NAF1_HUMAN - dbPTM
NAF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAF1_HUMAN
UniProt AC Q96HR8
Protein Name H/ACA ribonucleoprotein complex non-core subunit NAF1
Gene Name NAF1
Organism Homo sapiens (Human).
Sequence Length 494
Subcellular Localization Cytoplasm. Nucleus. Shuttles between the cytoplasm and the nucleus. Absent from the nucleolus (By similarity)..
Protein Description RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by NOLA1/GAR1 to yield mature H/ACA snoRNPs complex. Probably competes with NOLA1/GAR1 for binding with DKC1/NOLA4..
Protein Sequence MEVVEAAAAQLETLKFNGTDFGVGEGPAAPSPGSAPVPGTQPPLQSFEGSPDAGQTVEVKPAGEQPLQPVLNAVAAGTPAPQPQPPAESPACGDCVTSPGAAEPARAPDSLETSDSDSDSDSETDSDSSSSSSSSSSSSSSSSSSCISLPPVLSDGDDDLQIEKENKNFPLKTKDELLLNELPSVEELTIILPEDIELKPLGMVSSIIEQLVIIESMTNLPPVNEETVIFKSDRQAAGKIFEIFGPVAHPFYVLRFNSSDHIESKGIKIKETMYFAPSMKDFTQYIFTEKLKQDKGSDASWKNDQEPPPEALDFSDDEKEKEAKQRKKSQIQGRKKLKSEFNEPGEDFTEVHQNWNAHSSASEHAKGYRNREFTRGFSRARYPRSCHGRPPPQHFYNSEHMVSQETSGFPSQRQNNPIMPQYPFPLPVFDMHNFPLRPPPPPPPPPVNMGWATPNMAAHPLLNLPYSLPPPPPPPPLPPPPSSGDSNSHFGPYY
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-------MEVVEAAA
-------CHHHHHHH		8.7719413330
31PhosphorylationGEGPAAPSPGSAPVP
CCCCCCCCCCCCCCC		36.8526074081
34PhosphorylationPAAPSPGSAPVPGTQ
CCCCCCCCCCCCCCC		32.5526074081
40PhosphorylationGSAPVPGTQPPLQSF
CCCCCCCCCCCCCCC		31.6526074081
63UbiquitinationTVEVKPAGEQPLQPV
EEEEECCCCCCCHHH		42.4727667366
78O-linked_GlycosylationLNAVAAGTPAPQPQP
HHHHHCCCCCCCCCC		16.14OGP
88UbiquitinationPQPQPPAESPACGDC
CCCCCCCCCCCCCCC		64.1322817900
90UbiquitinationPQPPAESPACGDCVT
CCCCCCCCCCCCCCC		24.0722817900
93UbiquitinationPAESPACGDCVTSPG
CCCCCCCCCCCCCCC		33.2022817900
97PhosphorylationPACGDCVTSPGAAEP
CCCCCCCCCCCCCCC		35.2226074081
98PhosphorylationACGDCVTSPGAAEPA
CCCCCCCCCCCCCCC		10.8426074081
110PhosphorylationEPARAPDSLETSDSD
CCCCCCCCCCCCCCC		27.35-
130PhosphorylationETDSDSSSSSSSSSS
CCCCCCCCCCCCCCC		37.89-
131PhosphorylationTDSDSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
132PhosphorylationDSDSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
133PhosphorylationSDSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
134PhosphorylationDSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
135PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
136PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
137PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
138PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
139PhosphorylationSSSSSSSSSSSSSSC
CCCCCCCCCCCCCCC		35.87-
140PhosphorylationSSSSSSSSSSSSSCI
CCCCCCCCCCCCCCC		35.87-
141PhosphorylationSSSSSSSSSSSSCIS
CCCCCCCCCCCCCCC		35.87-
142PhosphorylationSSSSSSSSSSSCISL
CCCCCCCCCCCCCCC		35.87-
167UbiquitinationLQIEKENKNFPLKTK
CHHCHHCCCCCCCCH		62.1427667366
167SumoylationLQIEKENKNFPLKTK
CHHCHHCCCCCCCCH		62.14-
167SumoylationLQIEKENKNFPLKTK
CHHCHHCCCCCCCCH		62.14-
172UbiquitinationENKNFPLKTKDELLL
HCCCCCCCCHHHHHH		54.4933845483
184PhosphorylationLLLNELPSVEELTII
HHHHCCCCHHEEEEE		55.5825627689
232PhosphorylationEETVIFKSDRQAAGK
CCEEEEECHHHHHHH		27.5520068231
258PhosphorylationFYVLRFNSSDHIESK
EEEEEECCCCCHHCC		34.14-
265UbiquitinationSSDHIESKGIKIKET
CCCCHHCCCEEEEEE		52.4433845483
270UbiquitinationESKGIKIKETMYFAP
HCCCEEEEEEEEECC		41.9729967540
272PhosphorylationKGIKIKETMYFAPSM
CCEEEEEEEEECCCH		16.5124114839
274PhosphorylationIKIKETMYFAPSMKD
EEEEEEEEECCCHHH		12.1923917254
280UbiquitinationMYFAPSMKDFTQYIF
EEECCCHHHHHHHHH		54.7729967540
285PhosphorylationSMKDFTQYIFTEKLK
