dbPTM

HLTF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HLTF_HUMAN
UniProt AC	Q14527
Protein Name	Helicase-like transcription factor
Gene Name	HLTF
Organism	Homo sapiens (Human).
Sequence Length	1009
Subcellular Localization	Cytoplasm. Nucleus . Nucleus, nucleolus. Nucleus, nucleoplasm. Nuclear localization is stimulated by progesterone..
Protein Description	Has both helicase and E3 ubiquitin ligase activities. Possesses intrinsic ATP-dependent nucleosome-remodeling activity; This activity may be required for transcriptional activation or repression of specific target promoters (By similarity). These may include the SERPINE1 and HIV-1 promoters and the SV40 enhancer, to which this protein can bind directly. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA..
Protein Sequence	MSWMFKRDPVWKYLQTVQYGVHGNFPRLSYPTFFPRFEFQDVIPPDDFLTSDEEVDSVLFGSLRGHVVGLRYYTGVVNNNEMVALQRDPNNPYDKNAIKVNNVNGNQVGHLKKELAGALAYIMDNKLAQIEGVVPFGANNAFTMPLHMTFWGKEENRKAVSDQLKKHGFKLGPAPKTLGFNLESGWGSGRAGPSYSMPVHAAVQMTTEQLKTEFDKLFEDLKEDDKTHEMEPAEAIETPLLPHQKQALAWMVSRENSKELPPFWEQRNDLYYNTITNFSEKDRPENVHGGILADDMGLGKTLTAIAVILTNFHDGRPLPIERVKKNLLKKEYNVNDDSMKLGGNNTSEKADGLSKDASRCSEQPSISDIKEKSKFRMSELSSSRPKRRKTAVQYIESSDSEEIETSELPQKMKGKLKNVQSETKGRAKAGSSKVIEDVAFACALTSSVPTTKKKMLKKGACAVEGSKKTDVEERPRTTLIICPLSVLSNWIDQFGQHIKSDVHLNFYVYYGPDRIREPALLSKQDIVLTTYNILTHDYGTKGDSPLHSIRWLRVILDEGHAIRNPNAQQTKAVLDLESERRWVLTGTPIQNSLKDLWSLLSFLKLKPFIDREWWHRTIQRPVTMGDEGGLRRLQSLIKNITLRRTKTSKIKGKPVLELPERKVFIQHITLSDEERKIYQSVKNEGRATIGRYFNEGTVLAHYADVLGLLLRLRQICCHTYLLTNAVSSNGPSGNDTPEELRKKLIRKMKLILSSGSDEECAICLDSLTVPVITHCAHVFCKPCICQVIQNEQPHAKCPLCRNDIHEDNLLECPPEELARDSEKKSDMEWTSSSKINALMHALTDLRKKNPNIKSLVVSQFTTFLSLIEIPLKASGFVFTRLDGSMAQKKRVESIQCFQNTEAGSPTIMLLSLKAGGVGLNLSAASRVFLMDPAWNPAAEDQCFDRCHRLGQKQEVIITKFIVKDSVEENMLKIQNKKRELAAGAFGTKKPNADEMKQAKINEIRTLIDL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Ubiquitination	--MSWMFKRDPVWKY --CCCCCCCCHHHHH	39.52	-
12	Ubiquitination	FKRDPVWKYLQTVQY CCCCHHHHHHHHHCC	36.00	21890473
12 (in isoform 1)	Ubiquitination	-	36.00	21890473
19	Phosphorylation	KYLQTVQYGVHGNFP HHHHHHCCCCCCCCC	19.44	27642862
27	Dimethylation	GVHGNFPRLSYPTFF CCCCCCCCCCCCCCC	31.93	-
27	Methylation	GVHGNFPRLSYPTFF CCCCCCCCCCCCCCC	31.93	24129315
29	Phosphorylation	HGNFPRLSYPTFFPR CCCCCCCCCCCCCCC	30.28	21815630
30	Phosphorylation	GNFPRLSYPTFFPRF CCCCCCCCCCCCCCC	15.75	23186163
50	Phosphorylation	IPPDDFLTSDEEVDS CCCHHHCCCHHHHHH	33.84	28387310
51	Phosphorylation	PPDDFLTSDEEVDSV CCHHHCCCHHHHHHH	45.21	28464451
54 (in isoform 2)	Ubiquitination	-	57.52	21890473
57	Phosphorylation	TSDEEVDSVLFGSLR CCHHHHHHHHHHHHC	26.37	29523821
62	Phosphorylation	VDSVLFGSLRGHVVG HHHHHHHHHCCCEEE	13.94	20068231
93	Phosphorylation	QRDPNNPYDKNAIKV ECCCCCCCCCCCEEE	41.49	28152594
94 (in isoform 2)	Ubiquitination	-	38.70	21890473
95	Ubiquitination	DPNNPYDKNAIKVNN CCCCCCCCCCEEEEC	42.30	21906983
95 (in isoform 1)	Ubiquitination	-	42.30	21890473
99	Ubiquitination	PYDKNAIKVNNVNGN CCCCCCEEEECCCCC	36.18	-
112	Acetylation	GNQVGHLKKELAGAL CCCHHHHHHHHHHHH	38.23	25953088
112	Sumoylation	GNQVGHLKKELAGAL CCCHHHHHHHHHHHH	38.23	28112733
112	Ubiquitination	GNQVGHLKKELAGAL CCCHHHHHHHHHHHH	38.23	-
113	Ubiquitination	NQVGHLKKELAGALA CCHHHHHHHHHHHHH	65.41	-
121	Phosphorylation	ELAGALAYIMDNKLA HHHHHHHHHHCCCHH	9.53	-
136 (in isoform 2)	Ubiquitination	-	11.03	21890473
158	Acetylation	WGKEENRKAVSDQLK CCCHHHHHHHHHHHH	65.80	7668585
158	Ubiquitination	WGKEENRKAVSDQLK CCCHHHHHHHHHHHH	65.80	-
165	Acetylation	KAVSDQLKKHGFKLG HHHHHHHHHCCCCCC	36.77	7668595
165	Ubiquitination	KAVSDQLKKHGFKLG HHHHHHHHHCCCCCC	36.77	-
166	Ubiquitination	AVSDQLKKHGFKLGP HHHHHHHHCCCCCCC	58.51	-
170	Ubiquitination	QLKKHGFKLGPAPKT HHHHCCCCCCCCCCC	58.06	-
176	Ubiquitination	FKLGPAPKTLGFNLE CCCCCCCCCCCEECC	59.49	21890473
176 (in isoform 1)	Ubiquitination	-	59.49	21890473
188	Phosphorylation	NLESGWGSGRAGPSY ECCCCCCCCCCCCCC	20.71	24719451
195	Phosphorylation	SGRAGPSYSMPVHAA CCCCCCCCCCCHHHH	16.48	21457752
211	Sumoylation	QMTTEQLKTEFDKLF HHCHHHHHHHHHHHH	45.78	28112733
216	Ubiquitination	QLKTEFDKLFEDLKE HHHHHHHHHHHHHHH	61.47	21890473
216 (in isoform 1)	Ubiquitination	-	61.47	21890473
218 (in isoform 2)	Ubiquitination	-	9.40	21890473
222	Ubiquitination	DKLFEDLKEDDKTHE HHHHHHHHHCCCCCC	72.00	-
227 (in isoform 2)	Ubiquitination	-	30.02	21890473
238	Phosphorylation	EPAEAIETPLLPHQK CHHHHCCCCCCHHHH	17.08	-
245	Ubiquitination	TPLLPHQKQALAWMV CCCCHHHHHHHHHHH	34.21	-
258	Ubiquitination	MVSRENSKELPPFWE HHCCCCCCCCCCHHH	74.89	21890473
258 (in isoform 1)	Ubiquitination	-	74.89	21890473
281	Acetylation	TITNFSEKDRPENVH CCCCCCCCCCCCCCC	58.81	7693131
281	Ubiquitination	TITNFSEKDRPENVH CCCCCCCCCCCCCCC	58.81	-
306 (in isoform 2)	Ubiquitination	-	4.65	-
311 (in isoform 2)	Ubiquitination	-	28.89	-
329	Acetylation	RVKKNLLKKEYNVND HHHHHHHCCCCCCCC	46.88	7367247
329	Ubiquitination	RVKKNLLKKEYNVND HHHHHHHCCCCCCCC	46.88	-
330	Acetylation	VKKNLLKKEYNVNDD HHHHHHCCCCCCCCC	66.46	7367257
330	Ubiquitination	VKKNLLKKEYNVNDD HHHHHHCCCCCCCCC	66.46	-
340	Ubiquitination	NVNDDSMKLGGNNTS CCCCCCCCCCCCCHH	48.18	21890473
340 (in isoform 1)	Ubiquitination	-	48.18	21890473
349	Acetylation	GGNNTSEKADGLSKD CCCCHHHCCCCCCCC	52.09	26051181
349	Ubiquitination	GGNNTSEKADGLSKD CCCCHHHCCCCCCCC	52.09	21890473
349 (in isoform 1)	Ubiquitination	-	52.09	21890473
354	Phosphorylation	SEKADGLSKDASRCS HHCCCCCCCCHHHHC	33.74	-
355	Acetylation	EKADGLSKDASRCSE HCCCCCCCCHHHHCC	63.46	26051181
355	Ubiquitination	EKADGLSKDASRCSE HCCCCCCCCHHHHCC	63.46	-
361	Phosphorylation	SKDASRCSEQPSISD CCCHHHHCCCCCHHH	37.85	28555341
365	Phosphorylation	SRCSEQPSISDIKEK HHHCCCCCHHHHHHH	34.12	20860994
367	Phosphorylation	CSEQPSISDIKEKSK HCCCCCHHHHHHHHH	37.31	20860994
370	Ubiquitination	QPSISDIKEKSKFRM CCCHHHHHHHHHHCH	65.17	-
373	Phosphorylation	ISDIKEKSKFRMSEL HHHHHHHHHHCHHHH	37.81	18452278
378	Phosphorylation	EKSKFRMSELSSSRP HHHHHCHHHHHCCCC	31.00	25159151
381	Phosphorylation	KFRMSELSSSRPKRR HHCHHHHHCCCCCCC	23.40	25159151
382	Phosphorylation	FRMSELSSSRPKRRK HCHHHHHCCCCCCCH	42.88	28555341
390	Phosphorylation	SRPKRRKTAVQYIES CCCCCCHHHHHHHHC	30.19	30278072
394	Phosphorylation	RRKTAVQYIESSDSE CCHHHHHHHHCCCCH	10.48	30278072
397	Phosphorylation	TAVQYIESSDSEEIE HHHHHHHCCCCHHCC	29.86	25159151
398	Phosphorylation	AVQYIESSDSEEIET HHHHHHCCCCHHCCC	32.16	25159151
400	Phosphorylation	QYIESSDSEEIETSE HHHHCCCCHHCCCCC	38.79	25159151
401 (in isoform 2)	Ubiquitination	-	68.90	21890473
405	Phosphorylation	SDSEEIETSELPQKM CCCHHCCCCCCCHHH	32.91	28102081
406	Phosphorylation	DSEEIETSELPQKMK CCHHCCCCCCCHHHC	25.09	23663014
417	Sumoylation	QKMKGKLKNVQSETK HHHCHHHHCCCCCCC	59.57	-
417	Sumoylation	QKMKGKLKNVQSETK HHHCHHHHCCCCCCC	59.57	-
421	Phosphorylation	GKLKNVQSETKGRAK HHHHCCCCCCCCCCC	42.84	-
424	Ubiquitination	KNVQSETKGRAKAGS HCCCCCCCCCCCCCC	42.20	-
428	Ubiquitination	SETKGRAKAGSSKVI CCCCCCCCCCCCHHH	52.50	-
433	Ubiquitination	RAKAGSSKVIEDVAF CCCCCCCHHHHHHHH	49.26	-
442	Glutathionylation	IEDVAFACALTSSVP HHHHHHHHHHHCCCC	2.29	22555962
449 (in isoform 2)	Ubiquitination	-	35.98	21890473
452	Ubiquitination	TSSVPTTKKKMLKKG HCCCCCCHHHHHHCC	53.53	-
458	Ubiquitination	TKKKMLKKGACAVEG CHHHHHHCCCEEEEC	48.02	-
467	2-Hydroxyisobutyrylation	ACAVEGSKKTDVEER CEEEECCCCCCCCCC	71.23	-
469	Phosphorylation	AVEGSKKTDVEERPR EEECCCCCCCCCCCC	49.35	20068231
516 (in isoform 2)	Ubiquitination	-	44.75	21890473
523	Ubiquitination	REPALLSKQDIVLTT CCCHHCCCCCEEEEE	52.54	21890473
523 (in isoform 1)	Ubiquitination	-	52.54	21890473
531 (in isoform 2)	Ubiquitination	-	8.58	21890473
540 (in isoform 2)	Ubiquitination	-	26.14	21890473
541	Ubiquitination	LTHDYGTKGDSPLHS CCCCCCCCCCCCCHH	57.25	-
544	Phosphorylation	DYGTKGDSPLHSIRW CCCCCCCCCCHHHHH	37.72	27251275
548	Phosphorylation	KGDSPLHSIRWLRVI CCCCCCHHHHHHHHH	22.87	27251275
560 (in isoform 2)	Ubiquitination	-	18.88	21890473
571	Ubiquitination	NPNAQQTKAVLDLES CCCHHHCCEEEECCC	31.96	21890473
571 (in isoform 1)	Ubiquitination	-	31.96	21890473
601	Phosphorylation	KDLWSLLSFLKLKPF HHHHHHHHHHCCHHC	33.55	24719451
606	Ubiquitination	LLSFLKLKPFIDREW HHHHHCCHHCCCHHH	35.97	-
623	Phosphorylation	RTIQRPVTMGDEGGL HHCCCCCCCCCHHHH	20.37	26552605
635	Phosphorylation	GGLRRLQSLIKNITL HHHHHHHHHHHHCEE	36.33	23186163
638	Ubiquitination	RRLQSLIKNITLRRT HHHHHHHHHCEECCC	47.81	21906983
638 (in isoform 1)	Ubiquitination	-	47.81	21890473
641	Phosphorylation	QSLIKNITLRRTKTS HHHHHHCEECCCCCC	24.49	20068231
645	Phosphorylation	KNITLRRTKTSKIKG HHCEECCCCCCCCCC	32.04	20068231
653	Ubiquitination	KTSKIKGKPVLELPE CCCCCCCEEEEECCC	27.27	21906983
653 (in isoform 1)	Ubiquitination	-	27.27	21890473
662	Ubiquitination	VLELPERKVFIQHIT EEECCCCEEEEEEEE	39.57	21890473
662 (in isoform 1)	Ubiquitination	-	39.57	21890473
676	Ubiquitination	TLSDEERKIYQSVKN ECCHHHHHHHHHHHH	49.39	-
682	Ubiquitination	RKIYQSVKNEGRATI HHHHHHHHHCCCEEC	55.30	21906983
682 (in isoform 1)	Ubiquitination	-	55.30	21890473
719	Phosphorylation	LRQICCHTYLLTNAV HHHHHHHHHHHHHHH	11.27	20068231
720	Phosphorylation	RQICCHTYLLTNAVS HHHHHHHHHHHHHHH	3.97	20068231
723	Phosphorylation	CCHTYLLTNAVSSNG HHHHHHHHHHHHCCC	20.66	20068231
727	Phosphorylation	YLLTNAVSSNGPSGN HHHHHHHHCCCCCCC	18.71	27251275
728	Phosphorylation	LLTNAVSSNGPSGND HHHHHHHCCCCCCCC	38.93	26714015
732	Phosphorylation	AVSSNGPSGNDTPEE HHHCCCCCCCCCHHH	52.18	20068231
736	Phosphorylation	NGPSGNDTPEELRKK CCCCCCCCHHHHHHH	36.28	21712546
823	Ubiquitination	ELARDSEKKSDMEWT HHHCCCCCCCCCCCC	62.62	-
824	Ubiquitination	LARDSEKKSDMEWTS HHCCCCCCCCCCCCC	47.86	-
830 (in isoform 2)	Ubiquitination	-	12.86	21890473
837 (in isoform 2)	Ubiquitination	-	15.10	21890473
843	Phosphorylation	NALMHALTDLRKKNP HHHHHHHHHHHHHCC	33.50	20068231
858	Phosphorylation	NIKSLVVSQFTTFLS CHHHHHHHCHHHHHH	16.46	-
884	Phosphorylation	VFTRLDGSMAQKKRV EEEECCCHHHHHHCE	15.60	20860994
888	Acetylation	LDGSMAQKKRVESIQ CCCHHHHHHCEEEEE	32.77	25953088
889	Ubiquitination	DGSMAQKKRVESIQC CCHHHHHHCEEEEEE	49.98	-
911	Phosphorylation	SPTIMLLSLKAGGVG CCEEEEEEECCCCCC	24.70	24719451
925	Phosphorylation	GLNLSAASRVFLMDP CEECCHHCCEEEECC	28.79	20068231
