ADIP_HUMAN - dbPTM
ADIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADIP_HUMAN
UniProt AC Q9Y2D8
Protein Name Afadin- and alpha-actinin-binding protein
Gene Name SSX2IP
Organism Homo sapiens (Human).
Sequence Length 614
Subcellular Localization Cell junction, adherens junction. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite . Cytoplasm, cytoskeleton, cilium basal body . Not found at cell-matrix AJs..
Protein Description Belongs to an adhesion system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). May connect the nectin-afadin and E-cadherin-catenin system through alpha-actinin and may be involved in organization of the actin cytoskeleton at AJs through afadin and alpha-actinin (By similarity). Involved in cell movement: localizes at the leading edge of moving cells in response to PDGF and is required for the formation of the leading edge and the promotion of cell movement, possibly via activation of Rac signaling (By similarity). Acts as a centrosome maturation factor, probably by maintaining the integrity of the pericentriolar material and proper microtubule nucleation at mitotic spindle poles. The function seems to implicate at least in part WRAP73; the SSX2IP:WRAP73 complex is proposed to act as regulator of spindle anchoring at the mitotic centrosome. [PubMed: 23816619]
Protein Sequence MGDWMTVTDPGLSSESKTISQYTSETKMSPSSLYSQQVLCSSIPLSKNVHSFFSAFCTEDNIEQSISYLDQELTTFGFPSLYEESKGKETKRELNIVAVLNCMNELLVLQRKNLLAQENVETQNLKLGSDMDHLQSCYSKLKEQLETSRREMIGLQERDRQLQCKNRNLHQLLKNEKDEVQKLQNIIASRATQYNHDMKRKEREYNKLKERLHQLVMNKKDKKIAMDILNYVGRADGKRGSWRTGKTEARNEDEMYKILLNDYEYRQKQILMENAELKKVLQQMKKEMISLLSPQKKKPRERVDDSTGTVISDVEEDAGELSRESMWDLSCETVREQLTNSIRKQWRILKSHVEKLDNQVSKVHLEGFNDEDVISRQDHEQETEKLELEIQQCKEMIKTQQQLLQQQLATAYDDDTTSLLRDCYLLEEKERLKEEWSLFKEQKKNFERERRSFTEAAIRLGLERKAFEEERASWLKQQFLNMTTFDHQNSENVKLFSAFSGSSDWDNLIVHSRQPQKKPHSVSNGSPVCMSKLTKSLPASPSTSDFCQTRSCISEHSSINVLNITAEEIKPNQVGGECTNQKWSVASRPGSQEGCYSGCSLSYTNSHVEKDDLP
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
2 (in isoform 3)Phosphorylation-36.9724719451
4 (in isoform 3)Phosphorylation-4.4227251275
6Phosphorylation--MGDWMTVTDPGLS
--CCCCCCCCCCCCC		18.9229759185
8PhosphorylationMGDWMTVTDPGLSSE
CCCCCCCCCCCCCCC		27.5829759185
16PhosphorylationDPGLSSESKTISQYT
CCCCCCCCCCHHHHC		36.7329759185
18PhosphorylationGLSSESKTISQYTSE
CCCCCCCCHHHHCCC		34.83-
29PhosphorylationYTSETKMSPSSLYSQ
HCCCCCCCHHHHHHC		24.1629978859
31PhosphorylationSETKMSPSSLYSQQV
CCCCCCHHHHHHCHH		26.1829978859
32PhosphorylationETKMSPSSLYSQQVL
CCCCCHHHHHHCHHH		34.4129978859
34PhosphorylationKMSPSSLYSQQVLCS
CCCHHHHHHCHHHHC		13.3327251275
35PhosphorylationMSPSSLYSQQVLCSS
CCHHHHHHCHHHHCC		21.3029978859
112 (in isoform 1)Ubiquitination-38.7021890473
112UbiquitinationELLVLQRKNLLAQEN
HHHHHHHHHHHHHCC		38.7021890473
112UbiquitinationELLVLQRKNLLAQEN
HHHHHHHHHHHHHCC		38.7021890473
112 (in isoform 2)Ubiquitination-38.7021890473
126UbiquitinationNVETQNLKLGSDMDH
CHHHCCCCCCCCHHH		59.35-
129PhosphorylationTQNLKLGSDMDHLQS
HCCCCCCCCHHHHHH		39.9526552605
136PhosphorylationSDMDHLQSCYSKLKE
CCHHHHHHHHHHHHH		22.7626552605
138PhosphorylationMDHLQSCYSKLKEQL
HHHHHHHHHHHHHHH		17.6826552605
139PhosphorylationDHLQSCYSKLKEQLE
HHHHHHHHHHHHHHH		35.5226552605
142UbiquitinationQSCYSKLKEQLETSR
HHHHHHHHHHHHHHH		47.34-
174UbiquitinationRNLHQLLKNEKDEVQ
CCHHHHHHCCHHHHH		72.20-
182UbiquitinationNEKDEVQKLQNIIAS
CCHHHHHHHHHHHHH		58.16-
192PhosphorylationNIIASRATQYNHDMK
HHHHHHHHHCHHHHH		30.4025003641
219UbiquitinationLHQLVMNKKDKKIAM
HHHHHCCCCCHHHHH		44.23-
231PhosphorylationIAMDILNYVGRADGK
HHHHHHHHHHCCCCC		10.8023403867
257UbiquitinationRNEDEMYKILLNDYE
CCHHHHHHHHHCCHH		26.10-
268UbiquitinationNDYEYRQKQILMENA
CCHHHHHHHHHHHHH		30.24-
290PhosphorylationQMKKEMISLLSPQKK
HHHHHHHHHHCCCCC		23.1930266825
293PhosphorylationKEMISLLSPQKKKPR
HHHHHHHCCCCCCCC		30.4930266825
306PhosphorylationPRERVDDSTGTVISD
CCHHCCCCCCCEEEC		25.0329255136
307PhosphorylationRERVDDSTGTVISDV
CHHCCCCCCCEEECH		43.8129255136
309PhosphorylationRVDDSTGTVISDVEE
HCCCCCCCEEECHHH		18.1129255136
312PhosphorylationDSTGTVISDVEEDAG
CCCCCEEECHHHHHC		31.1319664994
322PhosphorylationEEDAGELSRESMWDL
HHHHCCCCHHHHHHH		29.6928176443
325PhosphorylationAGELSRESMWDLSCE
HCCCCHHHHHHHCHH		24.8622817900
339PhosphorylationETVREQLTNSIRKQW
HHHHHHHHHHHHHHH		26.9819691289
341PhosphorylationVREQLTNSIRKQWRI
HHHHHHHHHHHHHHH		20.6625159151
350UbiquitinationRKQWRILKSHVEKLD
HHHHHHHHHHHHHHH		35.82-
351PhosphorylationKQWRILKSHVEKLDN
HHHHHHHHHHHHHHH		29.3528102081
355UbiquitinationILKSHVEKLDNQVSK
HHHHHHHHHHHCCEE		61.11-
362 (in isoform 1)Ubiquitination-34.5121890473
362UbiquitinationKLDNQVSKVHLEGFN
HHHHCCEEEHHCCCC		34.5121906983
362 (in isoform 2)Ubiquitination-34.5121890473
394UbiquitinationELEIQQCKEMIKTQQ
HHHHHHHHHHHHHHH		46.08-
398 (in isoform 2)Ubiquitination-38.6821890473
398UbiquitinationQQCKEMIKTQQQLLQ
HHHHHHHHHHHHHHH		38.6821906983
398 (in isoform 1)Ubiquitination-38.6821890473
418PhosphorylationAYDDDTTSLLRDCYL
HCCCCHHHHHHHHHH		27.7424719451
429UbiquitinationDCYLLEEKERLKEEW
HHHHHHHHHHHHHHH		38.47-
433UbiquitinationLEEKERLKEEWSLFK
HHHHHHHHHHHHHHH		60.86-
437PhosphorylationERLKEEWSLFKEQKK
HHHHHHHHHHHHHHH		27.4924719451
440UbiquitinationKEEWSLFKEQKKNFE
HHHHHHHHHHHHHHH		65.61-
452PhosphorylationNFERERRSFTEAAIR
HHHHHHHHHHHHHHH		42.6221712546
454PhosphorylationERERRSFTEAAIRLG
HHHHHHHHHHHHHHC		26.4319691289
476 (in isoform 1)Ubiquitination-35.4821890473
476UbiquitinationEERASWLKQQFLNMT
HHHHHHHHHHHHCCC		35.4821890473
476UbiquitinationEERASWLKQQFLNMT
HHHHHHHHHHHHCCC		35.4821890473
476 (in isoform 2)Ubiquitination-35.4821890473
483PhosphorylationKQQFLNMTTFDHQNS
HHHHHCCCCCCCCCC		24.2028111955
484PhosphorylationQQFLNMTTFDHQNSE
HHHHCCCCCCCCCCC		19.1228111955
490PhosphorylationTTFDHQNSENVKLFS
CCCCCCCCCCEEEEE		24.7928111955
500PhosphorylationVKLFSAFSGSSDWDN
EEEEEECCCCCCCCC		37.1723186163
502PhosphorylationLFSAFSGSSDWDNLI
EEEECCCCCCCCCEE		24.7523186163
503PhosphorylationFSAFSGSSDWDNLIV
EEECCCCCCCCCEEE		46.3623186163
521PhosphorylationQPQKKPHSVSNGSPV
CCCCCCCCCCCCCCC		35.4527251275
523PhosphorylationQKKPHSVSNGSPVCM
CCCCCCCCCCCCCCH		38.1924719451
526PhosphorylationPHSVSNGSPVCMSKL
CCCCCCCCCCCHHHH		20.5728985074
534PhosphorylationPVCMSKLTKSLPASP
CCCHHHHCCCCCCCC		23.4830624053
535UbiquitinationVCMSKLTKSLPASPS
CCHHHHCCCCCCCCC		61.50-
536PhosphorylationCMSKLTKSLPASPST
CHHHHCCCCCCCCCC		34.0625159151
540PhosphorylationLTKSLPASPSTSDFC
HCCCCCCCCCCCHHH		19.9025159151
542PhosphorylationKSLPASPSTSDFCQT
CCCCCCCCCCHHHCC		37.7422617229
543PhosphorylationSLPASPSTSDFCQTR
CCCCCCCCCHHHCCH		35.3827794612
544PhosphorylationLPASPSTSDFCQTRS
CCCCCCCCHHHCCHH		32.7827794612
549PhosphorylationSTSDFCQTRSCISEH
CCCHHHCCHHHHCCC		26.2320068231
565PhosphorylationSINVLNITAEEIKPN
CEEEEEEEHHHCCCC		27.2619007248
582AcetylationGGECTNQKWSVASRP
CCCCCCCCCEEECCC		43.4310652607
584PhosphorylationECTNQKWSVASRPGS
CCCCCCCEEECCCCC		18.1627251275
587PhosphorylationNQKWSVASRPGSQEG
CCCCEEECCCCCCCC		36.5330576142
591PhosphorylationSVASRPGSQEGCYSG
EEECCCCCCCCCCCC		27.9530576142
596PhosphorylationPGSQEGCYSGCSLSY
CCCCCCCCCCCCCEE		20.9626471730
597PhosphorylationGSQEGCYSGCSLSYT
CCCCCCCCCCCCEEC		37.0828985074
600PhosphorylationEGCYSGCSLSYTNSH
CCCCCCCCCEECCCC		24.7129449344
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 ADIP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADIP_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 ADIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AFAD_HUMANMLLT4physical
12446711
ACTN1_HUMANACTN1physical
12446711
1433Z_HUMANYWHAZphysical
21988832
1433T_HUMANYWHAQphysical
21988832
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
ADIP_HUMANSSX2IPphysical
25416956
MORN4_HUMANMORN4physical
25416956
FRMD6_HUMANFRMD6physical
25416956
K1C40_HUMANKRT40physical
25416956
ZN792_HUMANZNF792physical
25416956
ZN417_HUMANZNF417physical
25416956
ZMAT2_HUMANZMAT2physical
25416956
TRI42_HUMANTRIM42physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
BRCA1_HUMANBRCA1physical
25184681
PCM1_HUMANPCM1physical
26638075
PTCD3_HUMANPTCD3physical
26638075
IPO7_HUMANIPO7physical
26638075
CP131_HUMANCEP131physical
26638075
MIB1_HUMANMIB1physical
26638075
WRP73_HUMANWRAP73physical
26638075
TBA1A_HUMANTUBA1Aphysical
26638075
NP1L4_HUMANNAP1L4physical
26638075
TBB2A_HUMANTUBB2Aphysical
26638075
CC138_HUMANCCDC138physical
26638075
DNJA3_HUMANDNAJA3physical
26638075
CCAR1_HUMANCCAR1physical
26638075
NTPCR_HUMANNTPCRphysical
26638075
NUMA1_HUMANNUMA1physical
26638075
SCLT1_HUMANSCLT1physical
26638075
RCN1_HUMANRCN1physical
26638075
SREK1_HUMANSREK1physical
26638075
AKTIP_HUMANAKTIPphysical
26638075
CAMP1_HUMANCAMSAP1physical
26638075
CC85C_HUMANCCDC85Cphysical
26638075
TCPH_HUMANCCT7physical
26638075
CENPH_HUMANCENPHphysical
26638075
CE350_HUMANCEP350physical
26638075
CEP55_HUMANCEP55physical
26638075
CEP85_HUMANCEP85physical
26638075
CKAP2_HUMANCKAP2physical
26638075
DVL1_HUMANDVL1physical
