CBPA6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CBPA6_HUMAN
• UniProt AC: Q8N4T0
• Protein Name: Carboxypeptidase A6
• Gene Name: CPA6
• Organism: Homo sapiens (Human).
• Sequence Length: 437
• Subcellular Localization: Secreted, extracellular space, extracellular matrix .
• Protein Description: May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II. [PubMed: 18178555 Releases a C-terminal amino acid, with preference for large hydrophobic C-terminal amino acids and shows only very weak activity toward small amino acids and histidine]
• Protein Sequence: MKCLGKRRGQAAAFLPLCWLFLKILQPGHSHLYNNRYAGDKVIRFIPKTEEEAYALKKISYQLKVDLWQPSSISYVSEGTVTDVHIPQNGSRALLAFLQEANIQYKVLIEDLQKTLEKGSSLHTQRNRRSLSGYNYEVYHSLEEIQNWMHHLNKTHSGLIHMFSIGRSYEGRSLFILKLGRRSRLKRAVWIDCGIHAREWIGPAFCQWFVKEALLTYKSDPAMRKMLNHLYFYIMPVFNVDGYHFSWTNDRFWRKTRSRNSRFRCRGVDANRNWKVKWCDEGASMHPCDDTYCGPFPESEPEVKAVANFLRKHRKHIRAYLSFHAYAQMLLYPYSYKYATIPNFRCVESAAYKAVNALQSVYGVRYRYGPASTTLYVSSGSSMDWAYKNGIPYAFAFELRDTGYFGFLLPEMLIKPTCTETMLAVKNITMHLLKKCP

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
60	Phosphorylation	AYALKKISYQLKVDL HHHHHHCCEEEEEEE	18.73	28188228
61	Phosphorylation	YALKKISYQLKVDLW HHHHHCCEEEEEEEE	22.72	28674151
89	N-linked_Glycosylation	TDVHIPQNGSRALLA EEEECCCCCHHHHHH	45.08	UniProtKB CARBOHYD
129 (in isoform 3)	Ubiquitination	-	45.56	-
144 (in isoform 3)	Ubiquitination	-	55.99	-
153	N-linked_Glycosylation	QNWMHHLNKTHSGLI HHHHHHHCCCCCCEE	42.71	UniProtKB CARBOHYD
216	Phosphorylation	FVKEALLTYKSDPAM HHHHHHHHCCCCHHH	29.74	19413330
326	Phosphorylation	AYLSFHAYAQMLLYP HHHHHHHHHHHHHHC	6.70	22817900
334	Phosphorylation	AQMLLYPYSYKYATI HHHHHHCCCCCCCCC	15.86	22817900
336	Phosphorylation	MLLYPYSYKYATIPN HHHHCCCCCCCCCCC	11.37	22817900
349	Phosphorylation	PNFRCVESAAYKAVN CCCCCHHHHHHHHHH	9.59	29083192
352	Phosphorylation	RCVESAAYKAVNALQ CCHHHHHHHHHHHHH	10.13	29083192
360	Phosphorylation	KAVNALQSVYGVRYR HHHHHHHHHHCCEEE	20.39	29083192
362	Phosphorylation	VNALQSVYGVRYRYG HHHHHHHHCCEEEEC	18.36	29083192
366	Phosphorylation	QSVYGVRYRYGPAST HHHHCCEEEECCCCE	13.04	29083192
368	Phosphorylation	VYGVRYRYGPASTTL HHCCEEEECCCCEEE	20.66	22817900
376	Phosphorylation	GPASTTLYVSSGSSM CCCCEEEEECCCCCH	9.01	22817900
387	Phosphorylation	GSSMDWAYKNGIPYA CCCHHHHHHCCCCEE	10.75	22817900
388	Ubiquitination	SSMDWAYKNGIPYAF CCHHHHHHCCCCEEE	40.73	-
419	Phosphorylation	MLIKPTCTETMLAVK HHCCCCCHHHHHHHH	36.65	29759185
421	Phosphorylation	IKPTCTETMLAVKNI CCCCCHHHHHHHHHH	10.18	29759185
427	N-linked_Glycosylation	ETMLAVKNITMHLLK HHHHHHHHHHHHHHH	28.50	UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CBPA6_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CBPA6_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CBPA6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZZEF1_HUMAN	ZZEF1	physical	28514442
AMER1_HUMAN	AMER1	physical	28514442
DICER_HUMAN	DICER1	physical	28514442
UBB_HUMAN	UBB	physical	28514442
PPM1G_HUMAN	PPM1G	physical	28514442
FNTB_HUMAN	FNTB	physical	28514442
HECD3_HUMAN	HECTD3	physical	28514442
TRBP2_HUMAN	TARBP2	physical	28514442
FUT11_HUMAN	FUT11	physical	28514442
PP6R1_HUMAN	PPP6R1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• : Note=A chromosomal aberration involving CPA6 was found in a patient with Duane retraction syndrome. Translocation t(6
• : 8)(q26
• : q13).
• 614417:
• 614418: Febrile seizures, familial, 11 (FEB11)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, AND MASSSPECTROMETRY.
PubMed: 19413330