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Protein

Host cell factor 1

Gene

Hcfc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

ReactomeiR-MMU-2151201. Transcriptional activation of mitochondrial biogenesis.
R-MMU-3214847. HATs acetylate histones.
R-MMU-5689603. UCH proteinases.

Names & Taxonomyi

Protein namesi
Gene namesi
Name:Hcfc1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000166352 – 1432HCF N-terminal chain 6By similarityAdd BLAST1431
ChainiPRO_00000166362 – 1332HCF N-terminal chain 5By similarityAdd BLAST1331
ChainiPRO_00000166372 – 1304HCF N-terminal chain 4By similarityAdd BLAST1303
ChainiPRO_00000166382 – 1110HCF N-terminal chain 3By similarityAdd BLAST1109
ChainiPRO_00000166392 – 1081HCF N-terminal chain 2By similarityAdd BLAST1080
ChainiPRO_00000166402 – 1019HCF N-terminal chain 1By similarityAdd BLAST1018
ChainiPRO_00000166411020 – 2045HCF C-terminal chain 1By similarityAdd BLAST1026
ChainiPRO_00000166421082 – 2045HCF C-terminal chain 2By similarityAdd BLAST964
ChainiPRO_00000166431111 – 2045HCF C-terminal chain 3By similarityAdd BLAST935
ChainiPRO_00000166441305 – 2045HCF C-terminal chain 4By similarityAdd BLAST741
ChainiPRO_00000166451333 – 2045HCF C-terminal chain 5By similarityAdd BLAST713
ChainiPRO_00000166461433 – 2045HCF C-terminal chain 6By similarityAdd BLAST613

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei6PhosphoserineBy similarity1
Cross-linki105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei288N6-acetyllysineCombined sources1
Cross-linki363Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei411PhosphoserineBy similarity1
Modified residuei504Omega-N-methylarginineCombined sources1
Modified residuei524Omega-N-methylarginineCombined sources1
Modified residuei598PhosphoserineBy similarity1
Modified residuei666PhosphoserineCombined sources1
Modified residuei669PhosphoserineBy similarity1
Modified residuei813N6-acetyllysineBy similarity1
Modified residuei1204PhosphoserineBy similarity1
Modified residuei1216Asymmetric dimethylarginineCombined sources1
Modified residuei1223PhosphoserineBy similarity1
Modified residuei1500PhosphothreonineBy similarity1
Modified residuei1506PhosphoserineBy similarity1
Modified residuei1516PhosphoserineCombined sources1
Modified residuei1781PhosphoserineBy similarity1
Cross-linki1817Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1818Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei1848PhosphoserineCombined sources1
Modified residuei2015N6-acetyllysineBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1019 – 1020Cleavage; by autolysisBy similarity2
Sitei1081 – 1082Cleavage; by autolysisBy similarity2
Sitei1110 – 1111Cleavage; by autolysisBy similarity2
Sitei1304 – 1305Cleavage; by autolysisBy similarity2
Sitei1332 – 1333Cleavage; by autolysisBy similarity2
Sitei1432 – 1433Cleavage; by autolysisBy similarity2

Keywords - PTMi

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

Proteomic databases

EPDiQ61191.
MaxQBiQ61191.
PaxDbiQ61191.
PeptideAtlasiQ61191.
PRIDEiQ61191.

PTM databases

iPTMnetiQ61191.
PhosphoSitePlusiQ61191.

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

BgeeiENSMUSG00000031386.
CleanExiMM_HCFC1.
ExpressionAtlasiQ61191. baseline and differential.
GenevisibleiQ61191. MM.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200248. 10 interactors.
IntActiQ61191. 4 interactors.
MINTiMINT-4097262.
STRINGi10090.ENSMUSP00000033761.