26638075
DVL2_HUMANDVL2physical
26638075
DVL3_HUMANDVL3physical
26638075
ECH1_HUMANECH1physical
26638075
F120A_HUMANFAM120Aphysical
26638075
WAC2A_HUMANFAM21Aphysical
26638075
FMR1_HUMANFMR1physical
26638075
GPTC1_HUMANGPATCH1physical
26638075
HAUS3_HUMANHAUS3physical
26638075
HAUS4_HUMANHAUS4physical
26638075
HAUS6_HUMANHAUS6physical
26638075
HAUS8_HUMANHAUS8physical
26638075
HOOK3_HUMANHOOK3physical
26638075
IFT74_HUMANIFT74physical
26638075
KANK2_HUMANKANK2physical
26638075
KTNA1_HUMANKATNA1physical
26638075
KTNB1_HUMANKATNB1physical
26638075
MOONR_HUMANKIAA0753physical
26638075
K1671_HUMANKIAA1671physical
26638075
LRC49_HUMANLRRC49physical
26638075
LUZP1_HUMANLUZP1physical
26638075
NEDD1_HUMANNEDD1physical
26638075
OFD1_HUMANOFD1physical
26638075
PIBF1_HUMANPIBF1physical
26638075
PKHG1_HUMANPLEKHG1physical
26638075
ASPP1_HUMANPPP1R13Bphysical
26638075
RINT1_HUMANRINT1physical
26638075
SDCG3_HUMANSDCCAG3physical
26638075
TCHP_HUMANTCHPphysical
26638075
TNR6B_HUMANTNRC6Bphysical
26638075
P53_HUMANTP53physical
26638075
ASPP2_HUMANTP53BP2physical
26638075
TPGS1_HUMANTPGS1physical
26638075
TRI26_HUMANTRIM26physical
26638075
TTK_HUMANTTKphysical
26638075
TXLNG_HUMANTXLNGphysical
26638075
WDR83_HUMANWDR83physical
26638075
XRN1_HUMANXRN1physical
26638075
ABLM1_HUMANABLIM1physical
26638075
PUR8_HUMANADSLphysical
26638075
AHI1_HUMANAHI1physical
26638075
CS025_HUMANC19orf25physical
26638075
CNOT1_HUMANCNOT1physical
26638075
CSPP1_HUMANCSPP1physical
26638075
DHX35_HUMANDHX35physical
26638075
4ET_HUMANEIF4ENIF1physical
26638075
HAUS1_HUMANHAUS1physical
26638075
IPO8_HUMANIPO8physical
26638075
IRAK1_HUMANIRAK1physical
26638075
KIF7_HUMANKIF7physical
26638075
LIMD1_HUMANLIMD1physical
26638075
MA7D3_HUMANMAP7D3physical
26638075
NDEL1_HUMANNDEL1physical
26638075
NDK7_HUMANNME7physical
26638075
OCRL_HUMANOCRLphysical
26638075
PDLI5_HUMANPDLIM5physical
26638075
PTAR1_HUMANPTAR1physical
26638075
SC24B_HUMANSEC24Bphysical
26638075
SI1L2_HUMANSIPA1L2physical
26638075
SMG7_HUMANSMG7physical
26638075
TAB1_HUMANTAB1physical
26638075
TBK1_HUMANTBK1physical
26638075
TNIP1_HUMANTNIP1physical
26638075
TNR6A_HUMANTNRC6Aphysical
26638075
TNR6C_HUMANTNRC6Cphysical
26638075
TRI37_HUMANTRIM37physical
26638075
TRIM9_HUMANTRIM9physical
26638075
TRIP6_HUMANTRIP6physical
26638075
VCIP1_HUMANVCPIP1physical
26638075
TBC31_HUMANTBC1D31physical
26638075
ZFY26_HUMANZFYVE26physical
21516116
ZNF71_HUMANZNF71physical
21516116
NIF3L_HUMANNIF3L1physical
21516116
ZGPAT_HUMANZGPATphysical
21516116
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 ADIP_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-312, AND MASSSPECTROMETRY.
"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-312; SER-536 ANDSER-540, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-339; SER-341; SER-540AND THR-565, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-325, ANDMASS SPECTROMETRY.

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