Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Helicase-like transcription factor

Gene

HLTF

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity6 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi38 – 287250Add
BLAST
Nucleotide bindingi294 – 3018ATPPROSITE-ProRule annotation
Zinc fingeri760 – 80142RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Helicase, Hydrolase, Ligase

Keywords - Biological processi

Transcription, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Helicase-like transcription factor (EC:3.6.4.-, EC:6.3.2.-)
Alternative name(s):
DNA-binding protein/plasminogen activator inhibitor 1 regulator
HIP116
RING finger protein 80
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3
Sucrose nonfermenting protein 2-like 3
Gene namesi
Name:HLTF
Synonyms:HIP116A, RNF80, SMARCA3, SNF2L3, ZBU1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11099. HLTF.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35949.

Polymorphism and mutation databases

BioMutaiHLTF.
DMDMi60390864.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10091009Helicase-like transcription factorPRO_0000030722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei195 – 1951Phosphotyrosine; by JAK21 Publication
Modified residuei397 – 3971PhosphoserineCombined sources
Modified residuei398 – 3981PhosphoserineCombined sources
Modified residuei400 – 4001PhosphoserineCombined sources
Modified residuei736 – 7361PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ14527.
MaxQBiQ14527.
PaxDbiQ14527.
PeptideAtlasiQ14527.
PRIDEiQ14527.

PTM databases

iPTMnetiQ14527.
PhosphoSiteiQ14527.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle.2 Publications

Gene expression databases

BgeeiQ14527.
CleanExiHS_HLTF.
ExpressionAtlasiQ14527. baseline and differential.
GenevisibleiQ14527. HS.

Organism-specific databases

HPAiHPA015284.
HPA049001.

Interactioni

Subunit structurei

Interacts with SP1 and SP3 independently of DNA; the interaction with these transcriptional factors may be required for basal transcription of target genes. Interacts with EGR1; the interaction requires prior binding to DNA and represses c-Rel via a DNA looping mechanism (By similarity). Interacts with GATA4 (By similarity). Interacts with PCNA; the interaction promotes polyubiquitination of PCNA through association with the UBE2B-RAD18 and UBE2V2-UBE2N ubiquitin ligase complexes. Interacts with RAD18, SHPRH, UBE2V2 and UBE2N.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
S100A10P609032EBI-1045161,EBI-717048

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: MGI

Protein-protein interaction databases

BioGridi112480. 51 interactions.
DIPiDIP-29828N.
IntActiQ14527. 22 interactions.
MINTiMINT-1639589.
STRINGi9606.ENSP00000308944.

Structurei

Secondary structure

1
1009
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi51 – 555Combined sources
Beta strandi58 – 6811Combined sources
Helixi70 – 723Combined sources
Beta strandi81 – 877Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi107 – 1115Combined sources
Helixi113 – 12412Combined sources
Beta strandi129 – 1346Combined sources
Beta strandi141 – 15212Combined sources
Helixi154 – 1563Combined sources
Helixi157 – 16610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L1INMR-A51-171[»]
2MZNNMR-A51-171[»]
4HREX-ray2.79G/H/K/L26-39[»]
4HRHX-ray3.00C/D26-39[»]
4S0NX-ray1.50A/B/C/D55-180[»]
4XZFX-ray1.38A58-174[»]
4XZGX-ray2.40A/B/C/D/E/F/G/H/I57-174[»]
5BNHX-ray1.70A/D55-175[»]
ProteinModelPortaliQ14527.
SMRiQ14527. Positions 57-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini435 – 606172Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini837 – 996160Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni925 – 100985Interaction with SP1 and SP3Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi557 – 5604DEGH box

