SAC1_HUMAN - dbPTM
SAC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAC1_HUMAN
UniProt AC Q9NTJ5
Protein Name Phosphatidylinositide phosphatase SAC1
Gene Name SACM1L
Organism Homo sapiens (Human).
Sequence Length 587
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Phosphoinositide phosphatase that hydrolyzes phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 4-phosphate (PtdIns(4)P). [PubMed: 24209621 Has low activity towards PtdIns(3,5)P2 (By similarity]
Protein Sequence MATAAYEQLKLHITPEKFYVEACDDGADDVLTIDRVSTEVTLAVKKDVPPSAVTRPIFGILGTIHLVAGNYLIVITKKIKVGEFFSHVVWKATDFDVLSYKKTMLHLTDIQLQDNKTFLAMLNHVLNVDGFYFSTTYDLTHTLQRLSNTSPEFQEMSLLERADQRFVWNGHLLRELSAQPEVHRFALPVLHGFITMHSCSINGKYFDWILISRRSCFRAGVRYYVRGIDSEGHAANFVETEQIVHYNGSKASFVQTRGSIPVFWSQRPNLKYKPLPQISKVANHMDGFQRHFDSQVIIYGKQVIINLINQKGSEKPLEQTFATMVSSLGSGMMRYIAFDFHKECKNMRWDRLSILLDQVAEMQDELSYFLVDSAGQVVANQEGVFRSNCMDCLDRTNVIQSLLARRSLQAQLQRLGVLHVGQKLEEQDEFEKIYKNAWADNANACAKQYAGTGALKTDFTRTGKRTHLGLIMDGWNSMIRYYKNNFSDGFRQDSIDLFLGNYSVDELESHSPLSVPRDWKFLALPIIMVVAFSMCIICLLMAGDTWTETLAYVLFWGVASIGTFFIILYNGKDFVDAPRLVQKEKID
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
6Phosphorylation--MATAAYEQLKLHI
--CCCHHHHHHHHCC
11.1827642862
10AcetylationTAAYEQLKLHITPEK
CHHHHHHHHCCCCHH
37.4025953088
45AcetylationTEVTLAVKKDVPPSA
CEEEEEEECCCCHHH
37.3325953088
101UbiquitinationDFDVLSYKKTMLHLT
CCHHHHHEEEEEEEE
38.09-
157PhosphorylationSPEFQEMSLLERADQ
CHHHHHHHHHHHHHH
29.1128857561
189UbiquitinationVHRFALPVLHGFITM
HHHHHHHHHHCCEEE
6.83-
205PhosphorylationSCSINGKYFDWILIS
EEEECCEEEEEEEEE
14.2520068231
212UbiquitinationYFDWILISRRSCFRA
EEEEEEEECHHHHHC
20.42-
212PhosphorylationYFDWILISRRSCFRA
EEEEEEEECHHHHHC
20.4220068231
230PhosphorylationYYVRGIDSEGHAANF
EEEECCCCCCCCCCE
43.4928270605
240PhosphorylationHAANFVETEQIVHYN
CCCCEEEEEEEEEEC
28.0828270605
250UbiquitinationIVHYNGSKASFVQTR
EEEECCCCEEEEEEC
49.82-
265PhosphorylationGSIPVFWSQRPNLKY
CCCCEEECCCCCCCC
12.5928857561
273UbiquitinationQRPNLKYKPLPQISK
CCCCCCCCCCCHHHH
38.19-
294PhosphorylationGFQRHFDSQVIIYGK
HHHHHCCCEEEEEEE
25.9623312004
342MalonylationYIAFDFHKECKNMRW
HHEEEHHHHHHCCCH
65.8726320211
362UbiquitinationLLDQVAEMQDELSYF
HHHHHHHCHHHHHEE
4.36-
386UbiquitinationANQEGVFRSNCMDCL
ECCCCCCCCCCHHHH
25.26-
387PhosphorylationNQEGVFRSNCMDCLD
CCCCCCCCCCHHHHC
23.9420068231
395UbiquitinationNCMDCLDRTNVIQSL
CCHHHHCHHHHHHHH
18.43-
396PhosphorylationCMDCLDRTNVIQSLL
CHHHHCHHHHHHHHH
33.2420068231
401PhosphorylationDRTNVIQSLLARRSL
CHHHHHHHHHHHHHH
17.7724076635
407PhosphorylationQSLLARRSLQAQLQR
HHHHHHHHHHHHHHH
21.1927174698
422UbiquitinationLGVLHVGQKLEEQDE
HCCCCCCCHHHCHHH
46.18-
423UbiquitinationGVLHVGQKLEEQDEF
CCCCCCCHHHCHHHH
52.52-
432UbiquitinationEEQDEFEKIYKNAWA
HCHHHHHHHHHHHHH
57.57-
432MethylationEEQDEFEKIYKNAWA
HCHHHHHHHHHHHHH
57.5766692039
435UbiquitinationDEFEKIYKNAWADNA
HHHHHHHHHHHHHHH
43.60-
447UbiquitinationDNANACAKQYAGTGA
HHHHHHHHHHCCCCC
43.66-
456UbiquitinationYAGTGALKTDFTRTG
HCCCCCCCCCCCCCC
45.5819608861
456MalonylationYAGTGALKTDFTRTG
HCCCCCCCCCCCCCC
45.5826320211
456AcetylationYAGTGALKTDFTRTG
HCCCCCCCCCCCCCC
45.5819608861
483UbiquitinationNSMIRYYKNNFSDGF
HHHHHHHHHCCCCCC
36.1621890473
483UbiquitinationNSMIRYYKNNFSDGF
HHHHHHHHHCCCCCC
36.1621890473
511PhosphorylationVDELESHSPLSVPRD
HHHHHHCCCCCCCCC
36.4929802988
514PhosphorylationLESHSPLSVPRDWKF
HHHCCCCCCCCCHHH
33.2024719451

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 SAC1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAC1_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 SAC1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAC1_HUMANSACM1Lphysical
14527956
COPA_HUMANCOPAphysical
14527956
COPB_HUMANCOPB1physical
14527956
COPE_HUMANCOPEphysical
14527956
COPG1_HUMANCOPG1physical
14527956

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 SAC1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-456, AND MASS SPECTROMETRY.

TOP