dbPTM

LCAP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LCAP_HUMAN
UniProt AC	Q9UIQ6
Protein Name	Leucyl-cystinyl aminopeptidase
Gene Name	LNPEP
Organism	Homo sapiens (Human).
Sequence Length	1025
Subcellular Localization	Cell membrane Single-pass type II membrane protein . In brain only the membrane-bound form is found. The protein resides in intracellular vesicles together with GLUT4 and can then translocate to the cell surface in response to insulin and/or oxytoc
Protein Description	Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain..
Protein Sequence	MEPFTNDRLQLPRNMIENSMFEEEPDVVDLAKEPCLHPLEPDEVEYEPRGSRLLVRGLGEHEMEEDEEDYESSAKLLGMSFMNRSSGLRNSATGYRQSPDGACSVPSARTMVVCAFVIVVAVSVIMVIYLLPRCTFTKEGCHKKNQSIGLIQPFATNGKLFPWAQIRLPTAVVPLRYELSLHPNLTSMTFRGSVTISVQALQVTWNIILHSTGHNISRVTFMSAVSSQEKQAEILEYAYHGQIAIVAPEALLAGHNYTLKIEYSANISSSYYGFYGFSYTDESNEKKYFAATQFEPLAARSAFPCFDEPAFKATFIIKIIRDEQYTALSNMPKKSSVVLDDGLVQDEFSESVKMSTYLVAFIVGEMKNLSQDVNGTLVSIYAVPEKIGQVHYALETTVKLLEFFQNYFEIQYPLKKLDLVAIPDFEAGAMENWGLLTFREETLLYDSNTSSMADRKLVTKIIAHELAHQWFGNLVTMKWWNDLWLNEGFATFMEYFSLEKIFKELSSYEDFLDARFKTMKKDSLNSSHPISSSVQSSEQIEEMFDSLSYFKGSSLLLMLKTYLSEDVFQHAVVLYLHNHSYASIQSDDLWDSFNEVTNQTLDVKRMMKTWTLQKGFPLVTVQKKGKELFIQQERFFLNMKPEIQPSDTSYLWHIPLSYVTEGRNYSKYQSVSLLDKKSGVINLTEEVLWVKVNINMNGYYIVHYADDDWEALIHQLKINPYVLSDKDRANLINNIFELAGLGKVPLKRAFDLINYLGNENHTAPITEALFQTDLIYNLLEKLGYMDLASRLVTRVFKLLQNQIQQQTWTDEGTPSMRELRSALLEFACTHNLGNCSTTAMKLFDDWMASNGTQSLPTDVMTTVFKVGAKTDKGWSFLLGKYISIGSEAEKNKILEALASSEDVRKLYWLMKSSLNGDNFRTQKLSFIIRTVGRHFPGHLLAWDFVKENWNKLVQKFPLGSYTIQNIVAGSTYLFSTKTHLSEVQAFFENQSEATFRLRCVQEALEVIQLNIQWMEKNLKSLTWWL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEPFTNDR -------CCCCCCCC	55.44	22814378
19	Phosphorylation	PRNMIENSMFEEEPD CHHHHHCCCCCCCCC	16.44	22199227
32	Phosphorylation	PDVVDLAKEPCLHPL CCHHHHCCCCCCCCC	70.28	27642862
46	Phosphorylation	LEPDEVEYEPRGSRL CCCCCCEECCCCCEE	36.09	25159151
51	Phosphorylation	VEYEPRGSRLLVRGL CEECCCCCEEEEECC	22.49	22499768
61	Ubiquitination	LVRGLGEHEMEEDEE EEECCCCCCCCCCCC	37.59	22505724
70	Phosphorylation	MEEDEEDYESSAKLL CCCCCCCHHHHHHHH	22.46	27273156
72	Phosphorylation	EDEEDYESSAKLLGM CCCCCHHHHHHHHCH	29.39	28450419
73	Phosphorylation	DEEDYESSAKLLGMS CCCCHHHHHHHHCHH	19.92	30576142
75	Ubiquitination	EDYESSAKLLGMSFM CCHHHHHHHHCHHHC	46.31	22505724
77	Phosphorylation	YESSAKLLGMSFMNR HHHHHHHHCHHHCCC	5.50	33259812
