SALL2_HUMAN - dbPTM
SALL2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SALL2_HUMAN
UniProt AC Q9Y467
Protein Name Sal-like protein 2
Gene Name SALL2
Organism Homo sapiens (Human).
Sequence Length 1007
Subcellular Localization Nucleus .
Protein Description Probable transcription factor that plays a role in eye development before, during, and after optic fissure closure..
Protein Sequence MSRRKQRKPQQLISDCEGPSASENGDASEEDHPQVCAKCCAQFTDPTEFLAHQNACSTDPPVMVIIGGQENPNNSSASSEPRPEGHNNPQVMDTEHSNPPDSGSSVPTDPTWGPERRGEESPGHFLVAATGTAAGGGGGLILASPKLGATPLPPESTPAPPPPPPPPPPPGVGSGHLNIPLILEELRVLQQRQIHQMQMTEQICRQVLLLGSLGQTVGAPASPSELPGTGTASSTKPLLPLFSPIKPVQTSKTLASSSSSSSSSSGAETPKQAFFHLYHPLGSQHPFSAGGVGRSHKPTPAPSPALPGSTDQLIASPHLAFPSTTGLLAAQCLGAARGLEATASPGLLKPKNGSGELSYGEVMGPLEKPGGRHKCRFCAKVFGSDSALQIHLRSHTGERPYKCNVCGNRFTTRGNLKVHFHRHREKYPHVQMNPHPVPEHLDYVITSSGLPYGMSVPPEKAEEEAATPGGGVERKPLVASTTALSATESLTLLSTSAGTATAPGLPAFNKFVLMKAVEPKNKADENTPPGSEGSAISGVAESSTATRMQLSKLVTSLPSWALLTNHFKSTGSFPFPYVLEPLGASPSETSKLQQLVEKIDRQGAVAVTSAASGAPTTSAPAPSSSASSGPNQCVICLRVLSCPRALRLHYGQHGGERPFKCKVCGRAFSTRGNLRAHFVGHKASPAARAQNSCPICQKKFTNAVTLQQHVRMHLGGQIPNGGTALPEGGGAAQENGSEQSTVSGAGSFPQQQSQQPSPEEELSEEEEEEDEEEEEDVTDEDSLAGRGSESGGEKAISVRGDSEEASGAEEEVGTVAAAATAGKEMDSNEKTTQQSSLPPPPPPDSLDQPQPMEQGSSGVLGGKEEGGKPERSSSPASALTPEGEATSVTLVEELSLQEAMRKEPGESSSRKACEVCGQAFPSQAALEEHQKTHPKEGPLFTCVFCRQGFLERATLKKHMLLAHHQVQPFAPHGPQNIAALSLVPGCSPSITSTGLSPFPRKDDPTIP
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
14PhosphorylationRKPQQLISDCEGPSA
CCCHHHHHCCCCCCC		44.8121406692
20PhosphorylationISDCEGPSASENGDA
HHCCCCCCCCCCCCC		56.1121406692
22PhosphorylationDCEGPSASENGDASE
CCCCCCCCCCCCCCC		35.6121406692
26 (in isoform 3)Phosphorylation-59.5127732954
28PhosphorylationASENGDASEEDHPQV
CCCCCCCCCCCCHHH		46.3821406692
121PhosphorylationPERRGEESPGHFLVA
CCCCCCCCCCEEEEE		31.7024173317
144PhosphorylationGGGLILASPKLGATP
CCCEEEECCCCCCCC		21.0824173317
222PhosphorylationQTVGAPASPSELPGT
CCCCCCCCHHHCCCC		28.0924173317
224PhosphorylationVGAPASPSELPGTGT
CCCCCCHHHCCCCCC		49.6327251275
243PhosphorylationKPLLPLFSPIKPVQT
CCCCCCCCCCCCCCC		33.1428348404
246UbiquitinationLPLFSPIKPVQTSKT
CCCCCCCCCCCCCCE		42.3921890473
250PhosphorylationSPIKPVQTSKTLASS
CCCCCCCCCCEECCC		32.2122199227
251PhosphorylationPIKPVQTSKTLASSS
CCCCCCCCCEECCCC		13.4222199227
253O-linked_GlycosylationKPVQTSKTLASSSSS
CCCCCCCEECCCCCC		27.5922661428
253PhosphorylationKPVQTSKTLASSSSS
CCCCCCCEECCCCCC		27.5930576142
256O-linked_GlycosylationQTSKTLASSSSSSSS
CCCCEECCCCCCCCC		33.5922661428
258PhosphorylationSKTLASSSSSSSSSS
CCEECCCCCCCCCCC		31.5730576142
259PhosphorylationKTLASSSSSSSSSSG
