AMPB_HUMAN - dbPTM
AMPB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMPB_HUMAN
UniProt AC Q9H4A4
Protein Name Aminopeptidase B
Gene Name RNPEP
Organism Homo sapiens (Human).
Sequence Length 650
Subcellular Localization Secreted.
Protein Description Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity)..
Protein Sequence MASGEHSPGSGAARRPLHSAQAVDVASASNFRAFELLHLHLDLRAEFGPPGPGAGSRGLSGTAVLDLRCLEPEGAAELRLDSHPCLEVTAAALRRERPGSEEPPAEPVSFYTQPFSHYGQALCVSFPQPCRAAERLQVLLTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKYKYSALIEVPDGFTAVMSASTWEKRGPNKFFFQMCQPIPSYLIALAIGDLVSAEVGPRSRVWAEPCLIDAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGFTMYAQRRISTILFGAAYTCLEAATGRALLRQHMDITGEENPLNKLRVKIEPGVDPDDTYNETPYEKGFCFVSYLAHLVGDQDQFDSFLKAYVHEFKFRSILADDFLDFYLEYFPELKKKRVDIIPGFEFDRWLNTPGWPPYLPDLSPGDSLMKPAEELAQLWAAEELDMKAIEAVAISPWKTYQLVYFLDKILQKSPLPPGNVKKLGDTYPSISNARNAELRLRWGQIVLKNDHQEDFWKVKEFLHNQGKQKYTLPLYHAMMGGSEVAQTLAKETFASTASQLHSNVVNYVQQIVAPKGS
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
2Acetylation------MASGEHSPG
------CCCCCCCCC		26.6621406692
3Phosphorylation-----MASGEHSPGS
-----CCCCCCCCCC		43.3330266825
7Phosphorylation-MASGEHSPGSGAAR
-CCCCCCCCCCCCCC		27.0129255136
10PhosphorylationSGEHSPGSGAARRPL
CCCCCCCCCCCCCCC		28.7430266825
19PhosphorylationAARRPLHSAQAVDVA
CCCCCCCCCCEECHH		29.7428464451
30UbiquitinationVDVASASNFRAFELL
ECHHHHCCCCHHHHH		30.0922817900
31UbiquitinationDVASASNFRAFELLH
CHHHHCCCCHHHHHH		5.7422817900
32UbiquitinationVASASNFRAFELLHL
HHHHCCCCHHHHHHH		42.4922817900
60O-linked_GlycosylationGAGSRGLSGTAVLDL
CCCCCCCCCEEEEEE		36.6023301498
85GlutathionylationLRLDSHPCLEVTAAA
ECCCCCCHHHHHHHH		4.1822555962
100PhosphorylationLRRERPGSEEPPAEP
HHCCCCCCCCCCCCC		41.2828348404
104UbiquitinationRPGSEEPPAEPVSFY
CCCCCCCCCCCCCEE		53.1621963094
108UbiquitinationEEPPAEPVSFYTQPF
CCCCCCCCCEECCCC		4.6822817900
151GlutathionylationVGEGPGVCWLAPEQT
CCCCCCEEEECCCCC		2.8222555962
161AcetylationAPEQTAGKKKPFVYT
CCCCCCCCCCCCEEE		55.9826051181
161UbiquitinationAPEQTAGKKKPFVYT
CCCCCCCCCCCCEEE		55.9821963094
162UbiquitinationPEQTAGKKKPFVYTQ
CCCCCCCCCCCEEEC		65.8422817900
163UbiquitinationEQTAGKKKPFVYTQG
CCCCCCCCCCEEECC		47.3722817900
247O-linked_GlycosylationSAEVGPRSRVWAEPC
CCCCCCCCCCCCCCC		34.0323301498
255UbiquitinationRVWAEPCLIDAAKEE
CCCCCCCHHHHHHHH		6.0929967540
263UbiquitinationIDAAKEEYNGVIEEF
HHHHHHHHCCHHHHH		20.5021963094
265UbiquitinationAAKEEYNGVIEEFLA
HHHHHHCCHHHHHHH		22.3727667366
267UbiquitinationKEEYNGVIEEFLATG
HHHHCCHHHHHHHHC		4.4422817900
300UbiquitinationPSFPFGGMENPCLTF
CCCCCCCCCCCHHHC		4.6229967540
302UbiquitinationFPFGGMENPCLTFVT
CCCCCCCCCHHHCHH		24.5627667366
310UbiquitinationPCLTFVTPCLLAGDR
CHHHCHHHHHHCCCH		11.0622817900
312UbiquitinationLTFVTPCLLAGDRSL
HHCHHHHHHCCCHHH		3.7522817900
383SulfoxidationRALLRQHMDITGEEN