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri760 – 80142RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1001. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00830000128423.
HOVERGENiHBG079192.
InParanoidiQ14527.
KOiK15711.
OMAiNDDAMKL.
OrthoDBiEOG761BT4.
PhylomeDBiQ14527.
TreeFamiTF332703.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.300. 3 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014905. HIRAN.
IPR030065. HLTF.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR10799:SF762. PTHR10799:SF762. 6 hits.
PfamiPF00271. Helicase_C. 1 hit.
PF08797. HIRAN. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00910. HIRAN. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q14527-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSWMFKRDPV WKYLQTVQYG VHGNFPRLSY PTFFPRFEFQ DVIPPDDFLT
60 70 80 90 100
SDEEVDSVLF GSLRGHVVGL RYYTGVVNNN EMVALQRDPN NPYDKNAIKV
110 120 130 140 150
NNVNGNQVGH LKKELAGALA YIMDNKLAQI EGVVPFGANN AFTMPLHMTF
160 170 180 190 200
WGKEENRKAV SDQLKKHGFK LGPAPKTLGF NLESGWGSGR AGPSYSMPVH
210 220 230 240 250
AAVQMTTEQL KTEFDKLFED LKEDDKTHEM EPAEAIETPL LPHQKQALAW
260 270 280 290 300
MVSRENSKEL PPFWEQRNDL YYNTITNFSE KDRPENVHGG ILADDMGLGK
310 320 330 340 350
TLTAIAVILT NFHDGRPLPI ERVKKNLLKK EYNVNDDSMK LGGNNTSEKA
360 370 380 390 400
DGLSKDASRC SEQPSISDIK EKSKFRMSEL SSSRPKRRKT AVQYIESSDS
410 420 430 440 450
EEIETSELPQ KMKGKLKNVQ SETKGRAKAG SSKVIEDVAF ACALTSSVPT
460 470 480 490 500
TKKKMLKKGA CAVEGSKKTD VEERPRTTLI ICPLSVLSNW IDQFGQHIKS
510 520 530 540 550
DVHLNFYVYY GPDRIREPAL LSKQDIVLTT YNILTHDYGT KGDSPLHSIR
560 570 580 590 600
WLRVILDEGH AIRNPNAQQT KAVLDLESER RWVLTGTPIQ NSLKDLWSLL
610 620 630 640 650
SFLKLKPFID REWWHRTIQR PVTMGDEGGL RRLQSLIKNI TLRRTKTSKI
660 670 680 690 700
KGKPVLELPE RKVFIQHITL SDEERKIYQS VKNEGRATIG RYFNEGTVLA
710 720 730 740 750
HYADVLGLLL RLRQICCHTY LLTNAVSSNG PSGNDTPEEL RKKLIRKMKL
760 770 780 790 800
ILSSGSDEEC AICLDSLTVP VITHCAHVFC KPCICQVIQN EQPHAKCPLC
810 820 830 840 850
RNDIHEDNLL ECPPEELARD SEKKSDMEWT SSSKINALMH ALTDLRKKNP
860 870 880 890 900
NIKSLVVSQF TTFLSLIEIP LKASGFVFTR LDGSMAQKKR VESIQCFQNT
910 920 930 940 950
EAGSPTIMLL SLKAGGVGLN LSAASRVFLM DPAWNPAAED QCFDRCHRLG
960 970 980 990 1000
QKQEVIITKF IVKDSVEENM LKIQNKKREL AAGAFGTKKP NADEMKQAKI

NEIRTLIDL
Length:1,009
Mass (Da):113,929
Last modified:March 1, 2005 - v2
Checksum:i0AB96F6C8484FD15
GO
Isoform 2 (identifier: Q14527-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.

Note: No experimental confirmation available.
Show »
Length:887
Mass (Da):99,919
Checksum:i7E4C330C2CF9DA4E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351P → L in CAA86571 (PubMed:8672239).Curated
Sequence conflicti211 – 2133KTE → PEF in AAB27691 (PubMed:8342330).Curated
Sequence conflicti337 – 3371D → G in CAA86571 (PubMed:8672239).Curated
Sequence conflicti337 – 3371D → G in CAA86572 (PubMed:8672239).Curated
Sequence conflicti337 – 3371D → G in CAD10805 (Ref. 3) Curated
Sequence conflicti382 – 3821S → T in AAA67436 (PubMed:7876228).Curated
Sequence conflicti429 – 4291Missing in AAH44659 (PubMed:15489334).Curated
Sequence conflicti913 – 9131K → R in CAA86571 (PubMed:8672239).Curated
Sequence conflicti913 – 9131K → R in CAA86572 (PubMed:8672239).Curated
Sequence conflicti913 – 9131K → R in CAD10805 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti311 – 3111N → S.
Corresponds to variant rs2305868 [ dbSNP | Ensembl ].
VAR_052121
Natural varianti362 – 3621E → Q.
Corresponds to variant rs2228257 [ dbSNP | Ensembl ].
VAR_052122
Natural varianti819 – 8191R → H.
Corresponds to variant rs2229361 [ dbSNP | Ensembl ].
VAR_029265

