SAC2_HUMAN - dbPTM
SAC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAC2_HUMAN
UniProt AC Q9Y2H2
Protein Name Phosphatidylinositide phosphatase SAC2 {ECO:0000305}
Gene Name INPP5F {ECO:0000312|HGNC:HGNC:17054}
Organism Homo sapiens (Human).
Sequence Length 1132
Subcellular Localization Membrane, clathrin-coated pit . Early endosome . Recycling endosome . Also found on macropinosomes.
Protein Description Inositol 4-phosphatase which mainly acts on phosphatidylinositol 4-phosphate. May be functionally linked to OCRL, which converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol, for a sequential dephosphorylation of phosphatidylinositol 4,5-bisphosphate at the 5 and 4 position of inositol, thus playing an important role in the endocytic recycling. [PubMed: 25869669 Regulator of TF:TFRC and integrins recycling pathway, is also involved in cell migration mechanisms]
Protein Sequence MELFQAKDHYILQQGERALWCSRRDGGLQLRPATDLLLAWNPICLGLVEGVIGKIQLHSDLPWWLILIRQKALVGKLPGDHEVCKVTKIAVLSLSEMEPQDLELELCKKHHFGINKPEKIIPSPDDSKFLLKTFTHIKSNVSAPNKKKVKESKEKEKLERRLLEELLKMFMDSESFYYSLTYDLTNSVQRQSTGERDGRPLWQKVDDRFFWNKYMIQDLTEIGTPDVDFWIIPMIQGFVQIEELVVNYTESSDDEKSSPETPPQESTCVDDIHPRFLVALISRRSRHRAGMRYKRRGVDKNGNVANYVETEQLIHVHNHTLSFVQTRGSVPVFWSQVGYRYNPRPRLDRSEKETVAYFCAHFEEQLNIYKKQVIINLVDQAGREKIIGDAYLKQVLLFNNSHLTYVSFDFHEHCRGMKFENVQTLTDAIYDIILDMKWCWVDEAGVICKQEGIFRVNCMDCLDRTNVVQAAIARVVMEQQLKKLGVMPPEQPLPVKCNRIYQIMWANNGDSISRQYAGTAALKGDFTRTGERKLAGVMKDGVNSANRYYLNRFKDAYRQAVIDLMQGIPVTEDLYSIFTKEKEHEALHKENQRSHQELISQLLQSYMKLLLPDDEKFHGGWALIDCDPSLIDATHRDVDVLLLLSNSAYYVAYYDDEVDKVNQYQRLSLENLEKIEIGPEPTLFGKPKFSCMRLHYRYKEASGYFHTLRAVMRNPEEDGKDTLQCIAEMLQITKQAMGSDLPIIEKKLERKSSKPHEDIIGIRSQNQGSLAQGKNFLMSKFSSLNQKVKQTKSNVNIGNLRKLGNFTKPEMKVNFLKPNLKVNLWKSDSSLETMENTGVMDKVQAESDGDMSSDNDSYHSDEFLTNSKSDEDRQLANSLESVGPIDYVLPSCGIIASAPRLGSRSQSLSSTDSSVHAPSEITVAHGSGLGKGQESPLKKSPSAGDVHILTGFAKPMDIYCHRFVQDAQNKVTHLSETRSVSQQASQERNQMTNQVSNETQSESTEQTPSRPSQLDVSLSATGPQFLSVEPAHSVASQKTPTSASSMLELETGLHVTPSPSESSSSRAVSPFAKIRSSMVQVASITQAGLTHGINFAVSKVQKSPPEPEIINQVQQNELKKMFIQCQTRIIQI
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
123PhosphorylationKPEKIIPSPDDSKFL
CCHHHCCCCCCCHHH
30.4730266825
127PhosphorylationIIPSPDDSKFLLKTF
HCCCCCCCHHHHHHH
32.4630266825
138AcetylationLKTFTHIKSNVSAPN
HHHHHHHHHCCCCCC
28.5119822409
192PhosphorylationTNSVQRQSTGERDGR
