NELFD_HUMAN - dbPTM
NELFD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NELFD_HUMAN
UniProt AC Q8IXH7
Protein Name Negative elongation factor C/D
Gene Name NELFCD
Organism Homo sapiens (Human).
Sequence Length 590
Subcellular Localization Nucleus .
Protein Description Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. Binds RNA which may help to stabilize the NELF complex on nucleic acid. In vitro, the NELFA:NELFCD subcomplex binds to ssDNA and ssRNA in a sequence- and structure-dependent manner..
Protein Sequence MAGAVPGAIMDEDYYGSAAEWGDEADGGQQEDDSGEGEDDAEVQQECLHKFSTRDYIMEPSIFNTLKRYFQAGGSPENVIQLLSENYTAVAQTVNLLAEWLIQTGVEPVQVQETVENHLKSLLIKHFDPRKADSIFTEEGETPAWLEQMIAHTTWRDLFYKLAEAHPDCLMLNFTVKLISDAGYQGEITSVSTACQQLEVFSRVLRTSLATILDGGEENLEKNLPEFAKMVCHGEHTYLFAQAMMSVLAQEEQGGSAVRRIAQEVQRFAQEKGHDASQITLALGTAASYPRACQALGAMLSKGALNPADITVLFKMFTSMDPPPVELIRVPAFLDLFMQSLFKPGARINQDHKHKYIHILAYAASVVETWKKNKRVSINKDELKSTSKAVETVHNLCCNENKGASELVAELSTLYQCIRFPVVAMGVLKWVDWTVSEPRYFQLQTDHTPVHLALLDEISTCHQLLHPQVLQLLVKLFETEHSQLDVMEQLELKKTLLDRMVHLLSRGYVLPVVSYIRKCLEKLDTDISLIRYFVTEVLDVIAPPYTSDFVQLFLPILENDSIAGTIKTEGEHDPVTEFIAHCKSNFIMVN
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
6 (in isoform 4)Phosphorylation-26.43-
15PhosphorylationAIMDEDYYGSAAEWG
CCCCCCCCCCHHHHC		19.54-
34PhosphorylationGGQQEDDSGEGEDDA
CCCCCCCCCCCCCHH		51.5724732914
53PhosphorylationECLHKFSTRDYIMEP
HHHHHHCCCCCCCCH		30.6027362937
56PhosphorylationHKFSTRDYIMEPSIF
HHHCCCCCCCCHHHH		10.0121406692
56NitrationHKFSTRDYIMEPSIF
HHHCCCCCCCCHHHH		10.01-
58 (in isoform 4)Ubiquitination-5.1521890473
61PhosphorylationRDYIMEPSIFNTLKR
CCCCCCHHHHHHHHH		26.8921406692
65PhosphorylationMEPSIFNTLKRYFQA
CCHHHHHHHHHHHHC		23.9421406692
67UbiquitinationPSIFNTLKRYFQAGG
HHHHHHHHHHHHCCC		42.9121890473
67 (in isoform 1)Ubiquitination-42.9121890473
67 (in isoform 3)Ubiquitination-42.9121890473
116 (in isoform 4)Ubiquitination-46.4821890473
121PhosphorylationTVENHLKSLLIKHFD
HHHHHHHHHHHHHCC		34.47-
125UbiquitinationHLKSLLIKHFDPRKA
HHHHHHHHHCCHHHC		37.882189047
125 (in isoform 3)Ubiquitination-37.8821890473
125 (in isoform 1)Ubiquitination-37.8821890473
237PhosphorylationMVCHGEHTYLFAQAM
HHHCCCHHHHHHHHH		20.0226074081
238PhosphorylationVCHGEHTYLFAQAMM
HHCCCHHHHHHHHHH		11.1726074081
246PhosphorylationLFAQAMMSVLAQEEQ
HHHHHHHHHHHHHHC		10.8226074081
256PhosphorylationAQEEQGGSAVRRIAQ
HHHHCCCHHHHHHHH		30.3426074081
272UbiquitinationVQRFAQEKGHDASQI
HHHHHHHHCCCHHHH		49.84-
277PhosphorylationQEKGHDASQITLALG
HHHCCCHHHHHHHHH		28.3324719451
280PhosphorylationGHDASQITLALGTAA
CCCHHHHHHHHHHHC		9.8019060867
285PhosphorylationQITLALGTAASYPRA
HHHHHHHHHCCHHHH		21.6519060867
289PhosphorylationALGTAASYPRACQAL
HHHHHCCHHHHHHHH		7.6319060867
291MethylationGTAASYPRACQALGA
HHHCCHHHHHHHHHH		39.50115484809
