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Q61191

- HCFC1_MOUSE

UniProt

Q61191 - HCFC1_MOUSE

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Protein

Host cell factor 1

Gene

Hcfc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in control of the cell cycle. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription respectively) together. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1019 – 10202Cleavage; by autolysisBy similarity
Sitei1081 – 10822Cleavage; by autolysisBy similarity
Sitei1110 – 11112Cleavage; by autolysisBy similarity
Sitei1304 – 13052Cleavage; by autolysisBy similarity
Sitei1332 – 13332Cleavage; by autolysisBy similarity
Sitei1432 – 14332Cleavage; by autolysisBy similarity

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. histone acetyltransferase activity (H4-K16 specific) Source: Ensembl
  3. histone acetyltransferase activity (H4-K5 specific) Source: Ensembl
  4. histone acetyltransferase activity (H4-K8 specific) Source: Ensembl
  5. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  6. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. histone H4-K16 acetylation Source: UniProtKB
  3. histone H4-K5 acetylation Source: UniProtKB
  4. histone H4-K8 acetylation Source: UniProtKB
  5. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  6. positive regulation of transcription from RNA polymerase II promoter Source: GOC
  7. protein stabilization Source: UniProtKB
  8. regulation of protein complex assembly Source: Ensembl
  9. release from viral latency Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

ReactomeiREACT_205251. Transcriptional activation of mitochondrial biogenesis.
REACT_226917. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:Hcfc1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:105942. Hcfc1.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication
Note: HCFC1R1 modulates its subcellular localization and overexpression of HCFC1R1 leads to accumulation of HCFC1 in the cytoplasm. Non-processed HCFC1 associates with chromatin. Colocalizes with CREB3 and CANX in the ER (By similarity).By similarity

GO - Cellular componenti

  1. Ada2/Gcn5/Ada3 transcription activator complex Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. histone acetyltransferase complex Source: UniProtKB
  4. mitochondrion Source: Ensembl
  5. MLL1 complex Source: UniProtKB
  6. MLL5-L complex Source: Ensembl
  7. neuronal cell body Source: UniProtKB
  8. nucleus Source: UniProtKB
  9. SAGA-type complex Source: Ensembl
  10. Set1C/COMPASS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 14321431HCF N-terminal chain 6By similarityPRO_0000016635Add
BLAST
Chaini2 – 13321331HCF N-terminal chain 5By similarityPRO_0000016636Add
BLAST
Chaini2 – 13041303HCF N-terminal chain 4By similarityPRO_0000016637Add
BLAST
Chaini2 – 11101109HCF N-terminal chain 3By similarityPRO_0000016638Add
BLAST
Chaini2 – 10811080HCF N-terminal chain 2By similarityPRO_0000016639Add
BLAST
Chaini2 – 10191018HCF N-terminal chain 1By similarityPRO_0000016640Add
BLAST
Chaini1020 – 20451026HCF C-terminal chain 1By similarityPRO_0000016641Add
BLAST
Chaini1082 – 2045964HCF C-terminal chain 2By similarityPRO_0000016642Add
BLAST
Chaini1111 – 2045935HCF C-terminal chain 3By similarityPRO_0000016643Add
BLAST
Chaini1305 – 2045741HCF C-terminal chain 4By similarityPRO_0000016644Add
BLAST
Chaini1333 – 2045713HCF C-terminal chain 5By similarityPRO_0000016645Add
BLAST
Chaini1433 – 2045613HCF C-terminal chain 6By similarityPRO_0000016646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei6 – 61PhosphoserineBy similarity
Cross-linki105 – 105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki163 – 163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki244 – 244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei288 – 2881N6-acetyllysine1 Publication
Cross-linki363 – 363Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei411 – 4111PhosphoserineBy similarity
Modified residuei666 – 6661PhosphoserineBy similarity
Modified residuei669 – 6691PhosphoserineBy similarity
Modified residuei813 – 8131N6-acetyllysineBy similarity
Modified residuei1204 – 12041PhosphoserineBy similarity
Modified residuei1500 – 15001PhosphothreonineBy similarity
Modified residuei1516 – 15161PhosphoserineBy similarity
Cross-linki1817 – 1817Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1818 – 1818Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei2015 – 20151N6-acetyllysineBy similarity