CEECCCCCCCCCCCC		35.87-
260PhosphorylationTLASSSSSSSSSSGA
EECCCCCCCCCCCCC		35.87-
261PhosphorylationLASSSSSSSSSSGAE
ECCCCCCCCCCCCCC		35.8730576142
263O-linked_GlycosylationSSSSSSSSSSGAETP
CCCCCCCCCCCCCCH		30.3922661428
269PhosphorylationSSSSGAETPKQAFFH
CCCCCCCCHHHHEEH		34.9419664995
344PhosphorylationRGLEATASPGLLKPK
HCCCCCCCCCCCCCC		18.3629978859
349UbiquitinationTASPGLLKPKNGSGE
CCCCCCCCCCCCCCC		60.01-
354PhosphorylationLLKPKNGSGELSYGE
CCCCCCCCCCCCCEE		38.1926074081
358PhosphorylationKNGSGELSYGEVMGP
CCCCCCCCCEEEECC		27.1326074081
384PhosphorylationFCAKVFGSDSALQIH
HHHEHHCCCCEEEEE		19.5423186163
386PhosphorylationAKVFGSDSALQIHLR
HEHHCCCCEEEEEEE		32.3523186163
394PhosphorylationALQIHLRSHTGERPY
EEEEEEECCCCCCCE		31.5924719451
396PhosphorylationQIHLRSHTGERPYKC
EEEEECCCCCCCEEE		41.8227251275
413MethylationCGNRFTTRGNLKVHF
CCCCEECCCCEEEEE		29.01115493223
467PhosphorylationKAEEEAATPGGGVER
HHHHHCCCCCCCCCC		29.5224173317
515UbiquitinationFNKFVLMKAVEPKNK
HCEEEEEECCCCCCC		45.15-
522UbiquitinationKAVEPKNKADENTPP
ECCCCCCCCCCCCCC		64.44-
527O-linked_GlycosylationKNKADENTPPGSEGS
CCCCCCCCCCCCCCC		28.9022661428
531O-linked_GlycosylationDENTPPGSEGSAISG
CCCCCCCCCCCCHHC		44.5522661428
534O-linked_GlycosylationTPPGSEGSAISGVAE
CCCCCCCCCHHCCCC		20.5522661428
542PhosphorylationAISGVAESSTATRMQ
CHHCCCCCCHHHHHH		24.2123879269
544PhosphorylationSGVAESSTATRMQLS
HCCCCCCHHHHHHHH		41.13-
546PhosphorylationVAESSTATRMQLSKL
CCCCCHHHHHHHHHH		27.11-
585PhosphorylationVLEPLGASPSETSKL
EEECCCCCHHHHHHH		27.4524173317
587PhosphorylationEPLGASPSETSKLQQ
ECCCCCHHHHHHHHH		51.52-
591UbiquitinationASPSETSKLQQLVEK
CCHHHHHHHHHHHHH		58.70-
598UbiquitinationKLQQLVEKIDRQGAV
HHHHHHHHHHHCCCE		42.29-
609PhosphorylationQGAVAVTSAASGAPT
CCCEEEEECCCCCCC		18.4218669648
616PhosphorylationSAASGAPTTSAPAPS
ECCCCCCCCCCCCCC		32.6118669648
623PhosphorylationTTSAPAPSSSASSGP
CCCCCCCCCCCCCCC		38.7418669648
641PhosphorylationVICLRVLSCPRALRL
EEEEEECCCCCHHHC		21.1524719451
650PhosphorylationPRALRLHYGQHGGER
CCHHHCCCCCCCCCC		24.07-
684PhosphorylationHFVGHKASPAARAQN
EECCCCCCHHHHHHC		21.6321406692
797PhosphorylationSGGEKAISVRGDSEE
CCCCCEEEEECCCHH		15.6030631047
802PhosphorylationAISVRGDSEEASGAE
EEEEECCCHHHCCCH		39.9119664994
806PhosphorylationRGDSEEASGAEEEVG
ECCCHHHCCCHHHHH		41.6419664994
814PhosphorylationGAEEEVGTVAAAATA
CCHHHHHHHHHHHHC		16.4930266825
820PhosphorylationGTVAAAATAGKEMDS
HHHHHHHHCCCCCCC		31.0821406692
823AcetylationAAAATAGKEMDSNEK
HHHHHCCCCCCCCCC		47.6111923025
835PhosphorylationNEKTTQQSSLPPPPP
CCCCCCCCCCCCCCC		24.8322210691
857PhosphorylationQPMEQGSSGVLGGKE
CCCCCCCCCCCCCCC		39.4822210691
