dbPTM

CBPD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CBPD_HUMAN
UniProt AC	O75976
Protein Name	Carboxypeptidase D
Gene Name	CPD
Organism	Homo sapiens (Human).
Sequence Length	1380
Subcellular Localization	Cell membrane Single-pass type I membrane protein .
Protein Description
Protein Sequence	MASGRDERPPWRLGRLLLLMCLLLLGSSARAAHIKKAEATTTTTSAGAEAAEGQFDRYYHEEELESALREAAAAGLPGLARLFSIGRSVEGRPLWVLRLTAGLGSLIPEGDAGPDAAGPDAAGPLLPGRPQVKLVGNMHGDETVSRQVLIYLARELAAGYRRGDPRLVRLLNTTDVYLLPSLNPDGFERAREGDCGFGDGGPSGASGRDNSRGRDLNRSFPDQFSTGEPPALDEVPEVRALIEWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKATGIYSKTSDDEVFKYLAKAYASNHPIMKTGEPHCPGDEDETFKDGITNGAHWYDVEGGMQDYNYVWANCFEITLELSCCKYPPASQLRQEWENNRESLITLIEKVHIGVKGFVKDSITGSGLENATISVAGINHNITTGRFGDFYRLLVPGTYNLTVVLTGYMPLTVTNVVVKEGPATEVDFSLRPTVTSVIPDTTEAVSTASTVAIPNILSGTSSSYQPIQPKDFHHHHFPDMEIFLRRFANEYPNITRLYSLGKSVESRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVHNTRIHLMPSMNPDGYEKSQEGDSISVIGRNNSNNFDLNRNFPDQFVQITDPTQPETIAVMSWMKSYPFVLSANLHGGSLVVNYPFDDDEQGLATYSKSPDDAVFQQIALSYSKENSQMFQGRPCKNMYPNEYFPHGITNGASWYNVPGGMQDWNYLQTNCFEVTIELGCVKYPLEKELPNFWEQNRRSLIQFMKQVHQGVRGFVLDATDGRGILNATISVAEINHPVTTYKTGDYWRLLVPGTYKITASARGYNPVTKNVTVKSEGAIQVNFTLVRSSTDSNNESKKGKGASSSTNDASDPTTKEFETLIKDLSAENGLESLMLRSSSNLALALYRYHSYKDLSEFLRGLVMNYPHITNLTNLGQSTEYRHIWSLEISNKPNVSEPEEPKIRFVAGIHGNAPVGTELLLALAEFLCLNYKKNPAVTQLVDRTRIVIVPSLNPDGRERAQEKDCTSKIGQTNARGKDLDTDFTNNASQPETKAIIENLIQKQDFSLSVALDGGSMLVTYPYDKPVQTVENKETLKHLASLYANNHPSMHMGQPSCPNKSDENIPGGVMRGAEWHSHLGSMKDYSVTYGHCPEITVYTSCCYFPSAARLPSLWADNKRSLLSMLVEVHKGVHGFVKDKTGKPISKAVIVLNEGIKVQTKEGGYFHVLLAPGVHNIIAIADGYQQQHSQVFVHHDAASSVVIVFDTDNRIFGLPRELVVTVSGATMSALILTACIIWCICSIKSNRHKDGFHRLRQHHDEYEDEIRMMSTGSKKSLLSHEFQDETDTEEETLYSSKH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
27	Phosphorylation	MCLLLLGSSARAAHI HHHHHHCHHHHHHHH	22.31	-
34	Ubiquitination	SSARAAHIKKAEATT HHHHHHHHHHHHCEE	4.14	29967540
40	O-linked_Glycosylation	HIKKAEATTTTTSAG HHHHHHCEEEECCHH	19.04	55824767
41	O-linked_Glycosylation	IKKAEATTTTTSAGA HHHHHCEEEECCHHH	29.23	55824773
41	Phosphorylation	IKKAEATTTTTSAGA HHHHHCEEEECCHHH	29.23	30576142
42	O-linked_Glycosylation	KKAEATTTTTSAGAE HHHHCEEEECCHHHH	24.58	55824779
42	Ubiquitination	KKAEATTTTTSAGAE HHHHCEEEECCHHHH	24.58	29967540
