AR6P4_HUMAN - dbPTM
AR6P4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AR6P4_HUMAN
UniProt AC Q66PJ3
Protein Name ADP-ribosylation factor-like protein 6-interacting protein 4
Gene Name ARL6IP4
Organism Homo sapiens (Human).
Sequence Length 421
Subcellular Localization Nucleus, nucleolus . Nucleus speckle .
Protein Description Involved in modulating alternative pre-mRNA splicing with either 5' distal site activation or preferential use of 3' proximal site. In case of infection by Herpes simplex virus (HSVI), may act as a splicing inhibitor of HSVI pre-mRNA..
Protein Sequence MPRCTYQLEQNPGFLPDGPGVHARAHCQDLSGPYGHEFATSESLGGRVGKTRAPQSGARSRMERAGPAGEEGGAREGRLLPRAPGAWVLRACAERAALEVGAASADTGVRGCGARGPAPLLASAGGGRARDGTWGVRTKGSGAALPSRPASRAAPRPEASSPPLPLEKARGGLSGPQGGRARGAMAHVGSRKRSRSRSRSRGRGSEKRKKKSRKDTSRNCSASTSQGRKASTAPGAEASPSPCITERSKQKARRRTRSSSSSSSSSSSSSSSSSSSSSSSSSDGRKKRGKYKDKRRKKKKKRKKLKKKGKEKAEAQQVEALPGPSLDQWHRSAGEEEDGPVLTDEQKSRIQAMKPMTKEEWDARQSIIRKVVDPETGRTRLIKGDGEVLEEIVTKERHREINKQATRGDCLAFQMRAGLLP
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
37 (in isoform 7)Phosphorylation-5.5229978859
39 (in isoform 7)Phosphorylation-7.0429978859
40 (in isoform 7)Phosphorylation-13.1729978859
41 (in isoform 7)Phosphorylation-11.9229978859
44 (in isoform 7)Phosphorylation-17.4123927012
46 (in isoform 7)Phosphorylation-36.9725849741
50 (in isoform 7)Phosphorylation-16.2929978859
104PhosphorylationALEVGAASADTGVRG
HHHHCCCCCCCCCCC		44.2228258704
107PhosphorylationVGAASADTGVRGCGA
HCCCCCCCCCCCCCC		51.5828258704
117UbiquitinationRGCGARGPAPLLASA
CCCCCCCCCCCEEEC		30.5929967540
129PhosphorylationASAGGGRARDGTWGV
EECCCCCCCCCCCCC		33.2732142685
137PhosphorylationRDGTWGVRTKGSGAA
CCCCCCCEECCCCCC		35.5432142685
141PhosphorylationWGVRTKGSGAALPSR
CCCEECCCCCCCCCC		39.2822468782
147PhosphorylationGSGAALPSRPASRAA
CCCCCCCCCCCCCCC		52.5622468782
151PhosphorylationALPSRPASRAAPRPE
CCCCCCCCCCCCCCC		54.1422468782
152UbiquitinationLPSRPASRAAPRPEA
CCCCCCCCCCCCCCC		50.1532015554
159UbiquitinationRAAPRPEASSPPLPL
CCCCCCCCCCCCCCH		3.32-
160PhosphorylationAAPRPEASSPPLPLE
CCCCCCCCCCCCCHH		28.8923403867
161PhosphorylationAPRPEASSPPLPLEK
CCCCCCCCCCCCHHH		21.0123403867
163UbiquitinationRPEASSPPLPLEKAR
CCCCCCCCCCHHHHC		25.45-
163UbiquitinationRPEASSPPLPLEKAR
CCCCCCCCCCHHHHC		25.4529967540
170MethylationPLPLEKARGGLSGPQ
CCCHHHHCCCCCCCC		28.30-
173UbiquitinationLEKARGGLSGPQGGR
HHHHCCCCCCCCCCC		42.4929967540
174PhosphorylationEKARGGLSGPQGGRA
HHHCCCCCCCCCCCH		33.32-
175UbiquitinationKARGGLSGPQGGRAR
HHCCCCCCCCCCCHH		14.23-
175UbiquitinationKARGGLSGPQGGRAR
HHCCCCCCCCCCCHH		14.2329967540
188UbiquitinationARGAMAHVGSRKRSR
HHHHHCCCCCCCHHH		63.14-
188UbiquitinationARGAMAHVGSRKRSR
HHHHHCCCCCCCHHH		63.1422505724
190O-linked_GlycosylationGAMAHVGSRKRSRSR
HHHCCCCCCCHHHHH		47.8230379171
190PhosphorylationGAMAHVGSRKRSRSR
HHHCCCCCCCHHHHH		47.8229396449
192UbiquitinationMAHVGSRKRSRSRSR
HCCCCCCCHHHHHHH		35.3332015554
198PhosphorylationRKRSRSRSRSRGRGS
CCHHHHHHHHCCCCH		30.83-
200UbiquitinationRSRSRSRSRGRGSEK
HHHHHHHHCCCCHHH		35.87-
200PhosphorylationRSRSRSRSRGRGSEK
HHHHHHHHCCCCHHH		35.87-
200UbiquitinationRSRSRSRSRGRGSEK
HHHHHHHHCCCCHHH		35.8721963094
205PhosphorylationSRSRGRGSEKRKKKS
HHHCCCCHHHHHHHC		35.87-
208UbiquitinationRGRGSEKRKKKSRKD
CCCCHHHHHHHCCCC		35.8724816145
211UbiquitinationGSEKRKKKSRKDTSR
CHHHHHHHCCCCCCC		35.8732015554
212PhosphorylationSEKRKKKSRKDTSRN
HHHHHHHCCCCCCCC		35.87-
216PhosphorylationKKKSRKDTSRNCSAS
HHHCCCCCCCCCCCC		35.8720068231
217PhosphorylationKKSRKDTSRNCSAST
HHCCCCCCCCCCCCH		35.8720068231
217 (in isoform 3)Phosphorylation-35.8728102081
217 (in isoform 4)Phosphorylation-35.8728102081
219UbiquitinationSRKDTSRNCSASTSQ
CCCCCCCCCCCCHHH		35.4929967540
221PhosphorylationKDTSRNCSASTSQGR
CCCCCCCCCCHHHCC		46.1325849741
221 (in isoform 2)Phosphorylation-46.13-
221 (in isoform 3)Phosphorylation-46.1329743597
221 (in isoform 4)Phosphorylation-46.1329743597
223PhosphorylationTSRNCSASTSQGRKA
CCCCCCCCHHHCCCC		45.3020068231
223 (in isoform 3)Phosphorylation-45.3023663014
223 (in isoform 4)Phosphorylation-45.3023663014
224PhosphorylationSRNCSASTSQGRKAS
CCCCCCCHHHCCCCC		46.4420068231
224 (in isoform 3)Phosphorylation-46.4425159151
224 (in isoform 4)Phosphorylation-46.4425159151
225PhosphorylationRNCSASTSQGRKAST
CCCCCCHHHCCCCCC		52.9630576142
225 (in isoform 3)Phosphorylation-52.9625159151
225 (in isoform 4)Phosphorylation-52.9625159151
229 (in isoform 3)Phosphorylation-53.8329514088
229 (in isoform 4)Phosphorylation-53.8329514088
231PhosphorylationTSQGRKASTAPGAEA
HHHCCCCCCCCCCCC		61.3323927012
231UbiquitinationTSQGRKASTAPGAEA
HHHCCCCCCCCCCCC		61.3329967540
231 (in isoform 2)Phosphorylation-61.3325849741
231 (in isoform 5)Phosphorylation-61.3325849741
232PhosphorylationSQGRKASTAPGAEAS
HHCCCCCCCCCCCCC		46.7527273156
232 (in isoform 2)Phosphorylation-46.7522985185
232 (in isoform 5)Phosphorylation-46.7522985185
239PhosphorylationTAPGAEASPSPCITE
CCCCCCCCCCCCCCH		67.6929255136
241PhosphorylationPGAEASPSPCITERS
CCCCCCCCCCCCHHH		50.6630266825
244UbiquitinationEASPSPCITERSKQK
CCCCCCCCCHHHHHH		12.6322505724
245PhosphorylationASPSPCITERSKQKA
CCCCCCCCHHHHHHH		62.4130266825
248PhosphorylationSPCITERSKQKARRR
CCCCCHHHHHHHHHH		52.84-
256PhosphorylationKQKARRRTRSSSSSS
HHHHHHHHHCCCCCC		41.91-
256UbiquitinationKQKARRRTRSSSSSS
HHHHHHHHHCCCCCC		41.9121963094
258PhosphorylationKARRRTRSSSSSSSS
HHHHHHHCCCCCCCC		39.90-
259PhosphorylationARRRTRSSSSSSSSS
HHHHHHCCCCCCCCC		21.8730576142
260PhosphorylationRRRTRSSSSSSSSSS
HHHHHCCCCCCCCCC		2.9725884760
261PhosphorylationRRTRSSSSSSSSSSS
HHHHCCCCCCCCCCC		60.75-
262PhosphorylationRTRSSSSSSSSSSSS
HHHCCCCCCCCCCCC		25.86-
263PhosphorylationTRSSSSSSSSSSSSS
HHCCCCCCCCCCCCC		29.7617081983
264PhosphorylationRSSSSSSSSSSSSSS
HCCCCCCCCCCCCCC		50.96-
264UbiquitinationRSSSSSSSSSSSSSS
HCCCCCCCCCCCCCC		50.9629967540
265PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		6.80-
266PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		54.59-
267PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		43.0730576142
268PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		6.6319664994
269PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		14.2619664994
270PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		25.8319664994
271PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		27.9519664994
272PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		29.4019664994
273PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		44.06-
274PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		58.91-
275PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		61.54-
276PhosphorylationSSSSSSSSSSSSSSD
CCCCCCCCCCCCCCC		65.06-
277PhosphorylationSSSSSSSSSSSSSDG
CCCCCCCCCCCCCCC		70.72-
278PhosphorylationSSSSSSSSSSSSDGR
CCCCCCCCCCCCCCC		19.93-
279PhosphorylationSSSSSSSSSSSDGRK
CCCCCCCCCCCCCCH		30.21-
280PhosphorylationSSSSSSSSSSDGRKK
CCCCCCCCCCCCCHH		12.59-
282PhosphorylationSSSSSSSSDGRKKRG
CCCCCCCCCCCHHCC		37.41-
285MethylationSSSSSDGRKKRGKYK
CCCCCCCCHHCCCHH		52.41-
292MethylationRKKRGKYKDKRRKKK
CHHCCCHHHHHHHHH		2.61-
293UbiquitinationKKRGKYKDKRRKKKK
HHCCCHHHHHHHHHH		34.3529967540
297UbiquitinationKYKDKRRKKKKKRKK
CHHHHHHHHHHHHHH		47.59-
304UbiquitinationKKKKKRKKLKKKGKE
HHHHHHHHHHHHHHH		40.4829967540
309UbiquitinationRKKLKKKGKEKAEAQ
HHHHHHHHHHHHHHH		35.88-
310 (in isoform 5)Phosphorylation-4.1926852163
312UbiquitinationLKKKGKEKAEAQQVE
HHHHHHHHHHHHHHH		38.0029967540
322UbiquitinationAQQVEALPGPSLDQW
HHHHHCCCCCCHHHH		56.38-
325PhosphorylationVEALPGPSLDQWHRS
HHCCCCCCHHHHHHC		35.2625159151
327UbiquitinationALPGPSLDQWHRSAG
CCCCCCHHHHHHCCC		11.3022505724
328UbiquitinationLPGPSLDQWHRSAGE
CCCCCHHHHHHCCCC		4.2024816145
331MethylationPSLDQWHRSAGEEED
CCHHHHHHCCCCCCC		3.30-
332PhosphorylationSLDQWHRSAGEEEDG
CHHHHHHCCCCCCCC		7.6619664994
334UbiquitinationDQWHRSAGEEEDGPV
HHHHHCCCCCCCCCC		41.69-
339UbiquitinationSAGEEEDGPVLTDEQ
CCCCCCCCCCCCHHH		44.8021963094
343PhosphorylationEEDGPVLTDEQKSRI
CCCCCCCCHHHHHHH		43.4025159151
347UbiquitinationPVLTDEQKSRIQAMK
CCCCHHHHHHHHHCC		26.1524816145
348PhosphorylationVLTDEQKSRIQAMKP
CCCHHHHHHHHHCCC		22.4426074081
350UbiquitinationTDEQKSRIQAMKPMT
CHHHHHHHHHCCCCC		6.7829967540
351UbiquitinationDEQKSRIQAMKPMTK
HHHHHHHHHCCCCCH		10.0429967540
354AcetylationKSRIQAMKPMTKEEW
HHHHHHCCCCCHHHH		2.2725953088
357PhosphorylationIQAMKPMTKEEWDAR
HHHCCCCCHHHHHHH		19.8526074081