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 122122Missing in isoform 2. 1 PublicationVSP_018873Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34673 mRNA. Translation: AAA67436.1.
Z46606 mRNA. Translation: CAA86571.1.
Z46606 mRNA. Translation: CAA86572.1.
AJ418064 Genomic DNA. Translation: CAD10805.1.
CH471052 Genomic DNA. Translation: EAW78889.1.
CH471052 Genomic DNA. Translation: EAW78892.1.
CH471052 Genomic DNA. Translation: EAW78893.1.
BC044659 mRNA. Translation: AAH44659.1.
S64671 mRNA. Translation: AAB27691.1.
CCDSiCCDS33875.1. [Q14527-1]
PIRiS49618.
RefSeqiNP_001305863.1. NM_001318934.1.
NP_001305864.1. NM_001318935.1. [Q14527-1]
NP_003062.2. NM_003071.3. [Q14527-1]
NP_620636.1. NM_139048.2. [Q14527-1]
UniGeneiHs.3068.

Genome annotation databases

EnsembliENST00000310053; ENSP00000308944; ENSG00000071794. [Q14527-1]
ENST00000392912; ENSP00000376644; ENSG00000071794. [Q14527-1]
ENST00000494055; ENSP00000420429; ENSG00000071794. [Q14527-1]
GeneIDi6596.
KEGGihsa:6596.
UCSCiuc003ewq.2. human. [Q14527-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L34673 mRNA. Translation: AAA67436.1.
Z46606 mRNA. Translation: CAA86571.1.
Z46606 mRNA. Translation: CAA86572.1.
AJ418064 Genomic DNA. Translation: CAD10805.1.
CH471052 Genomic DNA. Translation: EAW78889.1.
CH471052 Genomic DNA. Translation: EAW78892.1.
CH471052 Genomic DNA. Translation: EAW78893.1.
BC044659 mRNA. Translation: AAH44659.1.
S64671 mRNA. Translation: AAB27691.1.
CCDSiCCDS33875.1. [Q14527-1]
PIRiS49618.
RefSeqiNP_001305863.1. NM_001318934.1.
NP_001305864.1. NM_001318935.1. [Q14527-1]
NP_003062.2. NM_003071.3. [Q14527-1]
NP_620636.1. NM_139048.2. [Q14527-1]
UniGeneiHs.3068.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L1INMR-A51-171[»]
2MZNNMR-A51-171[»]
4HREX-ray2.79G/H/K/L26-39[»]
4HRHX-ray3.00C/D26-39[»]
4S0NX-ray1.50A/B/C/D55-180[»]
4XZFX-ray1.38A58-174[»]
4XZGX-ray2.40A/B/C/D/E/F/G/H/I57-174[»]
5BNHX-ray1.70A/D55-175[»]
ProteinModelPortaliQ14527.
SMRiQ14527. Positions 57-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112480. 51 interactions.
DIPiDIP-29828N.
IntActiQ14527. 22 interactions.
MINTiMINT-1639589.
STRINGi9606.ENSP00000308944.

PTM databases

iPTMnetiQ14527.
PhosphoSiteiQ14527.

Polymorphism and mutation databases

BioMutaiHLTF.
DMDMi60390864.

Proteomic databases

EPDiQ14527.
MaxQBiQ14527.
PaxDbiQ14527.
PeptideAtlasiQ14527.
PRIDEiQ14527.

