NHP2_HUMAN - dbPTM
NHP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NHP2_HUMAN
UniProt AC Q9NX24
Protein Name H/ACA ribonucleoprotein complex subunit 2
Gene Name NHP2
Organism Homo sapiens (Human).
Sequence Length 153
Subcellular Localization Nucleus, nucleolus. Nucleus, Cajal body. Also localized to Cajal bodies (coiled bodies).
Protein Description Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ("psi") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme..
Protein Sequence MTKIKADPDGPEAQAEACSGERTYQELLVNQNPIAQPLASRRLTRKLYKCIKKAVKQKQIRRGVKEVQKFVNKGEKGIMVLAGDTLPIEVYCHLPVMCEDRNLPYVYIPSKTDLGAAAGSKRPTCVIMVKPHEEYQEAYDECLEEVQSLPLPL
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
3Sumoylation-----MTKIKADPDG
-----CCCCCCCCCC
40.6928112733
5Sumoylation---MTKIKADPDGPE
---CCCCCCCCCCHH
48.57-
5Ubiquitination---MTKIKADPDGPE
---CCCCCCCCCCHH
48.57-
5Acetylation---MTKIKADPDGPE
---CCCCCCCCCCHH
48.5723749302
5Sumoylation---MTKIKADPDGPE
---CCCCCCCCCCHH
48.5725114211
18GlutathionylationPEAQAEACSGERTYQ
HHHHHHHHCCCCCHH
3.9522555962
19PhosphorylationEAQAEACSGERTYQE
HHHHHHHCCCCCHHH
51.2218523010
23PhosphorylationEACSGERTYQELLVN
HHHCCCCCHHHHHHC
25.8429978859
24PhosphorylationACSGERTYQELLVNQ
HHCCCCCHHHHHHCC
13.2524043423
48PhosphorylationRRLTRKLYKCIKKAV
HHHHHHHHHHHHHHH
13.57-
49AcetylationRLTRKLYKCIKKAVK
HHHHHHHHHHHHHHH
39.6625953088
56MethylationKCIKKAVKQKQIRRG
HHHHHHHHHHHHHHH
57.5523748837
69UbiquitinationRGVKEVQKFVNKGEK
HHHHHHHHHHHCCCC
57.36-
73UbiquitinationEVQKFVNKGEKGIMV
HHHHHHHCCCCCEEE
64.24-
91PhosphorylationDTLPIEVYCHLPVMC
CCCCEEEEECCCEEE
2.1427642862
105PhosphorylationCEDRNLPYVYIPSKT
ECCCCCCEEEECCCC
14.7328796482
107PhosphorylationDRNLPYVYIPSKTDL
CCCCCEEEECCCCCC
10.9828796482
110PhosphorylationLPYVYIPSKTDLGAA
CCEEEECCCCCCCCC
38.3324719451
111AcetylationPYVYIPSKTDLGAAA
CEEEECCCCCCCCCC
40.4825953088
111UbiquitinationPYVYIPSKTDLGAAA
CEEEECCCCCCCCCC
40.48-
112PhosphorylationYVYIPSKTDLGAAAG
EEEECCCCCCCCCCC
40.5721406692
120PhosphorylationDLGAAAGSKRPTCVI
CCCCCCCCCCCEEEE
22.2921406692
1212-HydroxyisobutyrylationLGAAAGSKRPTCVIM
CCCCCCCCCCEEEEE
62.57-
121UbiquitinationLGAAAGSKRPTCVIM
CCCCCCCCCCEEEEE
62.57-

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 NHP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NHP2_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 NHP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NOP58_HUMANNOP58physical
22939629
JMJD6_HUMANJMJD6physical
23455924

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613987Dyskeratosis congenita, autosomal recessive, 2 (DKCB2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NHP2_HUMAN

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Related Literatures of Post-Translational Modification
Sumoylation
ReferencePubMed
"A proteomic screen for nucleolar SUMO targets shows SUMOylationmodulates the function of Nop5/Nop58.";
Westman B.J., Verheggen C., Hutten S., Lam Y.W., Bertrand E.,Lamond A.I.;
Mol. Cell 39:618-631(2010).
Cited for: SUMOYLATION AT LYS-5.

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