ZNHI2_HUMAN - dbPTM
ZNHI2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNHI2_HUMAN
UniProt AC Q9UHR6
Protein Name Zinc finger HIT domain-containing protein 2
Gene Name ZNHIT2
Organism Homo sapiens (Human).
Sequence Length 403
Subcellular Localization
Protein Description
Protein Sequence MEPAGPCGFCPAGEVQPARYTCPRCNAPYCSLRCYRTHGTCAENFYRDQVLGELRGCSAPPSRLASALRRLRQQRETEDEPGEAGLSSGPAPGGLSGLWERLAPGEKAAFERLLSRGEAGRLLPPWRPWWWNRGAGPQLLEELDNAPGSDAAELELAPARTPPDSVKDASAAEPAAAERVLGDVPGACTPVVPTRIPAIVSLSRGPVSPLVRFQLPNVLFAYAHTLALYHGGDDALLSDFCATLLGVSGALGAQQVFASAEEALQAAAHVLEAGEHPPGPLGTRGAMHEVARILLGEGPTNQKGYTLAALGDLAQTLGRARKQAVAREERDHLYRARKKCQFLLAWTNENEAALTPLALDCARAHQAHAVVAEEVAALTGELERLWGGPVPPAPRTLIEELPS
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
1Acetylation-------MEPAGPCG
-------CCCCCCCC
14.5422814378
60PhosphorylationELRGCSAPPSRLASA
HHCCCCCCHHHHHHH
15.8832645325
62PhosphorylationRGCSAPPSRLASALR
CCCCCCHHHHHHHHH
38.58-
66PhosphorylationAPPSRLASALRRLRQ
CCHHHHHHHHHHHHH
32.2128674151
96PhosphorylationGPAPGGLSGLWERLA
CCCCCCCCHHHHHHC
34.8024667141
107UbiquitinationERLAPGEKAAFERLL
HHHCCCCHHHHHHHH
51.43-
115PhosphorylationAAFERLLSRGEAGRL
HHHHHHHHCCCCCCC
42.7126462736
149PhosphorylationELDNAPGSDAAELEL
HHHCCCCCCHHHHHC
24.0221955146
161PhosphorylationLELAPARTPPDSVKD
HHCCCCCCCCCCCCC
41.0830278072
165PhosphorylationPARTPPDSVKDASAA
CCCCCCCCCCCCHHC
36.5221955146
167UbiquitinationRTPPDSVKDASAAEP
CCCCCCCCCCHHCCH
52.0821906983
170PhosphorylationPDSVKDASAAEPAAA
CCCCCCCHHCCHHHH
37.8426434776
189PhosphorylationGDVPGACTPVVPTRI
CCCCCCCCCCCCCCC
20.7021712546
194PhosphorylationACTPVVPTRIPAIVS
CCCCCCCCCCCEEEE
29.6227251275
201PhosphorylationTRIPAIVSLSRGPVS
CCCCEEEECCCCCCC
17.9528555341
203PhosphorylationIPAIVSLSRGPVSPL
CCEEEECCCCCCCCC
27.9024719451
208PhosphorylationSLSRGPVSPLVRFQL
ECCCCCCCCCHHCCC
18.6926270265
300PhosphorylationILLGEGPTNQKGYTL
HHHCCCCCCCCCCHH
62.2320860994
303UbiquitinationGEGPTNQKGYTLAAL
CCCCCCCCCCHHHHH
56.8221906983
306PhosphorylationPTNQKGYTLAALGDL
CCCCCCCHHHHHHHH
20.7029496907
316PhosphorylationALGDLAQTLGRARKQ
HHHHHHHHHHHHHHH
26.10-
319MethylationDLAQTLGRARKQAVA
HHHHHHHHHHHHHHH
34.04115920681
322AcetylationQTLGRARKQAVAREE
HHHHHHHHHHHHHHH
41.447297999
338UbiquitinationDHLYRARKKCQFLLA
HHHHHHHHHCCEEEE
57.84-
339UbiquitinationHLYRARKKCQFLLAW
HHHHHHHHCCEEEEE
27.93-
403PhosphorylationTLIEELPS-------
HHHHHCCC-------
66.5327251275

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 ZNHI2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNHI2_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 ZNHI2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CKAP5_HUMANCKAP5physical
26344197
AAR2_HUMANAAR2physical
28561026
WDCP_HUMANC2orf44physical
28561026
ECD_HUMANECDphysical
28561026
U5S1_HUMANEFTUD2physical
28561026
PIHD1_HUMANPIH1D1physical
28561026
RPB1_HUMANPOLR2Aphysical
28561026
RPB3_HUMANPOLR2Cphysical
28561026
MYZAP_HUMANPOLR2Mphysical
28561026
GRL1A_HUMANPOLR2Mphysical
28561026
GL1AD_HUMANPOLR2Mphysical
28561026
RPC1_HUMANPOLR3Aphysical
28561026
PRP6_HUMANPRPF6physical
28561026
PRP8_HUMANPRPF8physical
28561026
RPAP2_HUMANRPAP2physical
28561026
RPAP3_HUMANRPAP3physical
28561026
RUVB1_HUMANRUVBL1physical
28561026
RUVB2_HUMANRUVBL2physical
28561026
U520_HUMANSNRNP200physical
28561026
SNR40_HUMANSNRNP40physical
28561026
TNG6_HUMANTANGO6physical
28561026
TTI1_HUMANTTI1physical
28561026
RMP_HUMANURI1physical
28561026
ZNHI2_HUMANZNHIT2physical
28561026
CD2B2_HUMANCD2BP2physical
28561026
DCAF8_HUMANDCAF8physical
28561026
DDX23_HUMANDDX23physical
28561026
PRP16_HUMANDHX38physical
28561026
DKC1_HUMANDKC1physical
28561026
EAPP_HUMANEAPPphysical
28561026
FBX3_HUMANFBXO3physical
28561026
NCDN_HUMANNCDNphysical
28561026
PFD2_HUMANPFDN2physical
28561026
PDIP2_HUMANPOLDIP2physical
28561026
RPB2_HUMANPOLR2Bphysical
28561026
PRP19_HUMANPRPF19physical
28561026
SNUT1_HUMANSART1physical
28561026
SART3_HUMANSART3physical
28561026
SHQ1_HUMANSHQ1physical
28561026
TCOF_HUMANTCOF1physical
28561026
TSSC4_HUMANTSSC4physical
28561026
UBR4_HUMANUBR4physical
28561026
USP9X_HUMANUSP9Xphysical
28561026
WDR92_HUMANWDR92physical
28561026
CWC22_HUMANCWC22physical
28561026
SNUT2_HUMANUSP39physical
28561026

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 ZNHI2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND MASSSPECTROMETRY.

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