80	Phosphorylation	SAKLLGMSFMNRSSG HHHHHCHHHCCCCCC	21.39	22617229
85	Phosphorylation	GMSFMNRSSGLRNSA CHHHCCCCCCCCCCC	24.61	23898821
86	Phosphorylation	MSFMNRSSGLRNSAT HHHCCCCCCCCCCCC	38.31	29978859
91	Phosphorylation	RSSGLRNSATGYRQS CCCCCCCCCCCCCCC	22.30	23401153
93	Phosphorylation	SGLRNSATGYRQSPD CCCCCCCCCCCCCCC	34.27	23898821
95	Phosphorylation	LRNSATGYRQSPDGA CCCCCCCCCCCCCCC	10.92	26434776
98	Phosphorylation	SATGYRQSPDGACSV CCCCCCCCCCCCCCC	18.89	27732954
103	S-palmitoylation	RQSPDGACSVPSART CCCCCCCCCCCCHHH	5.28	29575903
145	N-linked_Glycosylation	KEGCHKKNQSIGLIQ CCCCCCCCCCCCEEE	45.71	UniProtKB CARBOHYD
159	Ubiquitination	QPFATNGKLFPWAQI ECCCCCCCEECCCEE	49.37	-
177	Phosphorylation	TAVVPLRYELSLHPN CEEEEEEEEEEECCC	28.98	-
184	N-linked_Glycosylation	YELSLHPNLTSMTFR EEEEECCCCCCEEEE	45.24	19349973
184	N-linked_Glycosylation	YELSLHPNLTSMTFR EEEEECCCCCCEEEE	45.24	19349973
215	N-linked_Glycosylation	ILHSTGHNISRVTFM EEECCCCCHHHHEEH	34.96	UniProtKB CARBOHYD
226	Phosphorylation	VTFMSAVSSQEKQAE HEEHHHCCCHHHHHH	26.48	29083192
227	Phosphorylation	TFMSAVSSQEKQAEI EEHHHCCCHHHHHHH	35.44	29083192
256	N-linked_Glycosylation	EALLAGHNYTLKIEY HHHHCCCCEEEEEEE	30.48	19349973
256	N-linked_Glycosylation	EALLAGHNYTLKIEY HHHHCCCCEEEEEEE	30.48	UniProtKB CARBOHYD
266	N-linked_Glycosylation	LKIEYSANISSSYYG EEEEEEECCCCCCCE	28.83	UniProtKB CARBOHYD
269	Phosphorylation	EYSANISSSYYGFYG EEEECCCCCCCEECE	20.68	22468782
271	Phosphorylation	SANISSSYYGFYGFS EECCCCCCCEECEEE	15.00	22468782
280	Phosphorylation	GFYGFSYTDESNEKK EECEEEEECCCCCEE	31.90	22468782
287	Ubiquitination	TDESNEKKYFAATQF ECCCCCEEEEEEEEC	39.15	-
319	Ubiquitination	KATFIIKIIRDEQYT EEEEEEEEECCHHHH	1.89	29967540
320	Ubiquitination	ATFIIKIIRDEQYTA EEEEEEEECCHHHHH	3.74	29967540
325	Phosphorylation	KIIRDEQYTALSNMP EEECCHHHHHHCCCC	7.61	29978859
326	Phosphorylation	IIRDEQYTALSNMPK EECCHHHHHHCCCCC	22.33	29978859
329	Phosphorylation	DEQYTALSNMPKKSS CHHHHHHCCCCCCCE	28.72	29978859
333	Ubiquitination	TALSNMPKKSSVVLD HHHCCCCCCCEEEEC	55.29	29967540
334	Ubiquitination	ALSNMPKKSSVVLDD HHCCCCCCCEEEECC	41.93	29967540
335	Phosphorylation	LSNMPKKSSVVLDDG HCCCCCCCEEEECCC	34.20	20068231
336	Phosphorylation	SNMPKKSSVVLDDGL CCCCCCCEEEECCCC	25.73	20068231
368	N-linked_Glycosylation	FIVGEMKNLSQDVNG HHHHHHHCCCCCCCC	43.55	UniProtKB CARBOHYD
374	N-linked_Glycosylation	KNLSQDVNGTLVSIY HCCCCCCCCCEEEEE	46.12	UniProtKB CARBOHYD
442	Phosphorylation	LLTFREETLLYDSNT EEEEEEEEEECCCCC	19.81	22210691
