ANS1A_HUMAN - dbPTM
ANS1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANS1A_HUMAN
UniProt AC Q92625
Protein Name Ankyrin repeat and SAM domain-containing protein 1A
Gene Name ANKS1A
Organism Homo sapiens (Human).
Sequence Length 1134
Subcellular Localization Cytoplasm. Cell projection. Cytoplasmic before and after growth factor treatment.
Protein Description Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction (By similarity)..
Protein Sequence MGKEQELLEAARTGHLPAVEKLLSGKRLSSGFGGGGGGGSGGGGGGSGGGGGGLGSSSHPLSSLLSMWRGPNVNCVDSTGYTPLHHAALNGHKDVVEVLLRNDALTNVADSKGCYPLHLAAWKGDAQIVRLLIHQGPSHTRVNEQNNDNETALHCAAQYGHTEVVKVLLEELTDPTMRNNKFETPLDLAALYGRLEVVKMLLNAHPNLLSCNTKKHTPLHLAARNGHKAVVQVLLDAGMDSNYQTEMGSALHEAALFGKTDVVQILLAAGTDVNIKDNHGLTALDTVRELPSQKSQQIAALIEDHMTGKRSTKEVDKTPPPQPPLISSMDSISQKSQGDVEKAVTELIIDFDANAEEEGPYEALYNAISCHSLDSMASGRSSDQDSTNKEAEAAGVKPAGVRPRERPPPPAKPPPDEEEEDHIDKKYFPLTASEVLSMRPRIHGSAAREEDEHPYELLLTAETKKVVLVDGKTKDHRRSSSSRSQDSAEGQDGQVPEQFSGLLHGSSPVCEVGQDPFQLLCTAGQSHPDGSPQQGACHKASMQLEETGVHAPGASQPSALDQSKRVGYLTGLPTTNSRSHPETLTHTASPHPGGAEEGDRSGARSRAPPTSKPKAELKLSRSLSKSDSDLLTCSPTEDATMGSRSESLSNCSIGKKRLEKSPSFASEWDEIEKIMSSIGEGIDFSQERQKISGLRTLEQSVGEWLESIGLQQYESKLLLNGFDDVHFLGSNVMEEQDLRDIGISDPQHRRKLLQAARSLPKVKALGYDGNSPPSVPSWLDSLGLQDYVHSFLSSGYSSIDTVKNLWELELVNVLKVQLLGHRKRIIASLADRPYEEPPQKPPRFSQLRCQDLLSQTSSPLSQNDSCTGRSADLLLPPGDTGRRRHDSLHDPAAPSRAERFRIQEEHREAKLTLRPPSLAAPYAPVQSWQHQPEKLIFESCGYEANYLGSMLIKDLRGTESTQDACAKMRKSTEHMKKIPTIILSITYKGVKFIDASNKNVIAEHEIRNISCAAQDPEDLCTFAYITKDLQTSHHYCHVFSTVDVNLTYEIILTLGQAFEVAYQLALQAQKSRATGASAAEMIETKSSKPVPKPRVGVRKSALEPPDMDQDAQSHASVSWVVDPKPDSKRSLSTN
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------MGKEQELLE
------CCHHHHHHH
54.2112439753
3Ubiquitination-----MGKEQELLEA
-----CCHHHHHHHH
68.99-
21UbiquitinationGHLPAVEKLLSGKRL
CCCHHHHHHHCCCCC
48.40-
29PhosphorylationLLSGKRLSSGFGGGG
HHCCCCCCCCCCCCC
32.23101546335
30PhosphorylationLSGKRLSSGFGGGGG
HCCCCCCCCCCCCCC
42.6128674151
40PhosphorylationGGGGGGGSGGGGGGS
CCCCCCCCCCCCCCC
37.2228348404
181UbiquitinationDPTMRNNKFETPLDL
CCCCCCCCCCCHHHH
48.39-
215UbiquitinationLLSCNTKKHTPLHLA
CCCCCCCCCCCCHHH
51.15-
294UbiquitinationVRELPSQKSQQIAAL
HHHCCCHHHHHHHHH
55.35-
309UbiquitinationIEDHMTGKRSTKEVD
HHHHHCCCCCCCCCC
33.73-
318PhosphorylationSTKEVDKTPPPQPPL
CCCCCCCCCCCCCCC
36.2423401153
327PhosphorylationPPQPPLISSMDSISQ
CCCCCCCCCCHHHHH
27.5630266825
328PhosphorylationPQPPLISSMDSISQK
CCCCCCCCCHHHHHH
21.4423927012
331PhosphorylationPLISSMDSISQKSQG
CCCCCCHHHHHHCCC
18.5923927012
333PhosphorylationISSMDSISQKSQGDV
CCCCHHHHHHCCCHH
35.1923927012
336PhosphorylationMDSISQKSQGDVEKA
CHHHHHHCCCHHHHH