Post-translational modificationi

Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats. Cleavage is promoted by O-glycosylation (By similarity).By similarity
O-glycosylated. GlcNAcylation by OGT promotes proteolytic processing (By similarity).By similarity
Ubiquitinated. Lys-1817 and Lys-1818 are ubiquitinated both via 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. BAP1 mediated deubiquitination of 'Lys-48'-linked polyubiquitin chains; deubiquitination by BAP1 does not seem to stabilize the protein (By similarity).By similarity

Keywords - PTMi

Acetylation, Autocatalytic cleavage, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ61191.
PaxDbiQ61191.
PRIDEiQ61191.

PTM databases

PhosphoSiteiQ61191.

Expressioni

Tissue specificityi

Expressed in liver, pituitary gland, skeletal muscle, kidney, eye and brain (at protein level). Also observed at low level in heart, spleen and lung.2 Publications

Gene expression databases

BgeeiQ61191.
CleanExiMM_HCFC1.
ExpressionAtlasiQ61191. baseline and differential.
GenevestigatoriQ61191.

Interactioni

Subunit structurei

Composed predominantly of six polypeptides ranging from 110 to 150 kDa and a minor 300 kDa polypeptide. The majority of N- and C-terminal cleavage products remain tightly, albeit non-covalently, associated. Interacts with POU2F1, CREB3, ZBTB17, EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A, HDAC1, HDAC2, SUDS3), SAP30, SIN3B and FHL2. Component of a MLL1 complex, composed of at least the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, DPY30, E2F6, HCFC2, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8, PELP1, PHF20, PRP31, RING2, RUVBL1, RUVBL2, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Component of the MLL5-L complex, composed of at least KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts directly with OGT; the interaction, which requires the cleavage site domain, glycosylates and promotes proteolytic processing of HCFC1 and retains OGT in the nucleus. Interacts with TET2 and TET3. Interacts with HCFC1R1. Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L, CXXC1, HCFC1 and DPY30. Interacts (via HBM motif) with SETD1A. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (By similarity). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (By similarity). Interacts with THAP11.By similarity2 Publications

Protein-protein interaction databases

BioGridi200248. 9 interactions.
IntActiQ61191. 5 interactions.
MINTiMINT-4097262.
STRINGi10090.ENSMUSP00000110012.

Structurei

Secondary structure

1
2045
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1897 – 18993Combined sources
Beta strandi1905 – 19128Combined sources
Beta strandi1915 – 19217Combined sources
Beta strandi1924 – 19263Combined sources
Beta strandi1930 – 19389Combined sources
Beta strandi1965 – 19684Combined sources
Helixi1973 – 19775Combined sources
Beta strandi1984 – 199714Combined sources
Beta strandi2005 – 20106Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M26NMR-A1896-2020[»]
ProteinModelPortaliQ61191.
SMRiQ61191. Positions 360-400, 1821-2020.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati44 – 8946Kelch 1Sequence AnalysisAdd
BLAST
Repeati93 – 14048Kelch 2Sequence AnalysisAdd
BLAST
Repeati148 – 19447Kelch 3Sequence AnalysisAdd
BLAST
Repeati217 – 26549Kelch 4Sequence AnalysisAdd
BLAST
Repeati266 – 31348Kelch 5Sequence AnalysisAdd
BLAST
Domaini366 – 45792Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Repeati1010 – 103526HCF repeat 1Sequence AnalysisAdd
BLAST
Repeati1072 – 109726HCF repeat 2Sequence AnalysisAdd
BLAST
Repeati1101 – 112626HCF repeat 3Sequence AnalysisAdd
BLAST
Repeati1157 – 118226HCF repeat 4; degenerateAdd
BLAST
Repeati1295 – 132026HCF repeat 5Sequence AnalysisAdd
BLAST
Repeati1323 – 134826HCF repeat 6Sequence AnalysisAdd
BLAST
Repeati1358 – 138326HCF repeat 7; degenerateAdd
BLAST
Repeati1423 – 144826HCF repeat 8Sequence AnalysisAdd
BLAST
Domaini1808 – 189891Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1900 – 2016117Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni500 – 55051Required for interaction with OGTBy similarityAdd
BLAST
Regioni610 – 722113Interaction with SIN3ABy similarityAdd
BLAST
Regioni750 – 902153Interaction with ZBTB17By similarityAdd
BLAST
Regioni813 – 912100Interaction with GABP2By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi574 – 1500927Thr-richSequence AnalysisAdd
BLAST
Compositional biasi1622 – 167453Ala-richSequence AnalysisAdd
BLAST
Compositional biasi1684 – 172037Gln-richSequence AnalysisAdd
BLAST