952	Ubiquitination	RCHRLGQKQEVIITK HHHHCCCCCEEEEEE	46.78	21906983
952 (in isoform 1)	Ubiquitination	-	46.78	21890473
959	Ubiquitination	KQEVIITKFIVKDSV CCEEEEEEEEECCCH	23.76	21890473
959 (in isoform 1)	Ubiquitination	-	23.76	21890473
963	Acetylation	IITKFIVKDSVEENM EEEEEEECCCHHHHH	39.20	26051181
963	Ubiquitination	IITKFIVKDSVEENM EEEEEEECCCHHHHH	39.20	-
965	Phosphorylation	TKFIVKDSVEENMLK EEEEECCCHHHHHHH	26.22	20068231
972	Ubiquitination	SVEENMLKIQNKKRE CHHHHHHHHHHHHHH	31.32	-
987	Phosphorylation	LAAGAFGTKKPNADE HHHHCCCCCCCCHHH	29.46	20068231
988	Acetylation	AAGAFGTKKPNADEM HHHCCCCCCCCHHHH	67.61	23236377
988	Ubiquitination	AAGAFGTKKPNADEM HHHCCCCCCCCHHHH	67.61	-
989	Acetylation	AGAFGTKKPNADEMK HHCCCCCCCCHHHHH	43.26	26051181
989	Ubiquitination	AGAFGTKKPNADEMK HHCCCCCCCCHHHHH	43.26	-
996	Ubiquitination	KPNADEMKQAKINEI CCCHHHHHHHHHHHH	45.09	-
999	Ubiquitination	ADEMKQAKINEIRTL HHHHHHHHHHHHHHH	43.50	-

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
195	Y	Phosphorylation	Kinase	JAK2	O60674	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	CHFR	Q96EP1	PMID:20388495

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HLTF_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 HLTF_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCNA_HUMAN	PCNA	physical	18316726
UBE2N_HUMAN	UBE2N	physical	18316726
UB2V2_HUMAN	UBE2V2	physical	18316726
RAD18_HUMAN	RAD18	physical	18316726
SHPRH_HUMAN	SHPRH	physical	21396873
RAD18_HUMAN	RAD18	physical	21396873
SP1_HUMAN	SP1	physical	10391891
SP3_HUMAN	SP3	physical	10391891
DTL_HUMAN	DTL	physical	23555860
RAD18_HUMAN	RAD18	physical	23555860
BRCA1_HUMAN	BRCA1	physical	23901102
HSP7C_HUMAN	HSPA8	physical	21988832
ST1C2_HUMAN	SULT1C2	physical	21988832
UBC_HUMAN	UBC	physical	22904075
UB2V2_HUMAN	UBE2V2	physical	22904075
UBE2N_HUMAN	UBE2N	physical	22904075
PCNA_HUMAN	PCNA	physical	22904075
UBE2A_HUMAN	UBE2A	physical	22904075
HLTF_HUMAN	HLTF	physical	24198246
PCNA_HUMAN	PCNA	physical	26350214
FEN1_HUMAN	FEN1	genetic	28628639

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 HLTF_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-390; TYR-394; SER-397;SER-398; SER-400 AND THR-736, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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 SER-397; SER-398 ANDSER-400, AND MASS SPECTROMETRY.	18691976 [Abstract]
"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-397; SER-398 ANDSER-400, AND MASS SPECTROMETRY.	17081983 [Abstract]