872PhosphorylationEGGKPERSSSPASAL
CCCCCCCCCCCCCCC		33.2430278072
873PhosphorylationGGKPERSSSPASALT
CCCCCCCCCCCCCCC		46.7130278072
874PhosphorylationGKPERSSSPASALTP
CCCCCCCCCCCCCCC		26.2326074081
877PhosphorylationERSSSPASALTPEGE
CCCCCCCCCCCCCCC		27.4826074081
880PhosphorylationSSPASALTPEGEATS
CCCCCCCCCCCCCCE		21.0028464451
886PhosphorylationLTPEGEATSVTLVEE
CCCCCCCCEEEEEHH		21.3021406692
887PhosphorylationTPEGEATSVTLVEEL
CCCCCCCEEEEEHHH		21.8321406692
889PhosphorylationEGEATSVTLVEELSL
CCCCCEEEEEHHHHH		25.5028464451
895PhosphorylationVTLVEELSLQEAMRK
EEEEHHHHHHHHHHH		31.1427251275
907PhosphorylationMRKEPGESSSRKACE
HHHCCCCCHHHHHHH		39.2621406692
908PhosphorylationRKEPGESSSRKACEV
HHCCCCCHHHHHHHH		29.8421406692
909PhosphorylationKEPGESSSRKACEVC
HCCCCCHHHHHHHHH		47.2621406692
911UbiquitinationPGESSSRKACEVCGQ
CCCCHHHHHHHHHCC		60.3718655026
954PhosphorylationQGFLERATLKKHMLL
CCHHHHHHHHHHHHH		45.38-
996PhosphorylationSITSTGLSPFPRKDD
CCCCCCCCCCCCCCC		26.3224719451
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 SALL2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SALL2_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 SALL2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEP76_HUMANCEP76physical
16189514
ZMIZ2_HUMANZMIZ2physical
16189514
DDB1_HUMANDDB1physical
21228219
CUL4A_HUMANCUL4Aphysical
21228219
CUL4B_HUMANCUL4Bphysical
21228219
ATL4_HUMANADAMTSL4physical
19060904
CEP76_HUMANCEP76physical
25416956
ZMIZ2_HUMANZMIZ2physical
25416956
ATG2B_HUMANATG2Bphysical
28514442
ZMYM1_HUMANZMYM1physical
28514442
PTCD2_HUMANPTCD2physical
28514442
GFPT2_HUMANGFPT2physical
28514442
WIPI4_HUMANWDR45physical
28514442
TBB3_HUMANTUBB3physical
28514442
COT2_HUMANNR2F2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
216820Coloboma, ocular, autosomal recessive (COAR)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SALL2_HUMAN

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Related Literatures of Post-Translational Modification
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-797; SER-802 ANDSER-806, AND MASS 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-802 AND SER-806, ANDMASS 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 SER-609; THR-616 ANDSER-623, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Proteomic analysis of ubiquitinated proteins in normal hepatocytecell line Chang liver cells.";
Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
Proteomics 8:2885-2896(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-911, AND MASSSPECTROMETRY.

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