SAHH3_HUMAN - dbPTM
SAHH3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAHH3_HUMAN
UniProt AC Q96HN2
Protein Name Adenosylhomocysteinase 3
Gene Name AHCYL2
Organism Homo sapiens (Human).
Sequence Length 611
Subcellular Localization Cytoplasm . Microsome . Associates with membranes when phosphorylated, probably through interaction with ITPR1.
Protein Description May regulate the electrogenic sodium/bicarbonate cotransporter SLC4A4 activity and Mg(2+)-sensitivity. On the contrary of its homolog AHCYL1, does not regulate ITPR1 sensitivity to inositol 1,4,5-trisphosphate. [PubMed: 19220705]
Protein Sequence MSVQVVSAAAAAKVPEVELKDLSPSEAESQLGLSTAAVGAMAPPAGGGDPEAPAPAAERPPVPGPGSGPAAALSPAAGKVPQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVKKQIQFADQKQEFNKRPTKIGRRSLSRSISQSSTDSYSSAASYTDSSDDETSPRDKQQKNSKGSSDFCVKNIKQAEFGRREIEIAEQEMPALMALRKRAQGEKPLAGAKIVGCTHITAQTAVLMETLGALGAQCRWAACNIYSTLNEVAAALAESGFPVFAWKGESEDDFWWCIDRCVNVEGWQPNMILDDGGDLTHWIYKKYPNMFKKIKGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDMMFGGKQVVVCGYGEVGKGCCAALKAMGSIVYVTEIDPICALQACMDGFRLVKLNEVIRQVDIVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVASLRTPELTWERVRSQVDHVIWPDGKRIVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPTFDAHLTELTDEQAKYLGLNKNGPFKPNYYRY
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
2Acetylation------MSVQVVSAA
------CCHHHHHHH
22.6622223895
2Phosphorylation------MSVQVVSAA
------CCHHHHHHH
22.6629255136
7Phosphorylation-MSVQVVSAAAAAKV
-CCHHHHHHHHHHCC
17.2121406692
23PhosphorylationEVELKDLSPSEAESQ
CEEEECCCHHHHHHH
36.1928348404
25PhosphorylationELKDLSPSEAESQLG
EEECCCHHHHHHHHC
46.1728348404
34PhosphorylationAESQLGLSTAAVGAM
HHHHHCCCHHHHCCC
17.7528348404
35PhosphorylationESQLGLSTAAVGAMA
HHHHCCCHHHHCCCC
24.5528348404
67PhosphorylationPPVPGPGSGPAAALS
CCCCCCCCCCHHHCC
44.7428348404
74PhosphorylationSGPAAALSPAAGKVP
CCCHHHCCCCCCCCC
14.0428111955
84PhosphorylationAGKVPQASAMKRSDP
CCCCCCHHHHCCCCC
24.5325159151
89PhosphorylationQASAMKRSDPHHQHQ
CHHHHCCCCCCCCCH
50.4036012879
89UbiquitinationQASAMKRSDPHHQHQ
CHHHHCCCCCCCCCH
50.4032015554
107PhosphorylationDGGEALVSPDGTVTE
CCCCEECCCCCCCCC
20.3730266825
107 (in isoform 2)Phosphorylation-20.3725159151
111PhosphorylationALVSPDGTVTEAPRT
EECCCCCCCCCCCHH
31.4730266825
113PhosphorylationVSPDGTVTEAPRTVK
CCCCCCCCCCCHHHH
26.6830266825
113 (in isoform 2)Phosphorylation-26.6825159151
118PhosphorylationTVTEAPRTVKKQIQF
CCCCCCHHHHHHHHH
35.3021712546
121AcetylationEAPRTVKKQIQFADQ
CCCHHHHHHHHHHHH
48.58-
143PhosphorylationPTKIGRRSLSRSISQ
CCHHHHHHHHHHHCC
29.3630576142
145PhosphorylationKIGRRSLSRSISQSS
HHHHHHHHHHHCCCC
25.8128102081
147PhosphorylationGRRSLSRSISQSSTD
HHHHHHHHHCCCCCC
24.1868734381
149PhosphorylationRSLSRSISQSSTDSY
HHHHHHHCCCCCCCC
25.8416793548
151PhosphorylationLSRSISQSSTDSYSS
HHHHHCCCCCCCCCC
28.5468737123
152PhosphorylationSRSISQSSTDSYSSA