43	O-linked_Glycosylation	KAEATTTTTSAGAEA HHHCEEEECCHHHHH	19.36	55824785
44	O-linked_Glycosylation	AEATTTTTSAGAEAA HHCEEEECCHHHHHH	17.94	55824791
44	Phosphorylation	AEATTTTTSAGAEAA HHCEEEECCHHHHHH	17.94	30576142
45	O-linked_Glycosylation	EATTTTTSAGAEAAE HCEEEECCHHHHHHC	23.71	55824795
46	Ubiquitination	ATTTTTSAGAEAAEG CEEEECCHHHHHHCC	21.08	29967540
66	Phosphorylation	YHEEELESALREAAA CCHHHHHHHHHHHHH	45.27	22167270
138	Sulfoxidation	QVKLVGNMHGDETVS EEEEECCCCCCHHHH	2.84	21406390
172	N-linked_Glycosylation	PRLVRLLNTTDVYLL HHHHHCCCCCCEEEE	45.59	12754519
172	N-linked_Glycosylation	PRLVRLLNTTDVYLL HHHHHCCCCCCEEEE	45.59	12754519
173	Phosphorylation	RLVRLLNTTDVYLLP HHHHCCCCCCEEEEC	25.09	29759185
174	Phosphorylation	LVRLLNTTDVYLLPS HHHCCCCCCEEEECC	23.53	29759185
203	Phosphorylation	GFGDGGPSGASGRDN CCCCCCCCCCCCCCC	50.71	-
217	N-linked_Glycosylation	NSRGRDLNRSFPDQF CCCCCCCCHHCCCCC	41.67	UniProtKB CARBOHYD
225	O-linked_Glycosylation	RSFPDQFSTGEPPAL HHCCCCCCCCCCCCC	29.84	OGP
226	O-linked_Glycosylation	SFPDQFSTGEPPALD HCCCCCCCCCCCCCC	47.02	OGP
265	Phosphorylation	GGSVVASYPFDDSPE CCCEEEECCCCCCCC	9.74	-
270	Phosphorylation	ASYPFDDSPEHKATG EECCCCCCCCCCCCC	33.75	-
281	Ubiquitination	KATGIYSKTSDDEVF CCCCCCCCCCHHHHH	34.77	29967540
282	Phosphorylation	ATGIYSKTSDDEVFK CCCCCCCCCHHHHHH	31.29	-
283	Phosphorylation	TGIYSKTSDDEVFKY CCCCCCCCHHHHHHH	46.96	-
289	Ubiquitination	TSDDEVFKYLAKAYA CCHHHHHHHHHHHHH	44.52	29967540
293	Ubiquitination	EVFKYLAKAYASNHP HHHHHHHHHHHHCCC	39.06	29967540
356	Phosphorylation	LELSCCKYPPASQLR EEEHHCCCCCHHHHH	10.67	-
375	Phosphorylation	NNRESLITLIEKVHI HCHHHHHHHHHHHCC	27.29	28060719
399	N-linked_Glycosylation	ITGSGLENATISVAG CCCCCCCCEEEEEEE	47.64	UniProtKB CARBOHYD
410	N-linked_Glycosylation	SVAGINHNITTGRFG EEEEECCCCCCCCCC	28.90	UniProtKB CARBOHYD
429	N-linked_Glycosylation	LLVPGTYNLTVVLTG EECCCEEEEEEEEEC	29.13	UniProtKB CARBOHYD
479	O-linked_Glycosylation	EAVSTASTVAIPNIL HHHHHCCEEECCCCC	16.11	OGP
489	O-linked_Glycosylation	IPNILSGTSSSYQPI CCCCCCCCCCCCCCC	23.27	55833643
520	Phosphorylation	LRRFANEYPNITRLY HHHHHHHCCCCCEEE	11.03	-
522	N-linked_Glycosylation	RFANEYPNITRLYSL HHHHHCCCCCEEEEC	47.57	UniProtKB CARBOHYD
527	Phosphorylation	YPNITRLYSLGKSVE CCCCCEEEECCCCHH	9.88	-
528	O-linked_Glycosylation	PNITRLYSLGKSVES CCCCEEEECCCCHHC	34.93	29351928