448	N-linked_Glycosylation	ETLLYDSNTSSMADR EEEECCCCCCCHHCH	40.87	19349973
448	N-linked_Glycosylation	ETLLYDSNTSSMADR EEEECCCCCCCHHCH	40.87	19349973
491	Phosphorylation	WLNEGFATFMEYFSL HHHHHHHHHHHHHCH	22.66	22468782
495	Phosphorylation	GFATFMEYFSLEKIF HHHHHHHHHCHHHHH	6.15	22468782
497	Phosphorylation	ATFMEYFSLEKIFKE HHHHHHHCHHHHHHH	34.42	22468782
506	Phosphorylation	EKIFKELSSYEDFLD HHHHHHHHCHHHHHH	31.78	-
508	Phosphorylation	IFKELSSYEDFLDAR HHHHHHCHHHHHHHH	19.01	-
518	Phosphorylation	FLDARFKTMKKDSLN HHHHHHHHHCHHHCC	31.35	26074081
523	Phosphorylation	FKTMKKDSLNSSHPI HHHHCHHHCCCCCCC	38.03	26074081
525	N-linked_Glycosylation	TMKKDSLNSSHPISS HHCHHHCCCCCCCCH	45.47	19349973
525	N-linked_Glycosylation	TMKKDSLNSSHPISS HHCHHHCCCCCCCCH	45.47	UniProtKB CARBOHYD
526	Phosphorylation	MKKDSLNSSHPISSS HCHHHCCCCCCCCHH	35.00	26074081
527	Phosphorylation	KKDSLNSSHPISSSV CHHHCCCCCCCCHHC	32.01	26074081
531	Phosphorylation	LNSSHPISSSVQSSE CCCCCCCCHHCCCHH	22.47	26074081
532	Phosphorylation	NSSHPISSSVQSSEQ CCCCCCCHHCCCHHH	34.94	26074081
533	Phosphorylation	SSHPISSSVQSSEQI CCCCCCHHCCCHHHH	19.86	26074081
536	Phosphorylation	PISSSVQSSEQIEEM CCCHHCCCHHHHHHH	33.42	26074081
537	Phosphorylation	ISSSVQSSEQIEEMF CCHHCCCHHHHHHHH	19.21	26074081
578	N-linked_Glycosylation	AVVLYLHNHSYASIQ HHHHHHCCCCCEECC	24.17	UniProtKB CARBOHYD
598	N-linked_Glycosylation	DSFNEVTNQTLDVKR HHHHHHHHCHHCHHH	37.71	UniProtKB CARBOHYD
598	N-linked_Glycosylation	DSFNEVTNQTLDVKR HHHHHHHHCHHCHHH	37.71	19349973
608	Ubiquitination	LDVKRMMKTWTLQKG HCHHHHHHHHEECCC	31.41	-
609	Phosphorylation	DVKRMMKTWTLQKGF CHHHHHHHHEECCCC	13.04	29759185
611	Phosphorylation	KRMMKTWTLQKGFPL HHHHHHHEECCCCCE	25.25	29759185
626	Ubiquitination	VTVQKKGKELFIQQE EEEEECCCEEEEEEE	61.19	-
664	N-linked_Glycosylation	SYVTEGRNYSKYQSV HHCCCCCCCCCCEEE	57.18	UniProtKB CARBOHYD
665	Phosphorylation	YVTEGRNYSKYQSVS HCCCCCCCCCCEEEE	12.74	29978859
666	Phosphorylation	VTEGRNYSKYQSVSL CCCCCCCCCCEEEEE	28.56	29978859
668	Phosphorylation	EGRNYSKYQSVSLLD CCCCCCCCEEEEEEE	10.48	29978859
670	Phosphorylation	RNYSKYQSVSLLDKK CCCCCCEEEEEEECC	15.58	29978859
672	Phosphorylation	YSKYQSVSLLDKKSG CCCCEEEEEEECCCC	28.58	29978859
676	2-Hydroxyisobutyrylation	QSVSLLDKKSGVINL EEEEEEECCCCCEEC	49.13	-
678	Phosphorylation	VSLLDKKSGVINLTE EEEEECCCCCEECCC	43.99	-
682	N-linked_Glycosylation	DKKSGVINLTEEVLW ECCCCCEECCCEEEE	38.20	17660510
