15.2325072903
967PhosphorylationRVHANLQTIKNENLK
HHHHCHHHHCCCCCC		36.7724706070
969UbiquitinationHANLQTIKNENLKNK
HHCHHHHCCCCCCCH		62.69-
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 AMPQ_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMPQ_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 AMPQ_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AMPQ_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMPQ_HUMAN

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Related Literatures of Post-Translational Modification

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