CHHHHHHHHHHHHHH		8.5727642862
290UbiquitinationTQYIFTEKLKQDKGS
HHHHHHHHHHCCCCC		58.9122817900
292UbiquitinationYIFTEKLKQDKGSDA
HHHHHHHHCCCCCCC		68.4722817900
295UbiquitinationTEKLKQDKGSDASWK
HHHHHCCCCCCCCCC		58.7922817900
297PhosphorylationKLKQDKGSDASWKND
HHHCCCCCCCCCCCC		35.4323403867
300PhosphorylationQDKGSDASWKNDQEP
CCCCCCCCCCCCCCC		43.5023403867
315PhosphorylationPPEALDFSDDEKEKE
CCCCCCCCHHHHHHH		43.7619664994
329PhosphorylationEAKQRKKSQIQGRKK
HHHHHHHHHHHHHHH		35.2329496963
338SumoylationIQGRKKLKSEFNEPG
HHHHHHHHHHHCCCC		57.7428112733
339PhosphorylationQGRKKLKSEFNEPGE
HHHHHHHHHHCCCCC		58.8328555341
375MethylationYRNREFTRGFSRARY
CCCCHHHHCCCCCCC		49.8654549893
378 (in isoform 2)Phosphorylation-28.0525219547
379MethylationEFTRGFSRARYPRSC
HHHHCCCCCCCCCCC		22.3381450723
380 (in isoform 2)Phosphorylation-17.7325219547
381MethylationTRGFSRARYPRSCHG
HHCCCCCCCCCCCCC		40.66115484435
382 (in isoform 2)Phosphorylation-11.3025219547
384 (in isoform 2)Phosphorylation-42.8725219547
384MethylationFSRARYPRSCHGRPP
CCCCCCCCCCCCCCC		42.87115484443
387 (in isoform 2)Phosphorylation-36.2225219547
389MethylationYPRSCHGRPPPQHFY
CCCCCCCCCCCHHHC		19.52115484451
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 NAF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAF1_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 NAF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DKC1_HUMANDKC1physical
19095616
NHP2_HUMANNHP2physical
19095616
NOP10_HUMANNOP10physical
19095616
FBRL_HUMANFBLphysical
19095616
NOP10_HUMANNOP10physical
16601202
DKC1_HUMANDKC1physical
16601202
SHQ1_HUMANSHQ1physical
21931644
SHQ1_YEASTSHQ1physical
21931644
NHP2_HUMANNHP2physical
26344197
DKC1_HUMANDKC1physical
26496610
FKB1A_HUMANFKBP1Aphysical
26496610
MTOR_HUMANMTORphysical
26496610
ECHA_HUMANHADHAphysical
26496610
ECHB_HUMANHADHBphysical
26496610
RAD51_HUMANRAD51physical
26496610
REQU_HUMANDPF2physical
26496610
RL10_HUMANRPL10physical
26496610
TAF13_HUMANTAF13physical
26496610
TBP_HUMANTBPphysical
26496610
ICAM5_HUMANICAM5physical
26496610
TAF1C_HUMANTAF1Cphysical
26496610
TAF1B_HUMANTAF1Bphysical
26496610
TAF1A_HUMANTAF1Aphysical
26496610
DDX23_HUMANDDX23physical
26496610
ATPK_HUMANATP5J2physical
26496610
CAPON_HUMANNOS1APphysical
26496610
KEAP1_HUMANKEAP1physical
26496610
RANB9_HUMANRANBP9physical
26496610
DHRS2_HUMANDHRS2physical
26496610
RM03_HUMANMRPL3physical
26496610
JMJD6_HUMANJMJD6physical
26496610
SF3B1_HUMANSF3B1physical
26496610
IMA7_HUMANKPNA6physical
26496610
ABT1_HUMANABT1physical
26496610
PF21A_HUMANPHF21Aphysical
26496610
SNX9_HUMANSNX9physical
26496610
OTUD4_HUMANOTUD4physical
26496610
SHQ1_HUMANSHQ1physical
26496610
NOP10_HUMANNOP10physical
26496610
NHP2_HUMANNHP2physical
26496610
RABL6_HUMANRABL6physical
26496610
CAMP3_HUMANCAMSAP3physical
26496610
TAF1D_HUMANTAF1Dphysical
26496610
VANG1_HUMANVANGL1physical
26496610
MIB2_HUMANMIB2physical
26496610
SNX33_HUMANSNX33physical
26496610
CA226_HUMANC1orf226physical
26496610
DPOD1_HUMANPOLD1physical
27173435
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 NAF1_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-315, AND MASS SPECTROMETRY.
Phosphorylation
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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-315, 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-315, 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-315, AND MASSSPECTROMETRY.

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