682	N-linked_Glycosylation	DKKSGVINLTEEVLW ECCCCCEECCCEEEE	38.20	19349973
691	Acetylation	TEEVLWVKVNINMNG CCEEEEEEEEECCCC	20.27	12655749
758	N-linked_Glycosylation	DLINYLGNENHTAPI HHHHHHCCCCCCCCH	44.28	19349973
760	N-linked_Glycosylation	INYLGNENHTAPITE HHHHCCCCCCCCHHH	41.64	UniProtKB CARBOHYD
760	N-linked_Glycosylation	INYLGNENHTAPITE HHHHCCCCCCCCHHH	41.64	19349973
784	Phosphorylation	NLLEKLGYMDLASRL HHHHHCCCCHHHHHH	9.63	-
789	Phosphorylation	LGYMDLASRLVTRVF CCCCHHHHHHHHHHH	33.18	-
821	Phosphorylation	PSMRELRSALLEFAC CCHHHHHHHHHHHHH	35.57	27050516
834	N-linked_Glycosylation	ACTHNLGNCSTTAMK HHHCCCCCCCHHHHH	21.52	UniProtKB CARBOHYD
850	N-linked_Glycosylation	FDDWMASNGTQSLPT HHHHHHHCCCCCCCC	48.25	19349973
850	N-linked_Glycosylation	FDDWMASNGTQSLPT HHHHHHHCCCCCCCC	48.25	19349973
881	Phosphorylation	WSFLLGKYISIGSEA HHHHHHCEEECCCHH	9.71	22985185
886	Phosphorylation	GKYISIGSEAEKNKI HCEEECCCHHHHHHH	31.78	-
904	Methylation	LASSEDVRKLYWLMK HHCCHHHHHHHHHHH	35.27	115480467
921	Phosphorylation	LNGDNFRTQKLSFII CCCCCHHHHHHHHHH	26.39	27134283
960	Phosphorylation	VQKFPLGSYTIQNIV HHHCCCCCCEEEEHH	27.13	22210691
962	Phosphorylation	KFPLGSYTIQNIVAG HCCCCCCEEEEHHCC	20.13	22210691
970	Phosphorylation	IQNIVAGSTYLFSTK EEEHHCCCEEEEECC	12.25	22210691
989	N-linked_Glycosylation	EVQAFFENQSEATFR HHHHHHCCCCHHHHH	45.59	UniProtKB CARBOHYD

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 LCAP_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LCAP_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 LCAP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FHOD1_HUMAN	FHOD1	physical	12677009
TNKS2_HUMAN	TNKS2	physical	12080061
TNKS2_HUMAN	TNKS2	physical	10988299
TNKS1_HUMAN	TNKS	physical	11802774
TNKS2_HUMAN	TNKS2	physical	11802774
PRDX3_HUMAN	PRDX3	physical	22863883
REL_HUMAN	REL	physical	25416956
ITF2_HUMAN	TCF4	physical	25416956
FATE1_HUMAN	FATE1	physical	25416956
CALX_HUMAN	CANX	physical	26496610
RNC_HUMAN	DROSHA	physical	26496610
NDUAD_HUMAN	NDUFA13	physical	26496610
HEAT3_HUMAN	HEATR3	physical	26496610
GCC1_HUMAN	GCC1	physical	26496610
TM263_HUMAN	TMEM263	physical	26496610

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 LCAP_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184; ASN-448; ASN-682 ANDASN-850, AND MASS SPECTROMETRY.	19349973 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-70, AND MASSSPECTROMETRY.	17389395 [Abstract]