ASPH_HUMAN - dbPTM
ASPH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASPH_HUMAN
UniProt AC Q12797
Protein Name Aspartyl/asparaginyl beta-hydroxylase
Gene Name ASPH
Organism Homo sapiens (Human).
Sequence Length 758
Subcellular Localization Isoform 1: Endoplasmic reticulum membrane
Single-pass type II membrane protein .
Isoform 4: Sarcoplasmic reticulum membrane
Single-pass type II membrane protein .
Isoform 8: Endoplasmic reticulum membrane
Single-pass type II membrane protein .
Protein Description Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.; Isoform 8: membrane-bound Ca(2+)-sensing protein, which is a structural component of the ER-plasma membrane junctions. Isoform 8 regulates the activity of Ca(+2) released-activated Ca(+2) (CRAC) channels in T-cells..
Protein Sequence MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARRETKHGGHKNGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHVEGEDLQQEDGPTGEPQQEDDEFLMATDVDDRFETLEPEVSHEETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQEVPPETNRKTDDPEQKAKVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
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
8UbiquitinationMAQRKNAKSSGNSSS
CCCCCCCCCCCCCCC		55.3221906983
9PhosphorylationAQRKNAKSSGNSSSS
CCCCCCCCCCCCCCC		40.8625159151
10PhosphorylationQRKNAKSSGNSSSSG
CCCCCCCCCCCCCCC		41.0925159151
13PhosphorylationNAKSSGNSSSSGSGS
CCCCCCCCCCCCCCC		34.8125159151
14PhosphorylationAKSSGNSSSSGSGSG
CCCCCCCCCCCCCCC		32.3011007777
15PhosphorylationKSSGNSSSSGSGSGS
CCCCCCCCCCCCCCC		38.2425159151
16PhosphorylationSSGNSSSSGSGSGST
CCCCCCCCCCCCCCC		38.6425159151
18PhosphorylationGNSSSSGSGSGSTSA
CCCCCCCCCCCCCCC		31.5625159151
20PhosphorylationSSSSGSGSGSTSAGS
CCCCCCCCCCCCCCC		31.1325159151
22PhosphorylationSSGSGSGSTSAGSSS
CCCCCCCCCCCCCCC		22.3825159151
23PhosphorylationSGSGSGSTSAGSSSP
CCCCCCCCCCCCCCC		26.5625159151
24PhosphorylationGSGSGSTSAGSSSPG
CCCCCCCCCCCCCCC		32.1225159151
27PhosphorylationSGSTSAGSSSPGARR
CCCCCCCCCCCCCCC		27.6225159151
28PhosphorylationGSTSAGSSSPGARRE
CCCCCCCCCCCCCCC		39.3725159151
29PhosphorylationSTSAGSSSPGARRET
CCCCCCCCCCCCCCC		29.1125159151
36PhosphorylationSPGARRETKHGGHKN
CCCCCCCCCCCCCCC		26.9130576142
63 (in isoform 3)Phosphorylation-2.69-
63 (in isoform 5)Phosphorylation-2.69-
63 (in isoform 8)Phosphorylation-2.69-
63 (in isoform 9)Phosphorylation-2.69-
64 (in isoform 3)N-linked_Glycosylation-3.72-
66 (in isoform 3)Phosphorylation-5.20-
66 (in isoform 5)Phosphorylation-5.20-
66 (in isoform 8)Phosphorylation-5.20-
66 (in isoform 9)Phosphorylation-5.20-
81UbiquitinationWFDLVDYEEVLGKLG
HHHCCCHHHHHHHCC		36.8521890473
82 (in isoform 4)Phosphorylation-36.4926437602
90PhosphorylationVLGKLGIYDADGDGD
HHHHCCCCCCCCCCC		11.86-
92 (in isoform 7)Phosphorylation-13.00-
95 (in isoform 7)Phosphorylation-54.78-
96UbiquitinationIYDADGDGDFDVDDA
CCCCCCCCCCCHHHH		42.9121890473
96UbiquitinationIYDADGDGDFDVDDA
CCCCCCCCCCCHHHH		42.9121890473
96UbiquitinationIYDADGDGDFDVDDA
CCCCCCCCCCCHHHH		42.9121890473