HHHHCCCCCCCCCCC
28.7016793548
153PhosphorylationRSISQSSTDSYSSAA
HHHCCCCCCCCCCCH
33.9228270605
155PhosphorylationISQSSTDSYSSAASY
HCCCCCCCCCCCHHC
27.3119220705
156PhosphorylationSQSSTDSYSSAASYT
CCCCCCCCCCCHHCC
14.9528270605
157PhosphorylationQSSTDSYSSAASYTD
CCCCCCCCCCHHCCC
19.9028270605
158UbiquitinationSSTDSYSSAASYTDS
CCCCCCCCCHHCCCC
21.4421963094
158PhosphorylationSSTDSYSSAASYTDS
CCCCCCCCCHHCCCC
21.4419220705
160UbiquitinationTDSYSSAASYTDSSD
CCCCCCCHHCCCCCC
12.6722817900
161PhosphorylationDSYSSAASYTDSSDD
CCCCCCHHCCCCCCC
28.4328270605
162PhosphorylationSYSSAASYTDSSDDE
CCCCCHHCCCCCCCC
15.1628270605
163PhosphorylationYSSAASYTDSSDDET
CCCCHHCCCCCCCCC
27.239469109
165PhosphorylationSAASYTDSSDDETSP
CCHHCCCCCCCCCCH
28.0630576142
166PhosphorylationAASYTDSSDDETSPR
CHHCCCCCCCCCCHH
52.4730576142
170PhosphorylationTDSSDDETSPRDKQQ
CCCCCCCCCHHHHHH
51.5330576142
171PhosphorylationDSSDDETSPRDKQQK
CCCCCCCCHHHHHHH
18.85110756339
176UbiquitinationETSPRDKQQKNSKGS
CCCHHHHHHHCCCCC
64.8622817900
191UbiquitinationSDFCVKNIKQAEFGR
CCCHHHHHHHHHHCC
2.6532015554
192UbiquitinationDFCVKNIKQAEFGRR
CCHHHHHHHHHHCCH
53.5032015554
222UbiquitinationRKRAQGEKPLAGAKI
HHHHCCCCCCCCCEE
52.75-
245UbiquitinationQTAVLMETLGALGAQ
HHHHHHHHHHHHHHH
19.2732015554
248UbiquitinationVLMETLGALGAQCRW
HHHHHHHHHHHHHHH
13.1132015554
262UbiquitinationWAACNIYSTLNEVAA
HHHHHHHHHHHHHHH
23.7121963094
263UbiquitinationAACNIYSTLNEVAAA
HHHHHHHHHHHHHHH
19.3421963094
264UbiquitinationACNIYSTLNEVAAAL
HHHHHHHHHHHHHHH
4.1822817900
265UbiquitinationCNIYSTLNEVAAALA
HHHHHHHHHHHHHHH
41.6122817900
280UbiquitinationESGFPVFAWKGESED
HCCCCEEEECCCCCC
13.8022817900
281UbiquitinationSGFPVFAWKGESEDD
CCCCEEEECCCCCCC
9.5622817900
306UbiquitinationVEGWQPNMILDDGGD
CCCCCCCEEEECCCC
4.0222817900
319PhosphorylationGDLTHWIYKKYPNMF
CCHHHHHHHHCCCHH
9.0220090780
322PhosphorylationTHWIYKKYPNMFKKI
HHHHHHHCCCHHHHH
8.836831203
338PhosphorylationGIVEESVTGVHRLYQ
HHHHHHCCHHHHHHH
42.6450564075
344PhosphorylationVTGVHRLYQLSKAGK
CCHHHHHHHHHHCCC
13.836831211
347UbiquitinationVHRLYQLSKAGKLCV
HHHHHHHHHCCCEEE
12.6332015554
348UbiquitinationHRLYQLSKAGKLCVP
HHHHHHHHCCCEEEE
70.5232015554
350UbiquitinationLYQLSKAGKLCVPAM
HHHHHHCCCEEEEEC
27.4932015554
351UbiquitinationYQLSKAGKLCVPAMN
HHHHHCCCEEEEECC
43.5032015554
362PhosphorylationPAMNVNDSVTKQKFD
EECCCCCHHHHHHCC
26.8720068231
364PhosphorylationMNVNDSVTKQKFDNL
CCCCCHHHHHHCCCE
31.5420068231
364UbiquitinationMNVNDSVTKQKFDNL
CCCCCHHHHHHCCCE
31.5421963094
365UbiquitinationNVNDSVTKQKFDNLY
CCCCHHHHHHCCCEE
49.7021963094
366UbiquitinationVNDSVTKQKFDNLYC
CCCHHHHHHCCCEEE
42.1322817900
367UbiquitinationNDSVTKQKFDNLYCC
CCHHHHHHCCCEEEH
57.1322817900
377PhosphorylationNLYCCRESILDGLKR
CEEEHHHHHHHHHHH
14.7529759185
382UbiquitinationRESILDGLKRTTDMM
HHHHHHHHHHHHCCE
3.2022817900
383UbiquitinationESILDGLKRTTDMMF
HHHHHHHHHHHCCEE
