IST1_HUMAN - dbPTM
IST1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IST1_HUMAN
UniProt AC P53990
Protein Name IST1 homolog
Gene Name IST1
Organism Homo sapiens (Human).
Sequence Length 364
Subcellular Localization Cytoplasmic vesicle . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Midbody . Nucleus envelope . Localizes to centrosome and midbody of dividing cells (PubMed:19129480, PubMed:19129479, PubMed:20719964). Colocalized with SPART
Protein Description ESCRT-III-like protein involved in specific functions of the ESCRT machinery. Is required for efficient abscission during cytokinesis, but not for HIV-1 budding. The involvement in the MVB pathway is not established. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. [PubMed: 19129479]
Protein Sequence MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDSVVMAEAPPGVETDLIDVGFTDDVKKGGPGRGGSGGFTAPVGGPDGTVPMPMPMPMPSANTPFSYPLPKGPSDFNGLPMGTYQAFPNIHPPQIPATPPSYESVDDINADKNISSAQIVGPGPKPEASAKLPSRPADNYDNFVLPELPSVPDTLPTASAGASTSASEDIDFDDLSRRFEELKKKT
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
4Phosphorylation----MLGSGFKAERL
----CCCCCCCHHHH		36.7727470641
7Acetylation-MLGSGFKAERLRVN
-CCCCCCCHHHHHHH		53.5225953088
7Ubiquitination-MLGSGFKAERLRVN
-CCCCCCCHHHHHHH		53.52-
11UbiquitinationSGFKAERLRVNLRLV
CCCCHHHHHHHHHHH		5.5821906983
38UbiquitinationELAQKARKEIADYLA
HHHHHHHHHHHHHHH		59.33-
43PhosphorylationARKEIADYLAAGKDE
HHHHHHHHHHCCCCH		6.8225159151
48UbiquitinationADYLAAGKDERARIR
HHHHHCCCCHHHHHH		52.2521906983
48 (in isoform 1)Ubiquitination-52.2521890473
48 (in isoform 2)Ubiquitination-52.2521890473
48 (in isoform 3)Ubiquitination-52.2521890473
56PhosphorylationDERARIRVEHIIRED
CHHHHHHHHHHHCCH		6.1318083107
61 (in isoform 4)Ubiquitination-30.0821890473
66 (in isoform 6)Phosphorylation-3.4320068231
70 (in isoform 6)Phosphorylation-52.0129523821
79 (in isoform 6)Phosphorylation-1.9320068231
88PhosphorylationARFGLIQSMKELDSG
HHHCHHHHHHHHCHH		25.4821406692
89SulfoxidationRFGLIQSMKELDSGL
HHCHHHHHHHHCHHH		1.9321406390
92 (in isoform 6)Phosphorylation-5.4620068231
95 (in isoform 6)Phosphorylation-28.6820068231
98 (in isoform 6)Phosphorylation-57.6320068231
99 (in isoform 6)Phosphorylation-18.7620068231
112PhosphorylationWAAPRLQSEVAELKI
HHHHHHHHHHHHHHH		38.3327251275
118UbiquitinationQSEVAELKIVADQLC
HHHHHHHHHHHHHHH		27.00-
125GlutathionylationKIVADQLCAKYSKEY
HHHHHHHHHHHHHHH		2.2622555962
125 (in isoform 5)Phosphorylation-2.2627251275
127AcetylationVADQLCAKYSKEYGK
HHHHHHHHHHHHHHC		49.4025953088
127UbiquitinationVADQLCAKYSKEYGK
HHHHHHHHHHHHHHC		49.40-
134AcetylationKYSKEYGKLCRTNQI
HHHHHHHCCCCCCCC		43.4425953088
134MalonylationKYSKEYGKLCRTNQI
HHHHHHHCCCCCCCC		43.4426320211
134UbiquitinationKYSKEYGKLCRTNQI
HHHHHHHCCCCCCCC		43.44-