CCHHHHCCCCCCCCC
40.3430576142
193PhosphorylationNSVQRQSTGERDGRP
CHHHHCCCCCCCCCC
34.4230576142
257PhosphorylationESSDDEKSSPETPPQ
CCCCCCCCCCCCCCC
49.4225002506
258PhosphorylationSSDDEKSSPETPPQE
CCCCCCCCCCCCCCC
37.5125002506
261PhosphorylationDEKSSPETPPQESTC
CCCCCCCCCCCCCCC
43.5928985074
266PhosphorylationPETPPQESTCVDDIH
CCCCCCCCCCCCCCC
23.1223312004
267PhosphorylationETPPQESTCVDDIHP
CCCCCCCCCCCCCCH
18.7823312004
341PhosphorylationWSQVGYRYNPRPRLD
HHHCCCCCCCCCCCC
22.4922985185
369PhosphorylationFEEQLNIYKKQVIIN
HHHHHHHHCHHHHHH
15.8524260401
391PhosphorylationEKIIGDAYLKQVLLF
HHHCCHHHHHEEEEE
21.1221406692
430PhosphorylationQTLTDAIYDIILDMK
HHHHHHHHHHHHCCC
11.6522817900
544PhosphorylationVMKDGVNSANRYYLN
HHHCCCHHHHHHHHH
25.2325106551
575PhosphorylationIPVTEDLYSIFTKEK
CCCCHHHHHHHCHHH
16.43-
668PhosphorylationVNQYQRLSLENLEKI
CHHHHCCCHHHHCCC
35.5130266825
698PhosphorylationCMRLHYRYKEASGYF
EEEEEEEHHHHHCCH
13.1523186163
702PhosphorylationHYRYKEASGYFHTLR
EEEHHHHHCCHHHHH
34.8123186163
704PhosphorylationRYKEASGYFHTLRAV
EHHHHHCCHHHHHHH
6.9523186163
707PhosphorylationEASGYFHTLRAVMRN
HHHCCHHHHHHHHHC
14.1924043423
733PhosphorylationIAEMLQITKQAMGSD
HHHHHHHHHHHHCCC
12.2524114839
783PhosphorylationFLMSKFSSLNQKVKQ
HHHHHHHHHHHHHHH
34.1825002506
793PhosphorylationQKVKQTKSNVNIGNL
HHHHHCCCCCCCCHH
49.7725159151
827PhosphorylationLKVNLWKSDSSLETM
EEEEEEECCCCCHHH
31.0119664994
829PhosphorylationVNLWKSDSSLETMEN
EEEEECCCCCHHHHH
43.8623401153
830PhosphorylationNLWKSDSSLETMENT
EEEECCCCCHHHHHC
34.9029255136
833PhosphorylationKSDSSLETMENTGVM
ECCCCCHHHHHCCCC
34.7723927012
837PhosphorylationSLETMENTGVMDKVQ
CCHHHHHCCCCCEEE
20.1823403867
853PhosphorylationESDGDMSSDNDSYHS
CCCCCCCCCCCCCCC
33.5230576142
857PhosphorylationDMSSDNDSYHSDEFL
CCCCCCCCCCCCHHH
30.8830576142
869PhosphorylationEFLTNSKSDEDRQLA
HHHHCCCCHHHHHHH
46.1629507054
878PhosphorylationEDRQLANSLESVGPI
HHHHHHHHHHHCCCC
28.1026657352
881PhosphorylationQLANSLESVGPIDYV
HHHHHHHHCCCCCEE
37.3522199227
887PhosphorylationESVGPIDYVLPSCGI
HHCCCCCEECCCCCE
12.4727732954
905PhosphorylationAPRLGSRSQSLSSTD
CCCCCCCCCCCCCCC
26.3122617229
907PhosphorylationRLGSRSQSLSSTDSS
CCCCCCCCCCCCCCC
31.3125159151
909PhosphorylationGSRSQSLSSTDSSVH
CCCCCCCCCCCCCCC
36.1221082442
910PhosphorylationSRSQSLSSTDSSVHA
CCCCCCCCCCCCCCC
41.3423898821
911PhosphorylationRSQSLSSTDSSVHAP
CCCCCCCCCCCCCCC
36.2023663014