528	Phosphorylation	PNITRLYSLGKSVES CCCCEEEECCCCHHC	34.93	23898821
531	Ubiquitination	TRLYSLGKSVESREL CEEEECCCCHHCCEE	57.53	-
532	O-linked_Glycosylation	RLYSLGKSVESRELY EEEECCCCHHCCEEE	29.35	29351928
532	Phosphorylation	RLYSLGKSVESRELY EEEECCCCHHCCEEE	29.35	-
587	Phosphorylation	YLCKNFGTDPEVTDL HHHHHCCCCHHHHHH	44.22	-
607	Ubiquitination	IHLMPSMNPDGYEKS EEECCCCCCCCCCCC	35.53	32015554
611	Phosphorylation	PSMNPDGYEKSQEGD CCCCCCCCCCCCCCC	27.80	-
626	N-linked_Glycosylation	SISVIGRNNSNNFDL CEEEEECCCCCCCCC	51.58	UniProtKB CARBOHYD
653	Ubiquitination	DPTQPETIAVMSWMK CCCCHHHHHEEHHHH	2.31	29967540
679	Phosphorylation	GGSLVVNYPFDDDEQ CCEEEEECCCCCCCC	8.15	28787133
691	Phosphorylation	DEQGLATYSKSPDDA CCCCEEEECCCHHHH	14.43	28787133
692	O-linked_Glycosylation	EQGLATYSKSPDDAV CCCEEEECCCHHHHH	23.46	OGP
804	Phosphorylation	RGFVLDATDGRGILN CEEEEECCCCCCCEE	38.36	20068231
811	N-linked_Glycosylation	TDGRGILNATISVAE CCCCCCEEEEEEEEE	32.87	12754519
811	N-linked_Glycosylation	TDGRGILNATISVAE CCCCCCEEEEEEEEE	32.87	12754519
840	Phosphorylation	RLLVPGTYKITASAR EEEECCEEEEEEECC	13.30	20049867
845	Phosphorylation	GTYKITASARGYNPV CEEEEEEECCCCCCC	15.17	20049867
849	Phosphorylation	ITASARGYNPVTKNV EEEECCCCCCCCCCE	15.67	29083192
853	Phosphorylation	ARGYNPVTKNVTVKS CCCCCCCCCCEEEEE	20.40	29083192
854	Ubiquitination	RGYNPVTKNVTVKSE CCCCCCCCCEEEEEC	50.05	32015554
855	N-linked_Glycosylation	GYNPVTKNVTVKSEG CCCCCCCCEEEEECC	25.90	UniProtKB CARBOHYD
867	N-linked_Glycosylation	SEGAIQVNFTLVRSS ECCEEEEEEEEEECC	14.07	UniProtKB CARBOHYD
873	Phosphorylation	VNFTLVRSSTDSNNE EEEEEEECCCCCCCC	30.06	24144214
874	Phosphorylation	NFTLVRSSTDSNNES EEEEEECCCCCCCCC	26.18	24144214
875	Phosphorylation	FTLVRSSTDSNNESK EEEEECCCCCCCCCC	44.70	24144214
877	Phosphorylation	LVRSSTDSNNESKKG EEECCCCCCCCCCCC	41.46	24144214
879	N-linked_Glycosylation	RSSTDSNNESKKGKG ECCCCCCCCCCCCCC	59.89	UniProtKB CARBOHYD
881	Phosphorylation	STDSNNESKKGKGAS CCCCCCCCCCCCCCC	41.62	24144214
888	Phosphorylation	SKKGKGASSSTNDAS CCCCCCCCCCCCCCC	33.23	24144214
889	Phosphorylation	KKGKGASSSTNDASD CCCCCCCCCCCCCCC	40.42	24144214
890	Phosphorylation	KGKGASSSTNDASDP CCCCCCCCCCCCCCC	28.83	24144214
891	Phosphorylation	GKGASSSTNDASDPT CCCCCCCCCCCCCCC	38.78	24144214
895	Phosphorylation	SSSTNDASDPTTKEF CCCCCCCCCCCHHHH	47.16	24144214