294PhosphorylationASYPRACQALGAMLS
CCHHHHHHHHHHHHH		38.3419413330
298PhosphorylationRACQALGAMLSKGAL
HHHHHHHHHHHCCCC		9.1519413330
301PhosphorylationQALGAMLSKGALNPA
HHHHHHHHCCCCCHH		18.8919060867
310PhosphorylationGALNPADITVLFKMF
CCCCHHHHHHHHHHH		2.8919413330
316SulfoxidationDITVLFKMFTSMDPP
HHHHHHHHHHCCCCC		3.2921406390
340PhosphorylationFLDLFMQSLFKPGAR
HHHHHHHHHCCCCCC		24.8024719451
372AcetylationSVVETWKKNKRVSIN
HHHHHHHHCCCEECC		60.307306907
374AcetylationVETWKKNKRVSINKD
HHHHHHCCCEECCHH		64.167306917
377PhosphorylationWKKNKRVSINKDELK
HHHCCCEECCHHHHH		25.2029214152
380UbiquitinationNKRVSINKDELKSTS
CCCEECCHHHHHHHH		51.41-
380AcetylationNKRVSINKDELKSTS
CCCEECCHHHHHHHH		51.417306927
384AcetylationSINKDELKSTSKAVE
ECCHHHHHHHHHHHH		50.0325953088
392PhosphorylationSTSKAVETVHNLCCN
HHHHHHHHHHHHHCC		22.07-
4932-HydroxyisobutyrylationVMEQLELKKTLLDRM
HHHHHHHHHHHHHHH		34.04-
525PhosphorylationKCLEKLDTDISLIRY
HHHHHCCCCHHHHHH		45.7420068231
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
6YPhosphorylationKinaseSRCP12931
PSP
-KUbiquitinationE3 ubiquitin ligaseUBE3AQ05086
PMID:17131388
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NELFD_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 NELFD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF4G1_HUMANEIF4G1physical
17353931
CCAR2_HUMANCCAR2physical
17353931
COX41_HUMANCOX4I1physical
17353931
NELFE_HUMANNELFEphysical
17353931
RS11_HUMANRPS11physical
17353931
NELFB_HUMANNELFBphysical
17353931
COX5A_HUMANCOX5Aphysical
17353931
COX2_HUMANCOX2physical
17353931
MCM7_HUMANMCM7physical
17353931
COX6C_HUMANCOX6Cphysical
17353931
PHB2_HUMANPHB2physical
17353931
COPB2_HUMANCOPB2physical
17353931
RS14_HUMANRPS14physical
17353931
COX5B_HUMANCOX5Bphysical
17353931
DNPEP_HUMANDNPEPphysical
17353931
CX6B1_HUMANCOX6B1physical
17353931
RS26_HUMANRPS26physical
17353931
NELFB_HUMANNELFBphysical
12612062
ARPC4_HUMANARPC4physical
16169070
SYEP_HUMANEPRSphysical
16169070
SERF2_HUMANSERF2physical
16169070
DNJA1_HUMANDNAJA1physical
16169070
GSTM4_HUMANGSTM4physical
16169070
HDA11_HUMANHDAC11physical
16169070
MTA1_HUMANMTA1physical
16169070
ARAF_HUMANARAFphysical
11952167
UBE3A_HUMANUBE3Aphysical
17131388
ANDR_HUMANARphysical
20069563
AT1A1_HUMANATP1A1physical
20305087
NELFB_HUMANNELFBphysical
20305087
NELFE_HUMANNELFEphysical
20305087
NELFA_HUMANNELFAphysical
20305087
UBE3A_HUMANUBE3Aphysical
21988832
ZN638_HUMANZNF638physical
21988832
ANM5_HUMANPRMT5physical
23455924
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 NELFD_HUMAN

loading...

Related Literatures of Post-Translational Modification
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-280; THR-285; TYR-289AND SER-301, AND MASS SPECTROMETRY.

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