913PhosphorylationQSLSSTDSSVHAPSE
CCCCCCCCCCCCCCE
34.0623663014
914PhosphorylationSLSSTDSSVHAPSEI
CCCCCCCCCCCCCEE
22.2623663014
919PhosphorylationDSSVHAPSEITVAHG
CCCCCCCCEEEEECC
42.2727732954
922PhosphorylationVHAPSEITVAHGSGL
CCCCCEEEEECCCCC
13.9527732954
927PhosphorylationEITVAHGSGLGKGQE
EEEEECCCCCCCCCC
22.4526074081
935PhosphorylationGLGKGQESPLKKSPS
CCCCCCCCCCCCCCC
27.8726055452
940PhosphorylationQESPLKKSPSAGDVH
CCCCCCCCCCCCCCE
23.6230266825
942PhosphorylationSPLKKSPSAGDVHIL
CCCCCCCCCCCCEEE
52.5629255136
950PhosphorylationAGDVHILTGFAKPMD
CCCCEEEECCCCCCE
29.6528464451
959PhosphorylationFAKPMDIYCHRFVQD
CCCCCEEEHHHHHHH
4.3025159151
985PhosphorylationRSVSQQASQERNQMT
HCHHHHHHHHHHHHH
28.3928348404
1012PhosphorylationEQTPSRPSQLDVSLS
CCCCCCCHHCEEEEE
42.1224719451
1036PhosphorylationEPAHSVASQKTPTSA
CCCCCCCCCCCCCCH
30.0124719451
1039PhosphorylationHSVASQKTPTSASSM
CCCCCCCCCCCHHHH
24.9425002506
1041PhosphorylationVASQKTPTSASSMLE
CCCCCCCCCHHHHEE
42.0025002506
1042PhosphorylationASQKTPTSASSMLEL
CCCCCCCCHHHHEEE
27.6225002506
1044PhosphorylationQKTPTSASSMLELET
CCCCCCHHHHEEEEC
18.9525002506
1045PhosphorylationKTPTSASSMLELETG
CCCCCHHHHEEEECC
27.4025002506
1051PhosphorylationSSMLELETGLHVTPS
HHHEEEECCCEECCC
58.6325002506
1056PhosphorylationLETGLHVTPSPSESS
EECCCEECCCCCCCC
13.8025002506
1058PhosphorylationTGLHVTPSPSESSSS
CCCEECCCCCCCCCC
31.5225002506
1060PhosphorylationLHVTPSPSESSSSRA
CEECCCCCCCCCCCC
55.2225002506
1062PhosphorylationVTPSPSESSSSRAVS
ECCCCCCCCCCCCCC
39.6025002506
1063PhosphorylationTPSPSESSSSRAVSP
CCCCCCCCCCCCCCC
28.4225002506
1069PhosphorylationSSSSRAVSPFAKIRS
CCCCCCCCCHHHHHH
17.2023927012
1098PhosphorylationHGINFAVSKVQKSPP
CCHHEHHHCCCCCCC
24.5526074081
1102AcetylationFAVSKVQKSPPEPEI
EHHHCCCCCCCCHHH
68.8469663
1103PhosphorylationAVSKVQKSPPEPEII
HHHCCCCCCCCHHHH
28.7030266825
1103O-linked_GlycosylationAVSKVQKSPPEPEII
HHHCCCCCCCCHHHH
28.7029351928

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 SAC2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAC2_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 SAC2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SAC2_HUMAN !!

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 SAC2_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-1069, AND MASSSPECTROMETRY.

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