31.5828985074
372PhosphorylationYNAISCHSLDSMASG
HHHHHCCCHHHHHCC
37.8926074081
381PhosphorylationDSMASGRSSDQDSTN
HHHHCCCCCCCCCCH
41.6229116813
382PhosphorylationSMASGRSSDQDSTNK
HHHCCCCCCCCCCHH
37.6226657352
386PhosphorylationGRSSDQDSTNKEAEA
CCCCCCCCCHHHHHH
28.3923186163
387PhosphorylationRSSDQDSTNKEAEAA
CCCCCCCCHHHHHHC
59.6123186163
427PhosphorylationEDHIDKKYFPLTASE
CCCCCCCCCCCCHHH
19.0325106551
431PhosphorylationDKKYFPLTASEVLSM
CCCCCCCCHHHHHHC
28.5127251275
433PhosphorylationKYFPLTASEVLSMRP
CCCCCCHHHHHHCCC
24.0127251275
445PhosphorylationMRPRIHGSAAREEDE
CCCCCCCCCCCCCCC
12.4628796482
454PhosphorylationAREEDEHPYELLLTA
CCCCCCCCCEEEEEE
23.4217016520
455PhosphorylationREEDEHPYELLLTAE
CCCCCCCCEEEEEEC
22.5527273156
460PhosphorylationHPYELLLTAETKKVV
CCCEEEEEECCCEEE
23.5545561869
463PhosphorylationELLLTAETKKVVLVD
EEEEEECCCEEEEEC
33.4328152594
464UbiquitinationLLLTAETKKVVLVDG
EEEEECCCEEEEECC
34.77-
479PhosphorylationKTKDHRRSSSSRSQD
CCCCCCCCCCCCCCC
34.239847857
480PhosphorylationTKDHRRSSSSRSQDS
CCCCCCCCCCCCCCC
30.447658007
481PhosphorylationKDHRRSSSSRSQDSA
CCCCCCCCCCCCCCC
30.9011703631
482PhosphorylationDHRRSSSSRSQDSAE
CCCCCCCCCCCCCCC
37.5911704021
500PhosphorylationGQVPEQFSGLLHGSS
CCCCHHHHHHHCCCC
28.3826074081
506PhosphorylationFSGLLHGSSPVCEVG
HHHHHCCCCCCEECC
22.2626074081
507PhosphorylationSGLLHGSSPVCEVGQ
HHHHCCCCCCEECCC
26.4126074081
522PhosphorylationDPFQLLCTAGQSHPD
CHHHHHEECCCCCCC
33.5226074081
526PhosphorylationLLCTAGQSHPDGSPQ
HHEECCCCCCCCCCC
35.7526074081
531PhosphorylationGQSHPDGSPQQGACH
CCCCCCCCCCCCCCC
27.2426074081
541PhosphorylationQGACHKASMQLEETG
CCCCCHHHHHHHHHC
16.3226074081
563PhosphorylationQPSALDQSKRVGYLT
CCCHHCCCCCCCCCC
23.3028555341
568PhosphorylationDQSKRVGYLTGLPTT
CCCCCCCCCCCCCCC
9.7623403867
574PhosphorylationGYLTGLPTTNSRSHP
CCCCCCCCCCCCCCC
43.5925850435
575PhosphorylationYLTGLPTTNSRSHPE
CCCCCCCCCCCCCCC
29.2925850435
577PhosphorylationTGLPTTNSRSHPETL
CCCCCCCCCCCCCCC
32.8225850435
579PhosphorylationLPTTNSRSHPETLTH
CCCCCCCCCCCCCCC
43.1225849741
583PhosphorylationNSRSHPETLTHTASP
CCCCCCCCCCCCCCC
41.2129255136
585PhosphorylationRSHPETLTHTASPHP
CCCCCCCCCCCCCCC
25.3029255136
587PhosphorylationHPETLTHTASPHPGG
CCCCCCCCCCCCCCC
24.4829255136
589PhosphorylationETLTHTASPHPGGAE
CCCCCCCCCCCCCCC
25.5429255136
601PhosphorylationGAEEGDRSGARSRAP
CCCCCCCCCCCCCCC
41.3623403867
610PhosphorylationARSRAPPTSKPKAEL
CCCCCCCCCCCHHHH
48.6121406692
611PhosphorylationRSRAPPTSKPKAELK
CCCCCCCCCCHHHHH
53.3821406692
620PhosphorylationPKAELKLSRSLSKSD
CHHHHHHCHHCCCCH
20.4523401153
622PhosphorylationAELKLSRSLSKSDSD
HHHHHCHHCCCCHHH
33.3522167270
624PhosphorylationLKLSRSLSKSDSDLL
