dbPTM

CATD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CATD_HUMAN
UniProt AC	P07339
Protein Name	Cathepsin D
Gene Name	CTSD
Organism	Homo sapiens (Human).
Sequence Length	412
Subcellular Localization	Lysosome. Melanosome. Secreted, extracellular space. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. In aortic samples, detected as an extracellular protein loosely bound to the matrix (PubMed:20551380).
Protein Description	Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. [PubMed: 27333034 Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.]
Protein Sequence	MQPSSLLPLALCLLAAPASALVRIPLHKFTSIRRTMSEVGGSVEDLIAKGPVSKYSQAVPAVTEGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQSASSASALGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNRVGFAEAARL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MQPSSLLPLAL ----CCHHHHHHHHH	19.41	24043423
5	Phosphorylation	---MQPSSLLPLALC ---CCHHHHHHHHHH	40.38	24043423
19	Phosphorylation	CLLAAPASALVRIPL HHHHCCHHHHHHCCH	22.52	24043423
28	Ubiquitination	LVRIPLHKFTSIRRT HHHCCHHHHHHHHHH	59.00	21890473
30	Phosphorylation	RIPLHKFTSIRRTMS HCCHHHHHHHHHHHH	28.22	23909892
31	Phosphorylation	IPLHKFTSIRRTMSE CCHHHHHHHHHHHHH	19.75	29496963
35	Phosphorylation	KFTSIRRTMSEVGGS HHHHHHHHHHHCCCC	18.39	21406692
37	Phosphorylation	TSIRRTMSEVGGSVE HHHHHHHHHCCCCHH	28.63	21406692
42	Phosphorylation	TMSEVGGSVEDLIAK HHHHCCCCHHHHHHC	19.19	20068231
49	Ubiquitination	SVEDLIAKGPVSKYS CHHHHHHCCCCHHHC	57.67	-
53	Phosphorylation	LIAKGPVSKYSQAVP HHHCCCCHHHCCCCC	29.07	29116813
54	Ubiquitination	IAKGPVSKYSQAVPA HHCCCCHHHCCCCCC	49.51	21890473
56	Phosphorylation	KGPVSKYSQAVPAVT CCCCHHHCCCCCCCC	18.52	29116813
63	O-linked_Glycosylation	SQAVPAVTEGPIPEV CCCCCCCCCCCCHHH	37.01	55825339
63	Phosphorylation	SQAVPAVTEGPIPEV CCCCCCCCCCCCHHH	37.01	29116813
122	2-Hydroxyisobutyrylation	IACWIHHKYNSDKSS HHHHHHHHCCCCCCC	31.78	-
127	2-Hydroxyisobutyrylation	HHKYNSDKSSTYVKN HHHCCCCCCCEEEEC	46.24	-
127	Ubiquitination	HHKYNSDKSSTYVKN HHHCCCCCCCEEEEC	46.24	-
134	N-linked_Glycosylation	KSSTYVKNGTSFDIH CCCEEEECCEEEEEE	49.26	8393577
134	N-linked_Glycosylation	KSSTYVKNGTSFDIH CCCEEEECCEEEEEE	49.26	8393577
165	O-linked_Glycosylation	VPCQSASSASALGGV CCCCCCCCCHHHCCC	26.42	OGP
184	Ubiquitination	QVFGEATKQPGITFI EECCCCCCCCCEEEE	62.64	21890473
203	Phosphorylation	DGILGMAYPRISVNN CCCCCCCCCEEECCC	5.55	25599653
219	Sulfoxidation	LPVFDNLMQQKLVDQ HHHHHHHHHHHCCCC	5.07	28465586
230	Phosphorylation	LVDQNIFSFYLSRDP CCCCCCHHEECCCCC	14.80	25867546
232	Phosphorylation	DQNIFSFYLSRDPDA CCCCHHEECCCCCCC	11.54	25867546
234	Phosphorylation	NIFSFYLSRDPDAQP CCHHEECCCCCCCCC	24.21	25867546
246	Sulfoxidation	AQPGGELMLGGTDSK CCCCCEEECCCCCCC	2.58	28465586
250	Phosphorylation	GELMLGGTDSKYYKG CEEECCCCCCCCCCC	34.99	23911959
252	Phosphorylation	LMLGGTDSKYYKGSL EECCCCCCCCCCCCE	23.54	23911959
253	2-Hydroxyisobutyrylation	MLGGTDSKYYKGSLS ECCCCCCCCCCCCEE	56.24	-
253	Ubiquitination	MLGGTDSKYYKGSLS ECCCCCCCCCCCCEE	56.24	21890473
254	Phosphorylation	LGGTDSKYYKGSLSY CCCCCCCCCCCCEEE	17.86	25219547