97 (in isoform 3)Phosphorylation-41.1126437602
104UbiquitinationDFDVDDAKVLLGLKE
CCCHHHHHHHHCCCC		40.1721890473
110UbiquitinationAKVLLGLKERSTSEP
HHHHHCCCCCCCCCC		49.6521890473
1102-HydroxyisobutyrylationAKVLLGLKERSTSEP
HHHHHCCCCCCCCCC		49.65-
110SuccinylationAKVLLGLKERSTSEP
HHHHHCCCCCCCCCC		49.6523954790
110UbiquitinationAKVLLGLKERSTSEP
HHHHHCCCCCCCCCC		49.6521890473
110UbiquitinationAKVLLGLKERSTSEP
HHHHHCCCCCCCCCC		49.6521890473
114O-linked_GlycosylationLGLKERSTSEPAVPP
HCCCCCCCCCCCCCH		43.24OGP
128PhosphorylationPEEAEPHTEPEEQVP
HHHCCCCCCCHHHCC		65.04-
176O-linked_GlycosylationLQQEDGPTGEPQQED
CCCCCCCCCCCCCCC		60.76OGP
177 (in isoform 4)Phosphorylation-47.9621406692
178 (in isoform 4)Phosphorylation-42.2721406692
182 (in isoform 4)Phosphorylation-63.2821406692
190PhosphorylationDDEFLMATDVDDRFE
CCCEEECCCCCCCCC		23.6922468782
192 (in isoform 3)Phosphorylation-7.7721406692
193 (in isoform 3)Phosphorylation-44.1521406692
197 (in isoform 3)Phosphorylation-54.0721406692
197 (in isoform 4)Phosphorylation-54.0726437602
198PhosphorylationDVDDRFETLEPEVSH
CCCCCCCCCCCCCCC		33.4422468782
198 (in isoform 11)Phosphorylation-33.4426471730
201 (in isoform 4)Phosphorylation-50.8626437602
204PhosphorylationETLEPEVSHEETEHS
CCCCCCCCCCHHCCE		24.4224275569
204 (in isoform 11)Phosphorylation-24.4220071362
208 (in isoform 11)Phosphorylation-35.6926471730
211 (in isoform 11)Phosphorylation-15.6526471730
212 (in isoform 11)Phosphorylation-16.2826471730
212 (in isoform 3)Phosphorylation-16.2826437602
216 (in isoform 3)Phosphorylation-54.1126437602
217 (in isoform 11)Phosphorylation-16.3824275569
217O-linked_GlycosylationHSYHVEETVSQDCNQ
CEEECCHHHCHHCCH		16.38OGP
219 (in isoform 11)Phosphorylation-27.9320071362
220 (in isoform 11)Phosphorylation-55.7424275569
238PhosphorylationSEQENPDSSEPVVED
HHCCCCCCCCCCCCC		37.5524275569
239PhosphorylationEQENPDSSEPVVEDE
HCCCCCCCCCCCCCC		53.9824275569
280O-linked_GlycosylationGIEITEVTAPPEDNP
CCEEEEEECCCCCCC		27.49OGP
323AcetylationKTDDPEQKAKVKKKK
CCCCHHHHHHHHHCC		48.817693103
336AcetylationKKPKLLNKFDKTIKA
CCHHHHHHHHHHHHH		55.7125825284
3362-HydroxyisobutyrylationKKPKLLNKFDKTIKA
CCHHHHHHHHHHHHH		55.71-
339MalonylationKLLNKFDKTIKAELD
HHHHHHHHHHHHHHH		56.1126320211
350UbiquitinationAELDAAEKLRKRGKI
HHHHHHHHHHHCCCH		49.19-
3502-HydroxyisobutyrylationAELDAAEKLRKRGKI
HHHHHHHHHHHCCCH		49.19-
3562-HydroxyisobutyrylationEKLRKRGKIEEAVNA
HHHHHCCCHHHHHHH		51.48-
3652-HydroxyisobutyrylationEEAVNAFKELVRKYP
HHHHHHHHHHHHHCC		47.96-
3702-HydroxyisobutyrylationAFKELVRKYPQSPRA
HHHHHHHHCCCCHHH		54.53-
405PhosphorylationLRGAIETYQEVASLP
HHHHHHHHHHHHCCC		7.01-
420UbiquitinationDVPADLLKLSLKRRS
CCCHHHHHHHHCCHH		43.24-
452N-linked_GlycosylationRLVQLFPNDTSLKND
HHHHHCCCCCCCCCC		58.83UniProtKB CARBOHYD
452N-linked_GlycosylationRLVQLFPNDTSLKND
HHHHHCCCCCCCCCC		58.8320068230
464PhosphorylationKNDLGVGYLLIGDND
CCCCCCEEEEECCCC		8.91-
474UbiquitinationIGDNDNAKKVYEEVL
ECCCCCHHHHHHHHH		49.37-
475AcetylationGDNDNAKKVYEEVLS
CCCCCHHHHHHHHHC		47.8726051181
477PhosphorylationNDNAKKVYEEVLSVT
CCCHHHHHHHHHCCC		18.43-
484PhosphorylationYEEVLSVTPNDGFAK
HHHHHCCCCCCCCCE		17.01-
494PhosphorylationDGFAKVHYGFILKAQ
CCCCEEEHEEEHHHH		19.4028152594
499AcetylationVHYGFILKAQNKIAE
EEHEEEHHHHHHHHH		43.0125825284
4992-HydroxyisobutyrylationVHYGFILKAQNKIAE
EEHEEEHHHHHHHHH		43.01-
5032-HydroxyisobutyrylationFILKAQNKIAESIPY
EEHHHHHHHHHHCHH		31.08-
510PhosphorylationKIAESIPYLKEGIES
HHHHHCHHHHCCHHC		28.83-
512UbiquitinationAESIPYLKEGIESGD
HHHCHHHHCCHHCCC		48.3121890473
517PhosphorylationYLKEGIESGDPGTDD
HHHCCHHCCCCCCCC		46.7221955146
522PhosphorylationIESGDPGTDDGRFYF
HHCCCCCCCCCCEEE		35.9821955146
541UbiquitinationAMQRVGNKEAYKWYE
HHHHHCCHHHHHHHH		37.48-
545AcetylationVGNKEAYKWYELGHK
HCCHHHHHHHHHCCC		50.8025825284
545UbiquitinationVGNKEAYKWYELGHK
HCCHHHHHHHHHCCC		50.80-
5452-HydroxyisobutyrylationVGNKEAYKWYELGHK
HCCHHHHHHHHHCCC		50.80-
577PhosphorylationLKAQPWWTPKETGYT
CCCCCCCCCCCCCHH		22.18-
579UbiquitinationAQPWWTPKETGYTEL
CCCCCCCCCCCHHHH		61.61-
5792-HydroxyisobutyrylationAQPWWTPKETGYTEL
CCCCCCCCCCCHHHH		61.61-
583PhosphorylationWTPKETGYTELVKSL
CCCCCCCHHHHHHHH		12.4025690035
584PhosphorylationTPKETGYTELVKSLE
CCCCCCHHHHHHHHH		24.9625690035
588UbiquitinationTGYTELVKSLERNWK
CCHHHHHHHHHHHHH		63.05-
6072-HydroxyisobutyrylationEGLAVMDKAKGLFLP
CCCCHHHHCCCEECC		33.62-
6092-HydroxyisobutyrylationLAVMDKAKGLFLPED
CCHHHHCCCEECCCC		62.98-
622UbiquitinationEDENLREKGDWSQFT
CCCCHHHCCCHHHHH		56.59-
6222-HydroxyisobutyrylationEDENLREKGDWSQFT
CCCCHHHCCCHHHHH		56.59-
653AcetylationKTCTLLEKFPETTGC
CCCHHHHHCCCCCCC		67.2125825284
6532-HydroxyisobutyrylationKTCTLLEKFPETTGC
CCCHHHHHCCCCCCC		67.21-
706N-linked_GlycosylationGCKIRCANETKTWEE
CCEEEECCCCCCCCC		62.18UniProtKB 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 ASPH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASPH_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 ASPH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
MCUB_HUMANCCDC109Bphysical
28514442
MCU_HUMANMCUphysical
28514442
STEA3_HUMANSTEAP3physical
28514442
F162A_HUMANFAM162Aphysical
28514442
TM160_HUMANTMEM160physical
28514442
STX4_HUMANSTX4physical
28514442
EMRE_HUMANSMDT1physical
28514442
CIA30_HUMANNDUFAF1physical
28514442
LEMD2_HUMANLEMD2physical
28514442
TM192_HUMANTMEM192physical
28514442
ECSIT_HUMANECSITphysical
28514442
STXB3_HUMANSTXBP3physical
28514442
LRC59_HUMANLRRC59physical
28514442
STX8_HUMANSTX8physical
28514442
EXD2_HUMANEXD2physical
28514442
SEC20_HUMANBNIP1physical
28514442
ACAD9_HUMANACAD9physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601552Facial dysmorphism, lens dislocation, anterior segment abnormalities, and spontaneous filtering blebs (FDLAB)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASPH_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-452 (ISOFORM 1),GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64 (ISOFORM JUNCTIN-1),AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-29, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory