IPPK_HUMAN - dbPTM
IPPK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPPK_HUMAN
UniProt AC Q9H8X2
Protein Name Inositol-pentakisphosphate 2-kinase
Gene Name IPPK
Organism Homo sapiens (Human).
Sequence Length 491
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). InsP6 is involved in many processes such as mRNA export, non-homologous end-joining, endocytosis, ion channel regulation. It also protects cells from TNF-alpha-induced apoptosis..
Protein Sequence MEEGKMDENEWGYHGEGNKSLVVAHAQRCVVLRFLKFPPNRKKTSEEIFQHLQNIVDFGKNVMKEFLGENYVHYGEVVQLPLEFVKQLCLKIQSERPESRCDKDLDTLSGYAMCLPNLTRLQTYRFAEHRPILCVEIKPKCGFIPFSSDVTHEMKHKVCRYCMHQHLKVATGKWKQISKYCPLDLYSGNKQRMHFALKSLLQEAQNNLKIFKNGELIYGCKDARSPVADWSELAHHLKPFFFPSNGLASGPHCTRAVIRELVHVITRVLLSGSDKGRAGTLSPGLGPQGPRVCEASPFSRSLRCQGKNTPERSGLPKGCLLYKTLQVQMLDLLDIEGLYPLYNRVERYLEEFPEERKTLQIDGPYDEAFYQKLLDLSTEDDGTVAFALTKVQQYRVAMTAKDCSIMIALSPCLQDASSDQRPVVPSSRSRFAFSVSVLDLDLKPYESIPHQYKLDGKIVNYYSKTVRAKDNAVMSTRFKESEDCTLVLHKV
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
109PhosphorylationDKDLDTLSGYAMCLP
CCCHHHHHHHHHHHC
31.6729414761
119PhosphorylationAMCLPNLTRLQTYRF
HHHHCCCCHHHEEEC
35.6529414761
173UbiquitinationHLKVATGKWKQISKY
HHHHHCCCHHHHHHC
47.0329967540
179UbiquitinationGKWKQISKYCPLDLY
CCHHHHHHCCCCCCC
53.1229967540
186PhosphorylationKYCPLDLYSGNKQRM
HCCCCCCCCCCHHHH
17.7530576142
187PhosphorylationYCPLDLYSGNKQRMH
CCCCCCCCCCHHHHH
43.0930576142
190UbiquitinationLDLYSGNKQRMHFAL
CCCCCCCHHHHHHHH
42.6929967540
198MethylationQRMHFALKSLLQEAQ
HHHHHHHHHHHHHHH
35.31115971491
209UbiquitinationQEAQNNLKIFKNGEL
HHHHHHCCCCCCCEE
48.5029967540
238AcetylationSELAHHLKPFFFPSN
HHHHHHHCCCCCCCC
35.1126051181
266PhosphorylationRELVHVITRVLLSGS
HHHHHHHHHHHHCCC
17.4025690035
275UbiquitinationVLLSGSDKGRAGTLS
HHHCCCCCCCCCCCC
52.5827667366
280PhosphorylationSDKGRAGTLSPGLGP
CCCCCCCCCCCCCCC
24.0723186163
282PhosphorylationKGRAGTLSPGLGPQG
CCCCCCCCCCCCCCC
19.4325159151
296PhosphorylationGPRVCEASPFSRSLR
CCCCEECCCCCHHHC
12.2726699800
299PhosphorylationVCEASPFSRSLRCQG
CEECCCCCHHHCCCC
25.0926699800
309PhosphorylationLRCQGKNTPERSGLP
HCCCCCCCCCCCCCC
29.9725056879
317UbiquitinationPERSGLPKGCLLYKT
CCCCCCCCCCHHHHH
68.2629967540
357UbiquitinationEEFPEERKTLQIDGP
HHCCHHHCCCCCCCC
57.7921906983
404PhosphorylationAMTAKDCSIMIALSP
EECCCCCCEEEEEHH
25.89-
418PhosphorylationPCLQDASSDQRPVVP
HHHCCCCCCCCCCCC
39.21-
426PhosphorylationDQRPVVPSSRSRFAF
CCCCCCCCCCCCEEE
27.1223898821
457UbiquitinationHQYKLDGKIVNYYSK
CEEEECCEEEEEEEC
43.0529967540
457AcetylationHQYKLDGKIVNYYSK
CEEEECCEEEEEEEC
43.0526051181
461PhosphorylationLDGKIVNYYSKTVRA
ECCEEEEEEECEEEC
9.7529496907
462PhosphorylationDGKIVNYYSKTVRAK
CCEEEEEEECEEECC
9.8529496907
479UbiquitinationAVMSTRFKESEDCTL
EEEECCCCCCCCCEE
57.9729967540
490UbiquitinationDCTLVLHKV------
CCEEEEEEC------
45.5429967540

