SPN90_HUMAN - dbPTM
SPN90_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPN90_HUMAN
UniProt AC Q9NZQ3
Protein Name NCK-interacting protein with SH3 domain
Gene Name NCKIPSD
Organism Homo sapiens (Human).
Sequence Length 722
Subcellular Localization Nucleus. Colocalizes with DRF1 at membrane ruffles, and with Nck at Z-disks in mature cardiac myocytes.
Protein Description Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1). Induces microspike formation, in vivo (By similarity). In vitro, stimulates N-WASP-induced ARP2/3 complex activation in the absence of CDC42 (By similarity). May play an important role in the maintenance of sarcomeres and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion. Plays a role in angiogenesis..
Protein Sequence MYRALYAFRSAEPNALAFAAGETFLVLERSSAHWWLAARARSGETGYVPPAYLRRLQGLEQDVLQAIDRAIEAVHNTAMRDGGKYSLEQRGVLQKLIHHRKETLSRRGPSASSVAVMTSSTSDHHLDAAAARQPNGVCRAGFERQHSLPSSEHLGADGGLYQIPLPSSQIPPQPRRAAPTTPPPPVKRRDREALMASGSGGHNTMPSGGNSVSSGSSVSSTSLDTLYTSSSPSEPGSSCSPTPPPVPRRGTHTTVSQVQPPPSKASAPEPPAEEEVATGTTSASDDLEALGTLSLGTTEEKAAAEAAVPRTIGAELMELVRRNTGLSHELCRVAIGIIVGHIQASVPASSPVMEQVLLSLVEGKDLSMALPSGQVCHDQQRLEVIFADLARRKDDAQQRSWALYEDEGVIRCYLEELLHILTDADPEVCKKMCKRNEFESVLALVAYYQMEHRASLRLLLLKCFGAMCSLDAAIISTLVSSVLPVELARDMQTDTQDHQKLCYSALILAMVFSMGEAVPYAHYEHLGTPFAQFLLNIVEDGLPLDTTEQLPDLCVNLLLALNLHLPAADQNVIMAALSKHANVKIFSEKLLLLLNRGDDPVRIFKHEPQPPHSVLKFLQDVFGSPATAAIFYHTDMMALIDITVRHIADLSPGDKLRMEYLSLMHAIVRTTPYLQHRHRLPDLQAILRRILNEEETSPQCQMDRMIVREMCKEFLVLGEAPS
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
6Ubiquitination--MYRALYAFRSAEP
--CCHHHHHHHCCCC		11.6022505724
30PhosphorylationTFLVLERSSAHWWLA
EEEEEECCCHHHHHH		23.6228634298
31PhosphorylationFLVLERSSAHWWLAA
EEEEECCCHHHHHHH		30.3028634298
42PhosphorylationWLAARARSGETGYVP
HHHHHHHCCCCCCCC		39.7424719451
45PhosphorylationARARSGETGYVPPAY
HHHHCCCCCCCCHHH		37.0224719451
47PhosphorylationARSGETGYVPPAYLR
HHCCCCCCCCHHHHH		19.7328634298
52PhosphorylationTGYVPPAYLRRLQGL
CCCCCHHHHHHHHCC		13.4024719451
84UbiquitinationTAMRDGGKYSLEQRG
HHCCCCCCCCHHHHH		36.8822505724
85PhosphorylationAMRDGGKYSLEQRGV
HCCCCCCCCHHHHHH		23.05-
95UbiquitinationEQRGVLQKLIHHRKE
HHHHHHHHHHHHHHH		45.2929967540
107MethylationRKETLSRRGPSASSV
HHHHHHHCCCCHHHE		58.98115484577
110PhosphorylationTLSRRGPSASSVAVM
HHHHCCCCHHHEEEE		43.5423927012
112PhosphorylationSRRGPSASSVAVMTS
HHCCCCHHHEEEEEC		29.6829978859
113PhosphorylationRRGPSASSVAVMTSS
HCCCCHHHEEEEECC		17.5129978859
118PhosphorylationASSVAVMTSSTSDHH
HHHEEEEECCCCCCH		16.9623927012
119PhosphorylationSSVAVMTSSTSDHHL
HHEEEEECCCCCCHH		17.3323927012
120PhosphorylationSVAVMTSSTSDHHLD
HEEEEECCCCCCHHH		23.8223401153
121PhosphorylationVAVMTSSTSDHHLDA
EEEEECCCCCCHHHH		37.6323927012
122PhosphorylationAVMTSSTSDHHLDAA
EEEECCCCCCHHHHH		36.5723927012
147 (in isoform 3)Phosphorylation-33.3728796482
147 (in isoform 4)Phosphorylation-33.3728796482
147PhosphorylationAGFERQHSLPSSEHL
CCCCCCCCCCCCCCC		33.3725159151
150 (in isoform 4)Phosphorylation-54.3628796482
150 (in isoform 3)Phosphorylation-54.3628796482
150PhosphorylationERQHSLPSSEHLGAD
CCCCCCCCCCCCCCC		54.3626657352
151 (in isoform 3)Phosphorylation-27.3928796482
151 (in isoform 4)Phosphorylation-27.3928796482
151PhosphorylationRQHSLPSSEHLGADG
CCCCCCCCCCCCCCC		27.3926657352
161PhosphorylationLGADGGLYQIPLPSS
CCCCCCCEECCCCHH		13.9928796482
161 (in isoform 3)Phosphorylation-13.9928796482
161 (in isoform 4)Phosphorylation-13.9928796482
167PhosphorylationLYQIPLPSSQIPPQP