255	Phosphorylation	GGTDSKYYKGSLSYL CCCCCCCCCCCEEEE	16.77	25219547
258	Phosphorylation	DSKYYKGSLSYLNVT CCCCCCCCEEEEEEC	15.25	25219547
260	Phosphorylation	KYYKGSLSYLNVTRK CCCCCCEEEEEECCC	29.31	28060719
261	Phosphorylation	YYKGSLSYLNVTRKA CCCCCEEEEEECCCE	13.95	28060719
263	N-linked_Glycosylation	KGSLSYLNVTRKAYW CCCEEEEEECCCEEE	25.53	8393577
263	N-linked_Glycosylation	KGSLSYLNVTRKAYW CCCEEEEEECCCEEE	25.53	8393577
265	Phosphorylation	SLSYLNVTRKAYWQV CEEEEEECCCEEEEE	25.94	28060719
269	Phosphorylation	LNVTRKAYWQVHLDQ EEECCCEEEEEEHHH	10.21	25219547
301	Sulfoxidation	VDTGTSLMVGPVDEV EECCCCEEEECHHHH	3.07	30846556
313	Ubiquitination	DEVRELQKAIGAVPL HHHHHHHHHHCCCCE	55.38	-
325	Phosphorylation	VPLIQGEYMIPCEKV CCEECCEEEEECCCC	13.73	-
326	Sulfoxidation	PLIQGEYMIPCEKVS CEECCEEEEECCCCC	2.10	28465586
329	Glutathionylation	QGEYMIPCEKVSTLP CCEEEEECCCCCCCC	5.67	22555962
331	Ubiquitination	EYMIPCEKVSTLPAI EEEEECCCCCCCCEE	48.48	-
333	Phosphorylation	MIPCEKVSTLPAITL EEECCCCCCCCEEEE	34.98	23911959
334	Phosphorylation	IPCEKVSTLPAITLK EECCCCCCCCEEEEE	39.48	23911959
339	Phosphorylation	VSTLPAITLKLGGKG CCCCCEEEEEECCCC	21.68	20071362
341	Ubiquitination	TLPAITLKLGGKGYK CCCEEEEEECCCCEE	36.11	-
341	Malonylation	TLPAITLKLGGKGYK CCCEEEEEECCCCEE	36.11	30639696
347	Phosphorylation	LKLGGKGYKLSPEDY EEECCCCEECCHHHE	16.55	-
348	Ubiquitination	KLGGKGYKLSPEDYT EECCCCEECCHHHEE	51.67	21890473
354	Phosphorylation	YKLSPEDYTLKVSQA EECCHHHEEEEEECC	16.59	-
357	Ubiquitination	SPEDYTLKVSQAGKT CHHHEEEEEECCCCE	31.85	-
359	Phosphorylation	EDYTLKVSQAGKTLC HHEEEEEECCCCEEE	16.84	24247654
394	Phosphorylation	DVFIGRYYTVFDRDN CEEEECEEEEEECCC	8.62	-

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 CATD_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPGB_HUMAN	CTSA	physical	22939629
ACADM_HUMAN	ACADM	physical	26344197
ETFA_HUMAN	ETFA	physical	26344197
GRHPR_HUMAN	GRHPR	physical	26344197
ENPL_HUMAN	HSP90B1	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
RAB5A_HUMAN	RAB5A	physical	26344197
SCNNG_HUMAN	SCNN1G	physical	26344197
SCYL2_HUMAN	SCYL2	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
SYUA_HUMAN	SNCA	physical	25617759

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610127	Ceroid lipofuscinosis, neuronal, 10 (CLN10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CATD_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structures of native and inhibited forms of human cathepsinD: implications for lysosomal targeting and drug design."; Baldwin E.T., Bhat T.N., Gulnik S., Hosur M.V., Sowder R.C. II,Cachau R.E., Collins J., Silva A.M., Erickson J.W.; Proc. Natl. Acad. Sci. U.S.A. 90:6796-6800(1993). Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).	8393577 [Abstract]
"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-134 AND ASN-263, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-263, AND MASSSPECTROMETRY.	16263699 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-263, AND MASSSPECTROMETRY.	16335952 [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-263.	12754519 [Abstract]