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 IPPK_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPPK_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 IPPK_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LPAR1_HUMANLPAR1physical
28514442
TYRO3_HUMANTYRO3physical
28514442
ENPP4_HUMANENPP4physical
28514442
SELT_HUMANSELTphysical
28514442
SL9A1_HUMANSLC9A1physical
28514442
SC5D_HUMANSC5Dphysical
28514442
CERS4_HUMANCERS4physical
28514442
CERS5_HUMANCERS5physical
28514442
AT2B3_HUMANATP2B3physical
28514442
TM87B_HUMANTMEM87Bphysical
28514442
MTR1L_HUMANGPR50physical
28514442
ZDH17_HUMANZDHHC17physical
28514442
ATP9A_HUMANATP9Aphysical
28514442
AR6P1_HUMANARL6IP1physical
28514442
ZDH18_HUMANZDHHC18physical
28514442
COL12_HUMANCOLEC12physical
28514442
AT2B4_HUMANATP2B4physical
28514442
CHP3_HUMANTESCphysical
28514442
G137A_HUMANGPR137physical
28514442
GPC5B_HUMANGPRC5Bphysical
28514442
TM186_HUMANTMEM186physical
28514442
SNX13_HUMANSNX13physical
28514442
MAN1_HUMANLEMD3physical
28514442
CD97_HUMANCD97physical
28514442
SNX14_HUMANSNX14physical
28514442
CIA30_HUMANNDUFAF1physical
28514442
ECSIT_HUMANECSITphysical
28514442
ADCY6_HUMANADCY6physical
28514442
GOGA5_HUMANGOLGA5physical
28514442
RETR3_HUMANFAM134Cphysical
28514442
CKAP4_HUMANCKAP4physical
28514442
SCAP_HUMANSCAPphysical
28514442
CD032_HUMANC4orf32physical
28514442
RTN2_HUMANRTN2physical
28514442
FZD8_HUMANFZD8physical
28514442
TMM11_HUMANTMEM11physical
28514442
TM87A_HUMANTMEM87Aphysical
28514442
RMND1_HUMANRMND1physical
28514442
STX4_HUMANSTX4physical
28514442
SERC1_HUMANSERINC1physical
28514442
T161B_HUMANTMEM161Bphysical
28514442
NU2M_HUMANND2physical
28514442
CXCR4_HUMANCXCR4physical
28514442
CERS6_HUMANCERS6physical
28514442
LMBR1_HUMANLMBR1physical
28514442
NDC1_HUMANNDC1physical
28514442
STX8_HUMANSTX8physical
28514442
MPZL1_HUMANMPZL1physical
28514442
ZNT5_HUMANSLC30A5physical
28514442
CTR3_HUMANSLC7A3physical
28514442
TM223_HUMANTMEM223physical
28514442
REEP6_HUMANREEP6physical
28514442
ZDHC9_HUMANZDHHC9physical
28514442
YIPF4_HUMANYIPF4physical
28514442
LNP_HUMANKIAA1715physical
28514442
XYLK_HUMANFAM20Bphysical
28514442
SMAD5_HUMANSMAD5physical
28514442
FITM2_HUMANFITM2physical
28514442
EXTL2_HUMANEXTL2physical
28514442
ARL10_HUMANARL10physical
28514442
OCAD1_HUMANOCIAD1physical
28514442
CJ035_HUMANC10orf35physical
28514442
CGAT2_HUMANCSGALNACT2physical
28514442
EXTL3_HUMANEXTL3physical
28514442
PIGW_HUMANPIGWphysical
28514442
ITPR2_HUMANITPR2physical
28514442
MBOA7_HUMANMBOAT7physical
28514442
GPC5C_HUMANGPRC5Cphysical
28514442
PPAL_HUMANACP2physical
28514442
VEZA_HUMANVEZTphysical
28514442
MRS2_HUMANMRS2physical
28514442
STXB3_HUMANSTXBP3physical
28514442
MFSD8_HUMANMFSD8physical
28514442
HACD2_HUMANPTPLBphysical
28514442
GP1BB_HUMANGP1BBphysical
28514442
KTN1_HUMANKTN1physical
28514442
MBOA5_HUMANLPCAT3physical
28514442
LEG3_HUMANLGALS3physical
28514442
VAMP3_HUMANVAMP3physical
28514442
GOGB1_HUMANGOLGB1physical
28514442
CD47_HUMANCD47physical
28514442
LRC8A_HUMANLRRC8Aphysical
28514442
PCD19_HUMANPCDH19physical
28514442
KDSR_HUMANKDSRphysical
28514442
DGLB_HUMANDAGLBphysical
28514442
TSN15_HUMANTSPAN15physical
28514442
CSCL2_HUMANTMEM63Bphysical
28514442
AGRL3_HUMANLPHN3physical
28514442
ARV1_HUMANARV1physical
28514442
LCLT1_HUMANLCLAT1physical
28514442
ZDH13_HUMANZDHHC13physical
28514442
ACAD9_HUMANACAD9physical
28514442
CERS2_HUMANCERS2physical
28514442
GP108_HUMANGPR108physical
28514442
TTYH3_HUMANTTYH3physical
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 IPPK_HUMAN

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Related Literatures of Post-Translational Modification

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