HHHHHHHHCCCCCCC		2.7830846556
394UbiquitinationGEENPLNKLRVKIEP
CCCCCCHHCEEEEEC		45.4021906983
398AcetylationPLNKLRVKIEPGVDP
CCHHCEEEEECCCCC		34.6126051181
398SumoylationPLNKLRVKIEPGVDP
CCHHCEEEEECCCCC		34.61-
398SumoylationPLNKLRVKIEPGVDP
CCHHCEEEEECCCCC		34.61-
398UbiquitinationPLNKLRVKIEPGVDP
CCHHCEEEEECCCCC		34.6121906983
402UbiquitinationLRVKIEPGVDPDDTY
CEEEEECCCCCCCCC		24.5421906983
406UbiquitinationIEPGVDPDDTYNETP
EECCCCCCCCCCCCC		57.3221906983
408PhosphorylationPGVDPDDTYNETPYE
CCCCCCCCCCCCCCC		35.3119060867
409PhosphorylationGVDPDDTYNETPYEK
CCCCCCCCCCCCCCC		20.2822817900
412PhosphorylationPDDTYNETPYEKGFC
CCCCCCCCCCCCCCC		27.7728102081
414PhosphorylationDTYNETPYEKGFCFV
CCCCCCCCCCCCCHH		37.3822817900
414UbiquitinationDTYNETPYEKGFCFV
CCCCCCCCCCCCCHH		37.3829967540
424UbiquitinationGFCFVSYLAHLVGDQ
CCCHHHHHHHHHCCH		1.5627667366
436PhosphorylationGDQDQFDSFLKAYVH
CCHHHHHHHHHHHHH		33.4924719451
446UbiquitinationKAYVHEFKFRSILAD
HHHHHHHCHHHHHHH		36.5619608861
446AcetylationKAYVHEFKFRSILAD
HHHHHHHCHHHHHHH		36.5619608861
459UbiquitinationADDFLDFYLEYFPEL
HHHHHHHHHHHCHHH		9.7829967540
461UbiquitinationDFLDFYLEYFPELKK
HHHHHHHHHCHHHHH		33.4827667366
469UbiquitinationYFPELKKKRVDIIPG
HCHHHHHCCCCCCCC		56.9422817900
471UbiquitinationPELKKKRVDIIPGFE
HHHHHCCCCCCCCCC		9.4722817900
528PhosphorylationAIEAVAISPWKTYQL
HHHHHEECCCCHHHH		18.2527050516
532PhosphorylationVAISPWKTYQLVYFL
HEECCCCHHHHHHHH		16.7822210691
533PhosphorylationAISPWKTYQLVYFLD
EECCCCHHHHHHHHH		8.9822210691
537PhosphorylationWKTYQLVYFLDKILQ
CCHHHHHHHHHHHHH		13.66-
545UbiquitinationFLDKILQKSPLPPGN
HHHHHHHHCCCCCCC		51.0729967540
555UbiquitinationLPPGNVKKLGDTYPS
CCCCCCHHCCCCCCC		54.1127667366
562PhosphorylationKLGDTYPSISNARNA
HCCCCCCCHHCCCCC		28.3828857561
590UbiquitinationDHQEDFWKVKEFLHN
CCHHHHHHHHHHHHH		43.3429967540
592UbiquitinationQEDFWKVKEFLHNQG
HHHHHHHHHHHHHCC		38.7427667366
5922-HydroxyisobutyrylationQEDFWKVKEFLHNQG
HHHHHHHHHHHHHCC		38.74-
600AcetylationEFLHNQGKQKYTLPL
HHHHHCCCCEEEHHH		33.5825953088
600UbiquitinationEFLHNQGKQKYTLPL
HHHHHCCCCEEEHHH		33.5822817900
602UbiquitinationLHNQGKQKYTLPLYH
HHHCCCCEEEHHHHH		43.6222817900
604PhosphorylationNQGKQKYTLPLYHAM
HCCCCEEEHHHHHHH		29.00-
608PhosphorylationQKYTLPLYHAMMGGS
CEEEHHHHHHHHCCH		5.89-
650PhosphorylationQIVAPKGS-------
HHHCCCCC-------		43.0828450419
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 AMPB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of AMPB_HUMAN !!
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 AMPB_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-7, AND MASS SPECTROMETRY.
"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-446, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-7, AND MASS SPECTROMETRY.

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