HHHCHHCCCCHHHCC
31.2122167270
626PhosphorylationLSRSLSKSDSDLLTC
HCHHCCCCHHHCCEE
38.6829255136
628PhosphorylationRSLSKSDSDLLTCSP
HHCCCCHHHCCEECC
36.9329255136
632PhosphorylationKSDSDLLTCSPTEDA
CCHHHCCEECCCCCC
20.4530266825
633CarbamidationSDSDLLTCSPTEDAT
CHHHCCEECCCCCCC
4.6517322306
634PhosphorylationDSDLLTCSPTEDATM
HHHCCEECCCCCCCC
29.6230266825
636PhosphorylationDLLTCSPTEDATMGS
HCCEECCCCCCCCCC
30.1523927012
640PhosphorylationCSPTEDATMGSRSES
ECCCCCCCCCCCCHH
34.0925159151
643PhosphorylationTEDATMGSRSESLSN
CCCCCCCCCCHHHCC
23.0823927012
645PhosphorylationDATMGSRSESLSNCS
CCCCCCCCHHHCCCC
32.9830266825
647PhosphorylationTMGSRSESLSNCSIG
CCCCCCHHHCCCCCC
38.0419664994
649PhosphorylationGSRSESLSNCSIGKK
CCCCHHHCCCCCCHH
45.1030266825
651CarbamidationRSESLSNCSIGKKRL
CCHHHCCCCCCHHHH
2.5617322306
652PhosphorylationSESLSNCSIGKKRLE
CHHHCCCCCCHHHHH
38.3319664994
660UbiquitinationIGKKRLEKSPSFASE
CCHHHHHCCCCHHHC
72.72-
661PhosphorylationGKKRLEKSPSFASEW
CHHHHHCCCCHHHCH
19.1922167270
663PhosphorylationKRLEKSPSFASEWDE
HHHHCCCCHHHCHHH
40.3022167270
666PhosphorylationEKSPSFASEWDEIEK
HCCCCHHHCHHHHHH
36.8930266825
676PhosphorylationDEIEKIMSSIGEGID
HHHHHHHHHHCCCCC
23.4430266825
677PhosphorylationEIEKIMSSIGEGIDF
HHHHHHHHHCCCCCH
19.7519664994
685PhosphorylationIGEGIDFSQERQKIS
HCCCCCHHHHHHHHC
27.6421815630
692PhosphorylationSQERQKISGLRTLEQ
HHHHHHHCCCHHHHH
38.5250565645
696PhosphorylationQKISGLRTLEQSVGE
HHHCCCHHHHHHHHH
39.4228632149
744PhosphorylationDLRDIGISDPQHRRK
HHHHHCCCCHHHHHH
37.7228188228
751UbiquitinationSDPQHRRKLLQAARS
CCHHHHHHHHHHHHC
54.21-
767PhosphorylationPKVKALGYDGNSPPS
CCCCCCCCCCCCCCC
22.8725627689
771PhosphorylationALGYDGNSPPSVPSW
CCCCCCCCCCCCCHH
43.6625159151
774PhosphorylationYDGNSPPSVPSWLDS
CCCCCCCCCCHHHHH
50.4725627689
828PhosphorylationHRKRIIASLADRPYE
CHHHHHHHHCCCCCC
17.4321945579
834PhosphorylationASLADRPYEEPPQKP
HHHCCCCCCCCCCCC
33.5421945579
845PhosphorylationPQKPPRFSQLRCQDL
CCCCCCHHHHHHHHH
29.5930804277
854PhosphorylationLRCQDLLSQTSSPLS
HHHHHHHHCCCCCCC
38.4150565637
856PhosphorylationCQDLLSQTSSPLSQN
HHHHHHCCCCCCCCC
28.0029396449
857PhosphorylationQDLLSQTSSPLSQND
HHHHHCCCCCCCCCC
23.4824719451
858PhosphorylationDLLSQTSSPLSQNDS
HHHHCCCCCCCCCCC
32.9921815630
870PhosphorylationNDSCTGRSADLLLPP
CCCCCCCCCCEECCC
27.7225850435
880PhosphorylationLLLPPGDTGRRRHDS
EECCCCCCCCCCCCC
38.2029255136
887PhosphorylationTGRRRHDSLHDPAAP
CCCCCCCCCCCCCCC
22.8323401153
895PhosphorylationLHDPAAPSRAERFRI
CCCCCCCCHHHHHCC
39.1225850435
912PhosphorylationEHREAKLTLRPPSLA
HHHHHCCCCCCCCCC
21.73101546343
917PhosphorylationKLTLRPPSLAAPYAP
CCCCCCCCCCCCCCC
33.0729523821
922PhosphorylationPPSLAAPYAPVQSWQ