138PhosphorylationEYGKLCRTNQIGTVN
HHHCCCCCCCCCCCC		30.4027470641
143PhosphorylationCRTNQIGTVNDRLMH
CCCCCCCCCCHHHHH		20.1227470641
147MethylationQIGTVNDRLMHKLSV
CCCCCCHHHHHHCCC		28.80115480653
151AcetylationVNDRLMHKLSVEAPP
CCHHHHHHCCCCCCC		28.6125953088
151UbiquitinationVNDRLMHKLSVEAPP
CCHHHHHHCCCCCCC		28.6121906983
151 (in isoform 1)Ubiquitination-28.6121890473
151 (in isoform 2)Ubiquitination-28.6121890473
151 (in isoform 3)Ubiquitination-28.6121890473
153PhosphorylationDRLMHKLSVEAPPKI
HHHHHHCCCCCCCCC		23.7923312004
159UbiquitinationLSVEAPPKILVERYL
CCCCCCCCCEEEHHH		47.8421890473
159 (in isoform 1)Ubiquitination-47.8421890473
159 (in isoform 2)Ubiquitination-47.8421890473
159 (in isoform 3)Ubiquitination-47.8421890473
164 (in isoform 4)Ubiquitination-24.8721890473
172UbiquitinationYLIEIAKNYNVPYEP
HHHHHHHHCCCCCCC		25.2921890473
173PhosphorylationLIEIAKNYNVPYEPD
HHHHHHHCCCCCCCC		19.4826074081
177PhosphorylationAKNYNVPYEPDSVVM
HHHCCCCCCCCCEEE		35.4926074081
181PhosphorylationNVPYEPDSVVMAEAP
CCCCCCCCEEEEECC		27.5928348404
205UbiquitinationVGFTDDVKKGGPGRG
ECCCCCCCCCCCCCC		53.3321906983
205 (in isoform 1)Ubiquitination-53.3321890473
205 (in isoform 2)Ubiquitination-53.3321890473
205 (in isoform 3)Ubiquitination-53.3321890473
206UbiquitinationGFTDDVKKGGPGRGG
CCCCCCCCCCCCCCC		69.792190698
206 (in isoform 1)Ubiquitination-69.7921890473
206 (in isoform 2)Ubiquitination-69.7921890473
206 (in isoform 3)Ubiquitination-69.7921890473
214PhosphorylationGGPGRGGSGGFTAPV
CCCCCCCCCCCCCCC		38.2722199227
214 (in isoform 2)Phosphorylation-38.2720068231
214 (in isoform 3)Phosphorylation-38.2720068231
214 (in isoform 4)Phosphorylation-38.2720068231
218PhosphorylationRGGSGGFTAPVGGPD
CCCCCCCCCCCCCCC		33.0722199227
218 (in isoform 2)Phosphorylation-33.0729523821
218 (in isoform 3)Phosphorylation-33.0729523821
218 (in isoform 4)Phosphorylation-33.0729523821
218 (in isoform 4)Ubiquitination-33.0721890473
219 (in isoform 4)Ubiquitination-8.4321890473
227PhosphorylationPVGGPDGTVPMPMPM
CCCCCCCCCCCCCCC		28.9020068231
227 (in isoform 2)Phosphorylation-28.9020068231
227 (in isoform 3)Phosphorylation-28.9020068231
227 (in isoform 4)Phosphorylation-28.9020068231
227 (in isoform 5)Phosphorylation-28.9020068231
231 (in isoform 5)Phosphorylation-20.0429523821
238PhosphorylationPMPMPMPSANTPFSY
CCCCCCCCCCCCCCC		28.0927470641
240PhosphorylationPMPMPSANTPFSYPL
CCCCCCCCCCCCCCC		53.2620068231
240 (in isoform 2)Phosphorylation-53.2620068231
240 (in isoform 3)Phosphorylation-53.2620068231
240 (in isoform 4)Phosphorylation-53.2620068231
240 (in isoform 5)Phosphorylation-53.2620068231
241PhosphorylationMPMPSANTPFSYPLP
CCCCCCCCCCCCCCC		25.9820068231
243 (in isoform 2)Phosphorylation-11.7020068231
243 (in isoform 3)Phosphorylation-11.7020068231