53.9122817900
410UbiquitinationVGKGCCAALKAMGSI
HHHHHHHHHHHCCCE
8.8322817900
411UbiquitinationGKGCCAALKAMGSIV
HHHHHHHHHHCCCEE
1.6122817900
440AcetylationMDGFRLVKLNEVIRQ
HCCEEEEEHHHHHHH
50.6225953088
456UbiquitinationDIVITCTGNKNVVTR
CEEEECCCCCCEECH
45.3133845483
465UbiquitinationKNVVTREHLDRMKNS
CCEECHHHHHHHCCC
29.7329967540
472PhosphorylationHLDRMKNSCIVCNMG
HHHHHCCCEEEECCC
10.3316793548
481PhosphorylationIVCNMGHSNTEIDVA
EEECCCCCCCEEEHH
39.45113331545
483PhosphorylationCNMGHSNTEIDVASL
ECCCCCCCEEEHHHC
37.0150564083
492PhosphorylationIDVASLRTPELTWER
EEHHHCCCCCCCHHH
26.8021406692
496PhosphorylationSLRTPELTWERVRSQ
HCCCCCCCHHHHHHH
24.5021406692
499MethylationTPELTWERVRSQVDH
CCCCCHHHHHHHCCE
22.25-
502PhosphorylationLTWERVRSQVDHVIW
CCHHHHHHHCCEEEC
31.5324719451
512UbiquitinationDHVIWPDGKRIVLLA
CEEECCCCCEEEEEE
19.6422817900
513UbiquitinationHVIWPDGKRIVLLAE
EEECCCCCEEEEEEC
46.4622817900
514MethylationVIWPDGKRIVLLAEG
EECCCCCEEEEEECC
29.76-
533PhosphorylationLSCSTVPTFVLSITA
EECCCCCEEEEEHHH
23.2622210691
537PhosphorylationTVPTFVLSITATTQA
CCCEEEEEHHHHHHH
16.7622210691
542PhosphorylationVLSITATTQALALIE
EEEHHHHHHHHHHHH
14.9122210691
558UbiquitinationYNAPEGRYKQDVYLL
HCCCCCCCCCCEEEC
24.6933845483
559UbiquitinationNAPEGRYKQDVYLLP
CCCCCCCCCCEEECC
38.3733845483
563PhosphorylationGRYKQDVYLLPKKMD
CCCCCCEEECCHHHH
15.71110736809
567UbiquitinationQDVYLLPKKMDEYVA
CCEEECCHHHHHHHH
61.7829967540
568UbiquitinationDVYLLPKKMDEYVAS
CEEECCHHHHHHHHH
50.0429967540
605UbiquitinationLNKNGPFKPNYYRY-
CCCCCCCCCCCCCC-
35.17-
608PhosphorylationNGPFKPNYYRY----
CCCCCCCCCCC----
9.6121945579
609PhosphorylationGPFKPNYYRY-----
CCCCCCCCCC-----
15.2921945579
610MethylationPFKPNYYRY------
CCCCCCCCC------
21.96-

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 SAHH3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAHH3_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 SAHH3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSMD4_HUMANPSMD4physical
26344197
RS8_HUMANRPS8physical
26344197
SAHH2_HUMANAHCYL1physical
28514442
ZIC2_HUMANZIC2physical
28514442
FOXK2_HUMANFOXK2physical
28514442
IKBL1_HUMANNFKBIL1physical
28514442
PI42C_HUMANPIP4K2Cphysical
28514442
FOXK1_HUMANFOXK1physical
28514442
DUS11_HUMANDUSP11physical
28514442
HXB6_HUMANHOXB6physical
28514442
BANP_HUMANBANPphysical
28514442
PI42B_HUMANPIP4K2Bphysical
28514442
KI18B_HUMANKIF18Bphysical
28514442
HXB9_HUMANHOXB9physical
28514442
PLCD3_HUMANPLCD3physical
28514442
BCD1_HUMANZNHIT6physical
28514442
CAB39_HUMANCAB39physical
28514442
PI51A_HUMANPIP5K1Aphysical
28514442
WDR33_HUMANWDR33physical
28514442
PDD2L_HUMANPDCD2Lphysical
28514442
JUN_HUMANJUNphysical
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 SAHH3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-107, AND MASSSPECTROMETRY.

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