CEECCCCHHHCCCCC		42.4227251275
168PhosphorylationYQIPLPSSQIPPQPR
EECCCCHHHCCCCCC		30.1427251275
174PhosphorylationSSQIPPQPRRAAPTT
HHHCCCCCCCCCCCC		33.2332645325
180PhosphorylationQPRRAAPTTPPPPVK
CCCCCCCCCCCCCCC		47.4030266825
181PhosphorylationPRRAAPTTPPPPVKR
CCCCCCCCCCCCCCC		32.5129255136
227PhosphorylationSTSLDTLYTSSSPSE
CCCCCEEEECCCCCC		13.48-
242PhosphorylationPGSSCSPTPPPVPRR
CCCCCCCCCCCCCCC		31.94-
249MethylationTPPPVPRRGTHTTVS
CCCCCCCCCCCCCCC		48.57115484585
251PhosphorylationPPVPRRGTHTTVSQV
CCCCCCCCCCCCCCC		17.7823663014
253PhosphorylationVPRRGTHTTVSQVQP
CCCCCCCCCCCCCCC		28.8223663014
254PhosphorylationPRRGTHTTVSQVQPP
CCCCCCCCCCCCCCC		15.5723663014
256PhosphorylationRGTHTTVSQVQPPPS
CCCCCCCCCCCCCCC		23.6523663014
263PhosphorylationSQVQPPPSKASAPEP
CCCCCCCCCCCCCCC		46.7823663014
264AcetylationQVQPPPSKASAPEPP
CCCCCCCCCCCCCCC		52.7326051181
294PhosphorylationLEALGTLSLGTTEEK
HHHHCCCCCCCHHHH		25.29-
311O-linked_GlycosylationAEAAVPRTIGAELME
HHHHCCHHHHHHHHH		20.0728657654
311PhosphorylationAEAAVPRTIGAELME
HHHHCCHHHHHHHHH		20.0720068231
367PhosphorylationLVEGKDLSMALPSGQ
HHCCCCHHHCCCCCC		16.4928555341
404PhosphorylationQQRSWALYEDEGVIR
HHHHHHHHCCCCHHH		17.37-
577UbiquitinationQNVIMAALSKHANVK
HHHHHHHHHCCCCCE		5.2129967540
582UbiquitinationAALSKHANVKIFSEK
HHHHCCCCCEEEHHH		35.0230230243
584UbiquitinationLSKHANVKIFSEKLL
HHCCCCCEEEHHHHH		37.5329967540
589UbiquitinationNVKIFSEKLLLLLNR
CCEEEHHHHHHHHHC		43.1430230243
651PhosphorylationVRHIADLSPGDKLRM
HHHHHCCCCCCHHHH		27.6424532841
673PhosphorylationAIVRTTPYLQHRHRL
HHHHHCHHHCHHHCC		19.53-
697PhosphorylationILNEEETSPQCQMDR
HCCCCCCCCCHHHHH		19.0928674419
702SulfoxidationETSPQCQMDRMIVRE
CCCCCHHHHHHHHHH		4.6721406390
712UbiquitinationMIVREMCKEFLVLGE
HHHHHHHHHHHHHCC		50.63-
722PhosphorylationLVLGEAPS-------
HHHCCCCC-------		60.9628060719
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
161YPhosphorylationKinaseSRCP12931
PSP
227YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPN90_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 SPN90_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DMRTB_HUMANDMRTB1physical
16189514
DIAP3_HUMANDIAPH3physical
11509578
GRB2_HUMANGRB2physical
11157975
NCK1_HUMANNCK1physical
11278500
FCSD1_HUMANFCHSD1physical
28514442
ITSN2_HUMANITSN2physical
28514442
PALLD_HUMANPALLDphysical
28514442
GAS7_HUMANGAS7physical
28514442
ARHG6_HUMANARHGEF6physical
28514442
NCK1_HUMANNCK1physical
28514442
GIT1_HUMANGIT1physical
28514442
GIT2_HUMANGIT2physical
28514442
ARHG7_HUMANARHGEF7physical
28514442
ZFYV9_HUMANZFYVE9physical
28514442
PLCG1_HUMANPLCG1physical
28514442
ITSN1_HUMANITSN1physical
28514442
RFIP5_HUMANRAB11FIP5physical
28514442
EP15R_HUMANEPS15L1physical
28514442
GEMI8_HUMANGEMIN8physical
28514442
SNX33_HUMANSNX33physical
28514442
RBM15_HUMANRBM15physical
28514442
USP9Y_HUMANUSP9Yphysical
28514442
RB15B_HUMANRBM15Bphysical
28514442
NCK2_HUMANNCK2physical
28514442
BAIP2_HUMANBAIAP2physical
28514442
DACH1_HUMANDACH1physical
28514442
GEMI6_HUMANGEMIN6physical
28514442
GEMI2_HUMANGEMIN2physical
28514442
GRB2_HUMANGRB2physical
28514442
KC1A_HUMANCSNK1A1physical
28514442
JUN_HUMANJUNphysical
28514442
ARMC8_HUMANARMC8physical
28514442
PDD2L_HUMANPDCD2Lphysical
28514442
FBX28_HUMANFBXO28physical
28514442
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 SPN90_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-181, AND MASSSPECTROMETRY.

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