358UbiquitinationQAMKPMTKEEWDARQ
HHCCCCCHHHHHHHH		6.6729967540
362UbiquitinationPMTKEEWDARQSIIR
CCCHHHHHHHHHHHH		29967540
364UbiquitinationTKEEWDARQSIIRKV
CHHHHHHHHHHHHHH		22505724
366PhosphorylationEEWDARQSIIRKVVD
HHHHHHHHHHHHHCC		23401153
370AcetylationARQSIIRKVVDPETG
HHHHHHHHHCCCCCC		26051181
370UbiquitinationARQSIIRKVVDPETG
HHHHHHHHHCCCCCC		29967540
375UbiquitinationIRKVVDPETGRTRLI
HHHHCCCCCCCEEEE		22505724
376UbiquitinationRKVVDPETGRTRLIK
HHHCCCCCCCEEEEC		21963094
383SumoylationTGRTRLIKGDGEVLE
CCCEEEECCCHHHHH		-
383SumoylationTGRTRLIKGDGEVLE
CCCEEEECCCHHHHH		28112733
383UbiquitinationTGRTRLIKGDGEVLE
CCCEEEECCCHHHHH		22505724
384UbiquitinationGRTRLIKGDGEVLEE
CCEEEECCCHHHHHH		29967540
387UbiquitinationRLIKGDGEVLEEIVT
EEECCCHHHHHHHHC		21963094
394PhosphorylationEVLEEIVTKERHREI
HHHHHHHCHHHHHHH		21406692
395UbiquitinationVLEEIVTKERHREIN
HHHHHHCHHHHHHHH		21963094
403UbiquitinationERHREINKQATRGDC
HHHHHHHHHCCHHHH		29967540
407MethylationEINKQATRGDCLAFQ
HHHHHCCHHHHHHHH		-
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 AR6P4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AR6P4_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 AR6P4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AR6P4_HUMANARL6IP4physical
25416956
THAP1_HUMANTHAP1physical
25416956
JMJD6_HUMANJMJD6physical
26186194
CSK22_HUMANCSNK2A2physical
26186194
ZRAB2_HUMANZRANB2physical
26186194
EIF3J_HUMANEIF3Jphysical
26186194
SRPK1_HUMANSRPK1physical
26186194
CCDC9_HUMANCCDC9physical
26186194
NCBP3_HUMANC17orf85physical
26186194
ZC3HE_HUMANZC3H14physical
26186194
UBP7_HUMANUSP7physical
26186194
GPAM1_HUMANGPALPP1physical
26186194
PI42C_HUMANPIP4K2Cphysical
26186194
PI42B_HUMANPIP4K2Bphysical
26186194
PI42A_HUMANPIP4K2Aphysical
26186194
ACY1_HUMANACY1physical
26186194
GRB2_HUMANGRB2physical
25814554
P55G_HUMANPIK3R3physical
25814554
CCDC9_HUMANCCDC9physical
28514442
JMJD6_HUMANJMJD6physical
28514442
EIF3J_HUMANEIF3Jphysical
28514442
PI42C_HUMANPIP4K2Cphysical
28514442
PI42B_HUMANPIP4K2Bphysical
28514442
GPAM1_HUMANGPALPP1physical
28514442
PI42A_HUMANPIP4K2Aphysical
28514442
NCBP3_HUMANC17orf85physical
28514442
UBP7_HUMANUSP7physical
28514442
ZC3HE_HUMANZC3H14physical
28514442
ZRAB2_HUMANZRANB2physical
28514442
SRPK1_HUMANSRPK1physical
28514442
CSK22_HUMANCSNK2A2physical
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 AR6P4_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-271, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND MASSSPECTROMETRY.
"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-178; SER-180 ANDSER-271, 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 SER-271, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-271, ANDMASS SPECTROMETRY.

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