243 (in isoform 4)Phosphorylation-11.7020068231
244PhosphorylationPSANTPFSYPLPKGP
CCCCCCCCCCCCCCC		27.3520068231
245PhosphorylationSANTPFSYPLPKGPS
CCCCCCCCCCCCCCC		14.7920068231
246 (in isoform 2)Phosphorylation-40.7720068231
246 (in isoform 3)Phosphorylation-40.7720068231
246 (in isoform 4)Phosphorylation-40.7720068231
247 (in isoform 2)Phosphorylation-5.3420068231
247 (in isoform 3)Phosphorylation-5.3420068231
247 (in isoform 4)Phosphorylation-5.3420068231
253 (in isoform 5)Phosphorylation-44.1320068231
256 (in isoform 5)Phosphorylation-31.0220068231
259 (in isoform 5)Phosphorylation-8.2320068231
260 (in isoform 5)Phosphorylation-21.2320068231
276PhosphorylationHPPQIPATPPSYESV
CCCCCCCCCCCCCCH		30.3122199227
279PhosphorylationQIPATPPSYESVDDI
CCCCCCCCCCCHHHC		42.6129523821
291 (in isoform 5)Phosphorylation-39.6627251275
293PhosphorylationINADKNISSAQIVGP
CCCCCCCCCCEEECC		29.0820068231
294PhosphorylationNADKNISSAQIVGPG
CCCCCCCCCEEECCC		22.0120873877
294 (in isoform 5)Phosphorylation-22.0127251275
307PhosphorylationPGPKPEASAKLPSRP
CCCCCCHHCCCCCCC		25.0325159151
309 (in isoform 5)Phosphorylation-59.4427251275
312PhosphorylationEASAKLPSRPADNYD
CHHCCCCCCCCCCCC		62.4228796482
318PhosphorylationPSRPADNYDNFVLPE
CCCCCCCCCCCCCCC		16.8929759185
322 (in isoform 5)Phosphorylation-12.5127251275
327 (in isoform 5)Phosphorylation-31.4527642862
328PhosphorylationFVLPELPSVPDTLPT
CCCCCCCCCCCCCCC		59.9328796482
332PhosphorylationELPSVPDTLPTASAG
CCCCCCCCCCCCCCC		28.6828348404
333 (in isoform 5)Phosphorylation-4.6527642862
335PhosphorylationSVPDTLPTASAGAST
CCCCCCCCCCCCCCC		36.0427251275
337PhosphorylationPDTLPTASAGASTSA
CCCCCCCCCCCCCCC		29.7029802988
341PhosphorylationPTASAGASTSASEDI
CCCCCCCCCCCCCCC		23.2128348404
342PhosphorylationTASAGASTSASEDID
CCCCCCCCCCCCCCC		27.9828348404
343PhosphorylationASAGASTSASEDIDF
CCCCCCCCCCCCCCH		27.5728348404
345PhosphorylationAGASTSASEDIDFDD
CCCCCCCCCCCCHHH		35.2528348404
352 (in isoform 5)Phosphorylation-46.6827251275
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 IST1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IST1_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 IST1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHM1B_HUMANCHMP1Bphysical
19477918
ANC2_HUMANANAPC2physical
21439932
CDC20_HUMANCDC20physical
21439932
FZR1_HUMANFZR1physical
21439932
METK1_HUMANMAT1Aphysical
22939629
CAN7_HUMANCAPN7physical
25416956
UBQL1_HUMANUBQLN1physical
25416956
CHM1A_HUMANCHMP1Aphysical
26186194
AP1G2_HUMANAP1G2physical
26344197
MIB2_HUMANMIB2physical
26344197
VPS4A_HUMANVPS4Aphysical
26344197
VPS4B_HUMANVPS4Bphysical
26344197
CHM1A_HUMANCHMP1Aphysical
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 IST1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory