PPA5_HUMAN - dbPTM
PPA5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPA5_HUMAN
UniProt AC P13686
Protein Name Tartrate-resistant acid phosphatase type 5
Gene Name ACP5
Organism Homo sapiens (Human).
Sequence Length 325
Subcellular Localization Lysosome.
Protein Description Involved in osteopontin/bone sialoprotein dephosphorylation. Its expression seems to increase in certain pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias..
Protein Sequence MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQILGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQIAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKLARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSKEMTVTYIEASGKSLFKTRLPRRARP
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
44PhosphorylationVPNAPFHTAREMANA
CCCCCHHHHHHHHCH
27.9929083192
116N-linked_GlycosylationGNHDHLGNVSAQIAY
CCCCCCCCHHHHHHH
30.8115993892
147N-linked_GlycosylationHFKIPQTNVSVAIFM
EEECCCCCCEEEEEE
20.86UniProtKB CARBOHYD
222UbiquitinationGPTHCLVKQLRPLLA
CCCCCHHHHHHHHHH
30.57-
278PhosphorylationQRKVPNGYLRFHYGT
CCCCCCCEEEEEECC
11.018278711
283PhosphorylationNGYLRFHYGTEDSLG
CCEEEEEECCCCCCC
24.038278721
306PhosphorylationSKEMTVTYIEASGKS
CCEEEEEEEEECCCC
7.7622210691
313PhosphorylationYIEASGKSLFKTRLP
EEEECCCCHHHCCCC
42.4324719451

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 PPA5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPA5_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 PPA5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
S35F6_HUMANSLC35F6physical
16169070
GRP78_HUMANHSPA5physical
26186194
KLH15_HUMANKLHL15physical
26186194
CIZ1_HUMANCIZ1physical
26186194
PPA5_HUMANACP5physical
27432908
CALR_HUMANCALRphysical
27432908
SEP15_HUMANSEP15physical
27432908
UGGG1_HUMANUGGT1physical
27432908
CLGN_HUMANCLGNphysical
27432908
COA7_HUMANCOA7physical
27432908
OS9_HUMANOS9physical
27432908
PDIA3_HUMANPDIA3physical
27432908
CALX_HUMANCANXphysical
27432908
SE1L1_HUMANSEL1Lphysical
27432908
PDIA1_HUMANP4HBphysical
27432908
CAB45_HUMANSDF4physical
27432908
GANAB_HUMANGANABphysical
27432908
NGLY1_HUMANNGLY1physical
27432908
CIZ1_HUMANCIZ1physical
28514442
KLH15_HUMANKLHL15physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607944Spondyloenchondrodysplasia with immune dysregulation (SPENCDI)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PPA5_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structures of recombinant human purple acid phosphatase withand without an inhibitory conformation of the repression loop.";
Straeter N., Jasper B., Scholte M., Krebs B., Duff A.P., Langley D.B.,Han R., Averill B.A., Freeman H.C., Guss J.M.;
J. Mol. Biol. 351:233-246(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 22-325 IN COMPLEX WITH IRONIONS, AND GLYCOSYLATION AT ASN-116.

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