CCCCCCCCCCCCCCC
20.8675325
927PhosphorylationAPYAPVQSWQHQPEK
CCCCCCCCCCCCCCC
29.0123312004
946PhosphorylationSCGYEANYLGSMLIK
HCCCCHHHHHHHHHH
21.3518452278
949PhosphorylationYEANYLGSMLIKDLR
CCHHHHHHHHHHHHC
14.0718452278
958PhosphorylationLIKDLRGTESTQDAC
HHHHHCCCCCHHHHH
21.9618452278
980PhosphorylationEHMKKIPTIILSITY
HHHHCCCEEEEEEEE
24.9126074081
984PhosphorylationKIPTIILSITYKGVK
CCCEEEEEEEECCCE
11.5026074081
986PhosphorylationPTIILSITYKGVKFI
CEEEEEEEECCCEEE
18.7926074081
987PhosphorylationTIILSITYKGVKFID
EEEEEEEECCCEEEC
12.2226074081
1074PhosphorylationQAQKSRATGASAAEM
HHHHHHHCCCCHHHH
31.9720873877
1077PhosphorylationKSRATGASAAEMIET
HHHHCCCCHHHHHHC
29.3820873877
1081SulfoxidationTGASAAEMIETKSSK
CCCCHHHHHHCCCCC
2.6221406390
1084PhosphorylationSAAEMIETKSSKPVP
CHHHHHHCCCCCCCC
25.8720873877
1086PhosphorylationAEMIETKSSKPVPKP
HHHHHCCCCCCCCCC
51.5220873877
1087PhosphorylationEMIETKSSKPVPKPR
HHHHCCCCCCCCCCC
42.4020873877
1100PhosphorylationPRVGVRKSALEPPDM
CCCCCCHHHCCCCCC
27.7681018479
1118PhosphorylationAQSHASVSWVVDPKP
HHHCCCEEEEECCCC
16.2024719451

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 ANS1A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANS1A_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 ANS1A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPHA8_HUMANEPHA8physical
20100865
P55G_HUMANPIK3R3physical
25814554
RHG10_HUMANARHGAP10physical
25814554
DOK3_HUMANDOK3physical
25814554
KLF15_HUMANKLF15physical
25814554
NHLC2_HUMANNHLRC2physical
25814554
MOD5_HUMANTRIT1physical
25814554
RANB3_HUMANRANBP3physical
25814554
RB_HUMANRB1physical
25814554
SMRD1_HUMANSMARCD1physical
25814554

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 ANS1A_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Cloning of a novel phosphotyrosine binding domain containingmolecule, Odin, involved in signaling by receptor tyrosine kinases.";
Pandey A., Blagoev B., Kratchmarova I., Fernandez M., Nielsen M.,Kristiansen T.Z., Ohara O., Podtelejnikov A.V., Roche S., Lodish H.F.,Mann M.;
Oncogene 21:8029-8036(2002).
Cited for: PROTEIN SEQUENCE OF 540-564, ACETYLATION AT GLY-2, MASS SPECTROMETRY,AND CHARACTERIZATION.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663 AND SER-677, ANDMASS SPECTROMETRY.
"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-647; SER-661 ANDSER-663, AND MASS SPECTROMETRY.
"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 THR-318; SER-622; SER-626;SER-647 AND SER-661, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-455, AND MASSSPECTROMETRY.

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