898	Phosphorylation	TNDASDPTTKEFETL CCCCCCCCHHHHHHH	56.33	-
899	Phosphorylation	NDASDPTTKEFETLI CCCCCCCHHHHHHHH	33.68	-
900	Ubiquitination	DASDPTTKEFETLIK CCCCCCHHHHHHHHH	63.98	29967540
904	Phosphorylation	PTTKEFETLIKDLSA CCHHHHHHHHHHHHH	38.82	-
910	Phosphorylation	ETLIKDLSAENGLES HHHHHHHHHHCCHHH	43.61	-
933	Phosphorylation	LALALYRYHSYKDLS HHHHHHHHCCHHCHH	4.99	30576142
935	Phosphorylation	LALYRYHSYKDLSEF HHHHHHCCHHCHHHH	25.58	30576142
936	Phosphorylation	ALYRYHSYKDLSEFL HHHHHCCHHCHHHHH	8.66	30576142
940	Phosphorylation	YHSYKDLSEFLRGLV HCCHHCHHHHHHHHH	36.11	23403867
950	Phosphorylation	LRGLVMNYPHITNLT HHHHHHHCCCHHCCC	4.33	22210691
955	N-linked_Glycosylation	MNYPHITNLTNLGQS HHCCCHHCCCCCCCC	44.24	12754519
955	N-linked_Glycosylation	MNYPHITNLTNLGQS HHCCCHHCCCCCCCC	44.24	12754519
957	Phosphorylation	YPHITNLTNLGQSTE CCCHHCCCCCCCCCC	30.39	22210691
973	Ubiquitination	RHIWSLEISNKPNVS EEEEEEEECCCCCCC	7.16	29967540
978	N-linked_Glycosylation	LEISNKPNVSEPEEP EEECCCCCCCCCCCC	52.11	UniProtKB CARBOHYD
1027	Methylation	AVTQLVDRTRIVIVP HHHHCCCCCEEEEEC	20.58	-
1035	Phosphorylation	TRIVIVPSLNPDGRE CEEEEECCCCCCHHH	29.86	23312004
1050	Phosphorylation	RAQEKDCTSKIGQTN HHHHCCCCCHHCCCC	43.09	21406692
1051	Phosphorylation	AQEKDCTSKIGQTNA HHHCCCCCHHCCCCC	28.71	21406692
1056	Phosphorylation	CTSKIGQTNARGKDL CCCHHCCCCCCCCCC	26.15	21406692
1070	N-linked_Glycosylation	LDTDFTNNASQPETK CCCCCCCCCCCHHHH	37.60	19159218
1109	Ubiquitination	VTYPYDKPVQTVENK EEECCCCCCCEECCH	22.13	33845483
1110	Ubiquitination	TYPYDKPVQTVENKE EECCCCCCCEECCHH	10.31	32015554
1121	Phosphorylation	ENKETLKHLASLYAN CCHHHHHHHHHHHHC	29.73	32142685
1123	Phosphorylation	KETLKHLASLYANNH HHHHHHHHHHHHCCC	9.37	32645325
1132	Ubiquitination	LYANNHPSMHMGQPS HHHCCCCCCCCCCCC	17.48	21963094
1142	N-linked_Glycosylation	MGQPSCPNKSDENIP CCCCCCCCCCCCCCC	61.87	UniProtKB CARBOHYD
1220	Ubiquitination	KGVHGFVKDKTGKPI HCCCEECCCCCCCCC	51.77	29967540
1317	S-palmitoylation	SALILTACIIWCICS HHHHHHHHHHHHHHH	1.63	12643288
1321	S-palmitoylation	LTACIIWCICSIKSN HHHHHHHHHHHHHCC	1.26	12643288
1323	S-palmitoylation	ACIIWCICSIKSNRH HHHHHHHHHHHCCCC	2.89	12643288
1324	Phosphorylation	CIIWCICSIKSNRHK HHHHHHHHHHCCCCC	17.09	-
1331	Ubiquitination	SIKSNRHKDGFHRLR HHHCCCCCCCHHHHH	57.20	-
1344	Phosphorylation	LRQHHDEYEDEIRMM HHHCCHHHHHHHHCC	34.44	21082442
1352	Phosphorylation	EDEIRMMSTGSKKSL HHHHHCCCCCCHHHH	21.92	23312004
1353	Phosphorylation	DEIRMMSTGSKKSLL HHHHCCCCCCHHHHH	27.81	25072903
1355	Phosphorylation	IRMMSTGSKKSLLSH HHCCCCCCHHHHHCC	36.68	27422710
1356	2-Hydroxyisobutyrylation	RMMSTGSKKSLLSHE HCCCCCCHHHHHCCC	47.96	-
1356	Ubiquitination	RMMSTGSKKSLLSHE HCCCCCCHHHHHCCC	47.96	33845483
1357	Ubiquitination	MMSTGSKKSLLSHEF CCCCCCHHHHHCCCC	48.29	32015554
1358	Phosphorylation	MSTGSKKSLLSHEFQ CCCCCHHHHHCCCCC	37.98	23927012
1361	Phosphorylation	GSKKSLLSHEFQDET CCHHHHHCCCCCCCC	26.68	23927012
1368	Phosphorylation	SHEFQDETDTEEETL CCCCCCCCCCCCHHH	57.41	23927012
1370	Phosphorylation	EFQDETDTEEETLYS CCCCCCCCCCHHHHC	53.36	23927012
1374	Phosphorylation	ETDTEEETLYSSKH- CCCCCCHHHHCCCC-	33.99	30266825
1376	Phosphorylation	DTEEETLYSSKH--- CCCCHHHHCCCC---	20.51	23927012
1377	Phosphorylation	TEEETLYSSKH---- CCCHHHHCCCC----	35.70	23927012
1378	Phosphorylation	EEETLYSSKH----- CCHHHHCCCC-----	22.61	23927012
1379	Ubiquitination	EETLYSSKH------ CHHHHCCCC------	47.60	21963094

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 CBPD_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ECM29_HUMAN	KIAA0368	physical	20682791
UFSP2_HUMAN	UFSP2	physical	28514442
FOXK2_HUMAN	FOXK2	physical	28514442
AP1M1_HUMAN	AP1M1	physical	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 CBPD_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-811; ASN-955 AND ASN-1070,AND MASS SPECTROMETRY.	19159218 [Abstract]
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry."; Zhang H., Li X.-J., Martin D.B., Aebersold R.; Nat. Biotechnol. 21:660-666(2003). Cited for: GLYCOSYLATION AT ASN-172; ASN-811 AND ASN-955.	12754519 [Abstract]
Palmitoylation
Reference	PubMed
"Palmitoylation of carboxypeptidase D. Implications for intracellulartrafficking."; Kalinina E.V., Fricker L.D.; J. Biol. Chem. 278:9244-9249(2003). Cited for: PALMITOYLATION AT CYS-1317; CYS-1321 AND CYS-1323.	12643288 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1358; SER-1361; THR-1368AND THR-1370, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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 THR-1368 AND THR-1370, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1344 AND TYR-1376, ANDMASS SPECTROMETRY.	18083107 [Abstract]