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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 autolysis By similarityBy similarity
Sitei1081 – 10822Cleavage; by autolysis By similarityBy similarity
Sitei1110 – 11112Cleavage; by autolysis By similarityBy similarity
Sitei1304 – 13052Cleavage; by autolysis By similarityBy similarity
Sitei1332 – 13332Cleavage; by autolysis By similarityBy similarity
Sitei1432 – 14332Cleavage; by autolysis By similarityBy 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. protein binding Source: UniProtKB
  6. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  7. 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:Hcfc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:105942. Hcfc1.

Subcellular locationi

Nucleus. Cytoplasm
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.1 Publication

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 – 11Removed By similarity
Chaini2 – 14321431HCF N-terminal chain 6 By similarityPRO_0000016635Add
BLAST
Chaini2 – 13321331HCF N-terminal chain 5 By similarityPRO_0000016636Add
BLAST
Chaini2 – 13041303HCF N-terminal chain 4 By similarityPRO_0000016637Add
BLAST
Chaini2 – 11101109HCF N-terminal chain 3 By similarityPRO_0000016638Add
BLAST
Chaini2 – 10811080HCF N-terminal chain 2 By similarityPRO_0000016639Add
BLAST
Chaini2 – 10191018HCF N-terminal chain 1 By similarityPRO_0000016640Add
BLAST
Chaini1020 – 20451026HCF C-terminal chain 1 By similarityBy similarityPRO_0000016641Add
BLAST
Chaini1082 – 2045964HCF C-terminal chain 2 By similarityBy similarityPRO_0000016642Add
BLAST
Chaini1111 – 2045935HCF C-terminal chain 3 By similarityBy similarityPRO_0000016643Add
BLAST
Chaini1305 – 2045741HCF C-terminal chain 4 By similarityBy similarityPRO_0000016644Add
BLAST
Chaini1333 – 2045713HCF C-terminal chain 5 By similarityBy similarityPRO_0000016645Add
BLAST
Chaini1433 – 2045613HCF C-terminal chain 6 By similarityBy similarityPRO_0000016646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei6 – 61Phosphoserine By 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 – 4111Phosphoserine By similarity
Modified residuei666 – 6661Phosphoserine By similarity
Modified residuei669 – 6691Phosphoserine By similarity
Modified residuei813 – 8131N6-acetyllysine By similarity
Modified residuei1204 – 12041Phosphoserine By similarity
Modified residuei1500 – 15001Phosphothreonine By similarity
Modified residuei1516 – 15161Phosphoserine By 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-acetyllysine By 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.
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.

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

ArrayExpressiQ61191.
BgeeiQ61191.
CleanExiMM_HCFC1.
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. 4 interactions.
MINTiMINT-4097262.
STRINGi10090.ENSMUSP00000110012.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M26NMR-A1896-2020[»]
ProteinModelPortaliQ61191.
SMRiQ61191. Positions 360-400, 1821-2020.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni500 – 55051Required for interaction with OGT By similarityAdd
BLAST
Regioni610 – 722113Interaction with SIN3A By similarityAdd
BLAST
Regioni750 – 902153Interaction with ZBTB17 By similarityAdd
BLAST
Regioni813 – 912100Interaction with GABP2 By similarityAdd
BLAST

Compositional bias

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

Domaini

The HCF repeat is a highly specific proteolytic cleavage signal By similarity.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 5 Kelch repeats.

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00720000108539.
HOGENOMiHOG000293192.
HOVERGENiHBG051888.
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

MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG     50
GNEGIVDELH VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM 100
VEYGKYSNDL YELQASRWEW KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY 150
LFGGLANDSE DPKNNIPRYL NDLYILELRP GSGVVAWDIP ITYGVLPPPR 200
ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIETL TWNKPSLSGV 250
APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN 300
LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ 350
VCCKDLWYLE TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY 400
DIPATAATAT SPTPNPVPSV PANPPKSPAP AAAAPAVQPL TQVGITLVPQ 450
AATAPPSTTT IQVLPTVPGS SISVPTAART QGVPAVLKVT GPQATTGTPL 500
VTMRPASQAG KAPVTVTSLP ASVRMVVPTQ SAQGTVIGSN PQMSGMAALA 550
AAAAATQKIP PSSAPTVLSV PAGTTIVKTV AVTPGTTTLP ATVKVASSPV 600
MVSNPATRML KTAAAQVGTS VSSAANTSTR PIITVHKSGT VTVAQQAQVV 650
TTVVGGVTKT ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ 700
ASTGPVTQII QTKGPLPAGT ILKLVTSADG KPTTIITTTQ ASGAGTKPTI 750
LGISSVSPST TKPGTTTIIK TIPMSAIITQ AGATGVTSSP GIKSPITIIT 800
TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG QPGTILRTVP 850
MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGAH 900
STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT 950
MQPVSQPTQV TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG 1000
QGDVQPGTVT LVCSNPPCET HETGTTNTAT TTVVANLGGH PQPTQVQFVC 1050
DRQETAASLV TSAVGQQNGN VVRVCSNPPC ETHETGTTNT ATTATSNMAG 1100
QHGCSNPPCE THETGTTSTA TTAMSSMGTG QQRDTRRTTN TPTVVRITVA 1150
PGALERVQGT VKPQCQTQQT NMTTTTMTVQ ATGAPCSAGP LLRPSVALES 1200
GSHSPAFVQL ALPSVRVGLS GPSSKDMPTG RQPETYHTYT TNTPTTTRSI 1250
MVAGELGAAR VVPTSTYESL QASSPSSTMT MTALEALLCP SATVTQVCSN 1300
PPCETHETGT TNTATTSNAG SAQRVCSNPP CETHETGTTH TATTATSNGG 1350
AGQPEGGQQP ASGHPCETHQ TTSTGTTMSV SVGTLIPDAT SSHGTLESGL 1400
EVVAVPTVTS QAGSTLLASF PTQRVCSNPP CETHETGTTH TATTVTSNMS 1450
SNQDPPPAAS DQGEVASTQG DSTNITSASA ITTSVSSTLP RAVTTVTQST 1500
PVPGPSVPPP EELQVSPGPR QQLPPRQLLQ SASTPLMGES TEVLSASQTP 1550
ELQAAVDLSS TGDPSSGQEP TTSAVVATVV VQPPPPTQSE VDQLSLPQEL 1600
MAEAQAGTTT LMVTGLTPEE LAVTAAAEAA AQAAATEEAQ ALAIQAVLQA 1650
AQQAVMGTGE PMDTSEAAAA VTQAELGHLS AEGQEGQATT IPIVLTQQEL 1700
AALVQQQQQL QEAQAQAQQQ HHLPTEALAP ADSLNDPSIE SNCLNELASA 1750
VPSTVALLPS TATESLAPSN TFVAPQPVVA SPAKMQAAAT LTEVANGIES 1800
LGVKPDLPPP PSKAPVKKEN QWFDVGVIKG TSVMVTHYFL PPDDAVQSDD 1850
DSGTVPDYNQ LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF 1900
PGAPCAIKIS KSPDGAHLTW EPPSVTSGKI IEYSVYLAIQ SSQASGEPKS 1950
STPAQLAFMR VYCGPSPSCL VQSSSLSNAH IDYTTKPAII FRIAARNEKG 2000
YGPATQVRWL QETSKDSSGT KPASKRPMSS PEMKSAPKKS KADGQ 2045
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.

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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. 4 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 ENSGT00720000108539.
HOGENOMi HOG000293192.
HOVERGENi HBG051888.
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

ArrayExpressi Q61191.
Bgeei Q61191.
CleanExi MM_HCFC1.
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 liver.
  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 mesenchyme.
  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/c.
  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: September 3, 2014
This is version 137 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

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