Protocols and materials databases

DNASUi6596.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310053; ENSP00000308944; ENSG00000071794. [Q14527-1]
ENST00000392912; ENSP00000376644; ENSG00000071794. [Q14527-1]
ENST00000494055; ENSP00000420429; ENSG00000071794. [Q14527-1]
GeneIDi6596.
KEGGihsa:6596.
UCSCiuc003ewq.2. human. [Q14527-1]

Organism-specific databases

CTDi6596.
GeneCardsiHLTF.
H-InvDBHIX0024319.
HGNCiHGNC:11099. HLTF.
HPAiHPA015284.
HPA049001.
MIMi603257. gene.
neXtProtiNX_Q14527.
PharmGKBiPA35949.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1001. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00830000128423.
HOVERGENiHBG079192.
InParanoidiQ14527.
KOiK15711.
OMAiNDDAMKL.
OrthoDBiEOG761BT4.
PhylomeDBiQ14527.
TreeFamiTF332703.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiHLTF. human.
GeneWikiiHLTF.
GenomeRNAii6596.
PROiQ14527.
SOURCEiSearch...

Gene expression databases

BgeeiQ14527.
CleanExiHS_HLTF.
ExpressionAtlasiQ14527. baseline and differential.
GenevisibleiQ14527. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.40.50.300. 3 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014905. HIRAN.
IPR030065. HLTF.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR10799:SF762. PTHR10799:SF762. 6 hits.
PfamiPF00271. Helicase_C. 1 hit.
PF08797. HIRAN. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00910. HIRAN. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 4 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of an SNF2/SWI2-related protein that binds specifically to the SPH motifs of the SV40 enhancer and to the HIV-1 promoter."
    Sheridan P.L., Schorpp M., Voz M.L., Jones K.A.
    J. Biol. Chem. 270:4575-4587(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Cervix carcinoma.
  2. "Characterization of a helicase-like transcription factor involved in the expression of the human plasminogen activator inhibitor-1 gene."
    Ding H., Descheemaeker K., Marynen P., Nelles L., Carvalho T., Carmo-Fonseca M., Collen D., Belayew A.
    DNA Cell Biol. 15:429-442(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "Characterization of the human SMARCA3/HLTF gene."
    Ribaucour F., Wiedig M., Benotmane A.M., Coppee F., Belayew A.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  6. "On the regulation of the plasminogen activator inhibitor-1 gene expression."
    Descheemaeker K.
    Verh. K. Acad. Geneeskd. Belg. 55:225-264(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-213.
  7. "Developmental regulation of Zbu1, a DNA-binding member of the SWI2/SNF2 family."
    Gong X., Kaushal S., Ceccarelli E., Bogdanova N., Neville C., Nguyen T., Clark H., Khatib Z.A., Valentine M., Look A.T., Rosenthal N.
    Dev. Biol. 183:166-182(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "Functional interactions between Sp1 or Sp3 and the helicase-like transcription factor mediate basal expression from the human plasminogen activator inhibitor-1 gene."
    Ding H., Benotmane A.M., Suske G., Collen D., Belayew A.
    J. Biol. Chem. 274:19573-19580(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SP1 AND SP3.
  9. Cited for: EPIGENETIC INACTIVATION IN COLON CANCER.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-398; SER-400 AND THR-736, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination."
    Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L., Prakash S., Haracska L.
    Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, INTERACTION WITH PCNA; UBE2N AND RAD18.
  13. "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks."
    Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.
    Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, INTERACTION WITH PCNA; RAD18; SHPRH AND UBE2N.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Prolactin induces Jak2 phosphorylation of RUSHY195."
    Helmer R.A., Dertien J.S., Chilton B.S.
    Mol. Cell. Endocrinol. 338:79-83(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-195.
  18. "NMR structure of the HLTF hiran domain."
    Structural genomics consortium (SGC)
    Submitted (OCT-2010) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 51-171.

Entry informationi

Entry nameiHLTF_HUMAN
AccessioniPrimary (citable) accession number: Q14527
Secondary accession number(s): D3DNH3
, Q14536, Q16051, Q7KYJ6, Q86YA5, Q92652, Q96KM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: July 6, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Subject to frequent epigenetic inactivation by promoter methylation in colon cancer.

Caution

In contrast with other SMARC proteins, there is currently no evidence that it associates with actin or actin-related proteins. It may rather act as a sequence-specific DNA binding ATPase, whose precise function remains to be fully characterized.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.