Structurei

Secondary structure

12045
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1897 – 1899Combined sources3
Beta strandi1905 – 1912Combined sources8
Beta strandi1915 – 1921Combined sources7
Beta strandi1924 – 1926Combined sources3
Beta strandi1930 – 1938Combined sources9
Beta strandi1965 – 1968Combined sources4
Helixi1973 – 1977Combined sources5
Beta strandi1984 – 1997Combined sources14
Beta strandi2005 – 2010Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M26NMR-A1896-2020[»]
ProteinModelPortaliQ61191.
SMRiQ61191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati44 – 89Kelch 1Sequence analysisAdd BLAST46
Repeati93 – 140Kelch 2Sequence analysisAdd BLAST48
Repeati148 – 194Kelch 3Sequence analysisAdd BLAST47
Repeati217 – 265Kelch 4Sequence analysisAdd BLAST49
Repeati266 – 313Kelch 5Sequence analysisAdd BLAST48
Domaini366 – 457Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST92
Repeati1010 – 1035HCF repeat 1Sequence analysisAdd BLAST26
Repeati1072 – 1097HCF repeat 2Sequence analysisAdd BLAST26
Repeati1101 – 1126HCF repeat 3Sequence analysisAdd BLAST26
Repeati1157 – 1182HCF repeat 4; degenerateAdd BLAST26
Repeati1295 – 1320HCF repeat 5Sequence analysisAdd BLAST26
Repeati1323 – 1348HCF repeat 6Sequence analysisAdd BLAST26
Repeati1358 – 1383HCF repeat 7; degenerateAdd BLAST26
Repeati1423 – 1448HCF repeat 8Sequence analysisAdd BLAST26
Domaini1808 – 1898Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST91
Domaini1900 – 2016Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni500 – 550Required for interaction with OGTBy similarityAdd BLAST51
Regioni610 – 722Interaction with SIN3ABy similarityAdd BLAST113
Regioni750 – 902Interaction with ZBTB17By similarityAdd BLAST153
Regioni813 – 912Interaction with GABP2By similarityAdd BLAST100

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi574 – 1500Thr-richSequence analysisAdd BLAST927
Compositional biasi1622 – 1674Ala-richSequence analysisAdd BLAST53
Compositional biasi1684 – 1720Gln-richSequence analysisAdd BLAST37

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

eggNOGiENOG410KDN3. Eukaryota.
ENOG410Y5WM. LUCA.
GeneTreeiENSGT00760000119086.
HOGENOMiHOG000293192.
HOVERGENiHBG051888.
InParanoidiQ61191.
KOiK14966.
TreeFamiTF314757.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.120.10.80. 2 hits.
2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
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 differs from that shown. Reason: Frameshift at position 339.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti483V → R in AAB01163 (PubMed:9334261).Curated1
Sequence conflicti483V → R in AAD09225 (PubMed:9334261).Curated1
Sequence conflicti520P → S in CAF25305 (Ref. 6) Curated1
Sequence conflicti567 – 568VL → AW in AAB01163 (PubMed:9334261).Curated2
Sequence conflicti567 – 568VL → AW in AAD09225 (PubMed:9334261).Curated2
Sequence conflicti711Q → H in AAD09225 (PubMed:9334261).Curated1
Sequence conflicti1104C → S in AAB01163 (PubMed:9334261).Curated1
Sequence conflicti1104C → S in AAD09225 (PubMed:9334261).Curated1
Sequence conflicti1230G → A in AAB01163 (PubMed:9334261).Curated1
Sequence conflicti1230G → A in AAD09225 (PubMed:9334261).Curated1

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.2. 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.
CCDSiCCDS30218.1.
RefSeqiNP_032250.2. NM_008224.4.
UniGeneiMm.491126.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2M26NMR-A1896-2020[»]
ProteinModelPortaliQ61191.
SMRiQ61191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200248. 10 interactors.
IntActiQ61191. 4 interactors.
MINTiMINT-4097262.
STRINGi10090.ENSMUSP00000033761.

PTM databases

iPTMnetiQ61191.
PhosphoSitePlusiQ61191.

Proteomic databases

EPDiQ61191.
MaxQBiQ61191.
PaxDbiQ61191.
PeptideAtlasiQ61191.
PRIDEiQ61191.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033761; ENSMUSP00000033761; ENSMUSG00000031386.
GeneIDi15161.
KEGGimmu:15161.
UCSCiuc009tnm.2. mouse.

Organism-specific databases

CTDi3054.
MGIiMGI:105942. Hcfc1.

Phylogenomic databases

eggNOGiENOG410KDN3. Eukaryota.
ENOG410Y5WM. LUCA.
GeneTreeiENSGT00760000119086.
HOGENOMiHOG000293192.
HOVERGENiHBG051888.
InParanoidiQ61191.
KOiK14966.
TreeFamiTF314757.

Enzyme and pathway databases

ReactomeiR-MMU-2151201. Transcriptional activation of mitochondrial biogenesis.
R-MMU-3214847. HATs acetylate histones.
R-MMU-5689603. UCH proteinases.

Miscellaneous databases

ChiTaRSiHcfc1. mouse.
PROiQ61191.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031386.
CleanExiMM_HCFC1.
ExpressionAtlasiQ61191. baseline and differential.
GenevisibleiQ61191. MM.

Family and domain databases

CDDicd00063. FN3. 2 hits.
Gene3Di2.120.10.80. 2 hits.
2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
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]
ProtoNetiSearch...

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 30, 2016
This is version 158 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

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.