Domaini

The HCF repeat is a highly specific proteolytic cleavage signal.By similarity
The kelch repeats fold into a 6-bladed kelch beta-propeller called the beta-propeller domain which mediates interaction with HCFC1R1.By similarity

Sequence similaritiesi

Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 5 Kelch repeats.Sequence Analysis

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000119086.
HOGENOMiHOG000293192.
HOVERGENiHBG051888.
InParanoidiQ61191.
KOiK14966.
OrthoDBiEOG790G05.
TreeFamiTF314757.

Family and domain databases

Gene3Di2.120.10.80. 2 hits.
2.60.40.10. 2 hits.
InterProiIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
[Graphical view]
PfamiPF01344. Kelch_1. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61191-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG
60 70 80 90 100
GNEGIVDELH VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM
110 120 130 140 150
VEYGKYSNDL YELQASRWEW KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY
160 170 180 190 200
LFGGLANDSE DPKNNIPRYL NDLYILELRP GSGVVAWDIP ITYGVLPPPR
210 220 230 240 250
ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIETL TWNKPSLSGV
260 270 280 290 300
APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN
310 320 330 340 350
LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ
360 370 380 390 400
VCCKDLWYLE TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY
410 420 430 440 450
DIPATAATAT SPTPNPVPSV PANPPKSPAP AAAAPAVQPL TQVGITLVPQ
460 470 480 490 500
AATAPPSTTT IQVLPTVPGS SISVPTAART QGVPAVLKVT GPQATTGTPL
510 520 530 540 550
VTMRPASQAG KAPVTVTSLP ASVRMVVPTQ SAQGTVIGSN PQMSGMAALA
560 570 580 590 600
AAAAATQKIP PSSAPTVLSV PAGTTIVKTV AVTPGTTTLP ATVKVASSPV
610 620 630 640 650
MVSNPATRML KTAAAQVGTS VSSAANTSTR PIITVHKSGT VTVAQQAQVV
660 670 680 690 700
TTVVGGVTKT ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ
710 720 730 740 750
ASTGPVTQII QTKGPLPAGT ILKLVTSADG KPTTIITTTQ ASGAGTKPTI
760 770 780 790 800
LGISSVSPST TKPGTTTIIK TIPMSAIITQ AGATGVTSSP GIKSPITIIT
810 820 830 840 850
TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG QPGTILRTVP
860 870 880 890 900
MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGAH
910 920 930 940 950
STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT
960 970 980 990 1000
MQPVSQPTQV TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG
1010 1020 1030 1040 1050
QGDVQPGTVT LVCSNPPCET HETGTTNTAT TTVVANLGGH PQPTQVQFVC
1060 1070 1080 1090 1100
DRQETAASLV TSAVGQQNGN VVRVCSNPPC ETHETGTTNT ATTATSNMAG
1110 1120 1130 1140 1150
QHGCSNPPCE THETGTTSTA TTAMSSMGTG QQRDTRRTTN TPTVVRITVA
1160 1170 1180 1190 1200
PGALERVQGT VKPQCQTQQT NMTTTTMTVQ ATGAPCSAGP LLRPSVALES
1210 1220 1230 1240 1250
GSHSPAFVQL ALPSVRVGLS GPSSKDMPTG RQPETYHTYT TNTPTTTRSI
1260 1270 1280 1290 1300
MVAGELGAAR VVPTSTYESL QASSPSSTMT MTALEALLCP SATVTQVCSN
1310 1320 1330 1340 1350
PPCETHETGT TNTATTSNAG SAQRVCSNPP CETHETGTTH TATTATSNGG
1360 1370 1380 1390 1400
AGQPEGGQQP ASGHPCETHQ TTSTGTTMSV SVGTLIPDAT SSHGTLESGL
1410 1420 1430 1440 1450
EVVAVPTVTS QAGSTLLASF PTQRVCSNPP CETHETGTTH TATTVTSNMS
1460 1470 1480 1490 1500
SNQDPPPAAS DQGEVASTQG DSTNITSASA ITTSVSSTLP RAVTTVTQST
1510 1520 1530 1540 1550
PVPGPSVPPP EELQVSPGPR QQLPPRQLLQ SASTPLMGES TEVLSASQTP
1560 1570 1580 1590 1600
ELQAAVDLSS TGDPSSGQEP TTSAVVATVV VQPPPPTQSE VDQLSLPQEL
1610 1620 1630 1640 1650
MAEAQAGTTT LMVTGLTPEE LAVTAAAEAA AQAAATEEAQ ALAIQAVLQA
1660 1670 1680 1690 1700
AQQAVMGTGE PMDTSEAAAA VTQAELGHLS AEGQEGQATT IPIVLTQQEL
1710 1720 1730 1740 1750
AALVQQQQQL QEAQAQAQQQ HHLPTEALAP ADSLNDPSIE SNCLNELASA
1760 1770 1780 1790 1800
VPSTVALLPS TATESLAPSN TFVAPQPVVA SPAKMQAAAT LTEVANGIES
1810 1820 1830 1840 1850
LGVKPDLPPP PSKAPVKKEN QWFDVGVIKG TSVMVTHYFL PPDDAVQSDD
1860 1870 1880 1890 1900
DSGTVPDYNQ LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF
1910 1920 1930 1940 1950
PGAPCAIKIS KSPDGAHLTW EPPSVTSGKI IEYSVYLAIQ SSQASGEPKS
1960 1970 1980 1990 2000
STPAQLAFMR VYCGPSPSCL VQSSSLSNAH IDYTTKPAII FRIAARNEKG
2010 2020 2030 2040
YGPATQVRWL QETSKDSSGT KPASKRPMSS PEMKSAPKKS KADGQ
Length:2,045
Mass (Da):210,437
Last modified:July 27, 2011 - v2
Checksum:iAD0EC38C9DB19F22
GO

Sequence cautioni

The sequence CAF25305.1 differs from that shown. Reason: Frameshift at position 339. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti483 – 4831V → R in AAB01163. (PubMed:9334261)Curated
Sequence conflicti483 – 4831V → R in AAD09225. (PubMed:9334261)Curated
Sequence conflicti520 – 5201P → S in CAF25305. 1 PublicationCurated
Sequence conflicti567 – 5682VL → AW in AAB01163. (PubMed:9334261)Curated
Sequence conflicti567 – 5682VL → AW in AAD09225. (PubMed:9334261)Curated
Sequence conflicti711 – 7111Q → H in AAD09225. (PubMed:9334261)Curated
Sequence conflicti1104 – 11041C → S in AAB01163. (PubMed:9334261)Curated
Sequence conflicti1104 – 11041C → S in AAD09225. (PubMed:9334261)Curated
Sequence conflicti1230 – 12301G → A in AAB01163. (PubMed:9334261)Curated
Sequence conflicti1230 – 12301G → A in AAD09225. (PubMed:9334261)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53925 Genomic DNA. Translation: AAB01163.1.
U80821 Genomic DNA. Translation: AAD09225.1.
AL672002 Genomic DNA. Translation: CAM18726.1.
CH466650 Genomic DNA. Translation: EDL29851.1.
BC053742 mRNA. Translation: AAH53742.1.
AK088827 mRNA. Translation: BAC40597.1.
AJ627036 mRNA. Translation: CAF25305.1. Frameshift.
CCDSiCCDS30218.1.
RefSeqiNP_032250.2. NM_008224.4.
UniGeneiMm.491126.

Genome annotation databases

EnsembliENSMUST00000033761; ENSMUSP00000033761; ENSMUSG00000031386.
GeneIDi15161.
KEGGimmu:15161.
UCSCiuc009tnm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53925 Genomic DNA. Translation: AAB01163.1 .
U80821 Genomic DNA. Translation: AAD09225.1 .
AL672002 Genomic DNA. Translation: CAM18726.1 .
CH466650 Genomic DNA. Translation: EDL29851.1 .
BC053742 mRNA. Translation: AAH53742.1 .
AK088827 mRNA. Translation: BAC40597.1 .
AJ627036 mRNA. Translation: CAF25305.1 . Frameshift.
CCDSi CCDS30218.1.
RefSeqi NP_032250.2. NM_008224.4.
UniGenei Mm.491126.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2M26 NMR - A 1896-2020 [» ]
ProteinModelPortali Q61191.
SMRi Q61191. Positions 360-400, 1821-2020.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200248. 9 interactions.
IntActi Q61191. 5 interactions.
MINTi MINT-4097262.
STRINGi 10090.ENSMUSP00000110012.

PTM databases

PhosphoSitei Q61191.

Proteomic databases

MaxQBi Q61191.
PaxDbi Q61191.
PRIDEi Q61191.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033761 ; ENSMUSP00000033761 ; ENSMUSG00000031386 .
GeneIDi 15161.
KEGGi mmu:15161.
UCSCi uc009tnm.1. mouse.

Organism-specific databases

CTDi 3054.
MGIi MGI:105942. Hcfc1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000119086.
HOGENOMi HOG000293192.
HOVERGENi HBG051888.
InParanoidi Q61191.
KOi K14966.
OrthoDBi EOG790G05.
TreeFami TF314757.

Enzyme and pathway databases

Reactomei REACT_205251. Transcriptional activation of mitochondrial biogenesis.
REACT_226917. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi Hcfc1. mouse.
NextBioi 287652.
PROi Q61191.
SOURCEi Search...

Gene expression databases

Bgeei Q61191.
CleanExi MM_HCFC1.
ExpressionAtlasi Q61191. baseline and differential.
Genevestigatori Q61191.

Family and domain databases

Gene3Di 2.120.10.80. 2 hits.
2.60.40.10. 2 hits.
InterProi IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
[Graphical view ]
Pfami PF01344. Kelch_1. 1 hit.
[Graphical view ]
SMARTi SM00060. FN3. 2 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 1 hit.
PROSITEi PS50853. FN3. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse homologue of the human transcription factor C1 (host cell factor). Conservation of forms and function."
    Kristie T.M.
    J. Biol. Chem. 272:26749-26755(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
    Tissue: Fetal liver1 Publication.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Limb mesenchyme1 Publication.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-209.
    Strain: NOD.
    Tissue: Thymus.
  6. "Towards functional annotation of all Xq28 genes: expression and intracellular localization analyses reveal novel candidates for disease genes."
    Kolb A.A., Mehrle A., Bechtel S., Wellenreuther R., Simpson J., Pepperkok R., Wiemann S., Poustka A.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 165-520.
    Strain: NMRI.
    Tissue: Embryo.
  7. "Nuclear localization of the C1 factor (host cell factor) in sensory neurons correlates with reactivation of herpes simplex virus from latency."
    Kristie T.M., Vogel J.L., Sears A.E.
    Proc. Natl. Acad. Sci. U.S.A. 96:1229-1233(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: BALB/c1 Publication.
  8. "O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry."
    Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  9. "Ronin is essential for embryogenesis and the pluripotency of mouse embryonic stem cells."
    Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F., Songyang Z., Thomson J.A., Zwaka T.P.
    Cell 133:1162-1174(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THAP11.
  10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHCFC1_MOUSE
AccessioniPrimary (citable) accession number: Q61191
Secondary accession number(s): B1AUX1
, Q684R1, Q7TSB0, Q8C2D0, Q9QWH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3