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Q61191 (HCFC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length2045 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7

Subunit structure

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. Ref.1 Ref.9 UniProtKB P51610

Subcellular location

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. Ref.7

Tissue specificity

Expressed in liver, pituitary gland, skeletal muscle, kidney, eye and brain (at protein level). Also observed at low level in heart, spleen and lung. Ref.1 Ref.7

Domain

The HCF repeat is a highly specific proteolytic cleavage signal By similarity. UniProtKB P51610

The kelch repeats fold into a 6-bladed kelch beta-propeller called the beta-propeller domain which mediates interaction with HCFC1R1 By similarity.

Post-translational modification

Proteolytically cleaved at one or several PPCE--THET sites within the HCF repeats. Cleavage is promoted by O-glycosylation By similarity. UniProtKB P51610

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.

Sequence similarities

Contains 3 fibronectin type-III domains.

Contains 5 Kelch repeats.

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCytoplasm
Nucleus
   DomainKelch repeat
Repeat
   Molecular functionChromatin regulator
   PTMAcetylation
Autocatalytic cleavage
Glycoprotein
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

histone H4-K16 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4-K5 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4-K8 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18836447. Source: GOC

protein stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein complex assembly

Inferred from electronic annotation. Source: Ensembl

release from viral latency

Inferred from direct assay Ref.7. Source: UniProtKB

   Cellular_componentAda2/Gcn5/Ada3 transcription activator complex

Inferred from electronic annotation. Source: Ensembl

MLL1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

MLL5-L complex

Inferred from electronic annotation. Source: Ensembl

SAGA-type complex

Inferred from electronic annotation. Source: Ensembl

Set1C/COMPASS complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

histone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionRNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 18836447. Source: MGI

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone acetyltransferase activity (H4-K16 specific)

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase activity (H4-K5 specific)

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase activity (H4-K8 specific)

Inferred from electronic annotation. Source: Ensembl

transcription coactivator activity

Traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 14321431HCF N-terminal chain 6 By similarity
PRO_0000016635
Chain2 – 13321331HCF N-terminal chain 5 By similarity
PRO_0000016636
Chain2 – 13041303HCF N-terminal chain 4 By similarity
PRO_0000016637
Chain2 – 11101109HCF N-terminal chain 3 By similarity
PRO_0000016638
Chain2 – 10811080HCF N-terminal chain 2 By similarity
PRO_0000016639
Chain2 – 10191018HCF N-terminal chain 1 By similarity
PRO_0000016640
Chain1020 – 20451026HCF C-terminal chain 1 By similarity UniProtKB P51610
PRO_0000016641
Chain1082 – 2045964HCF C-terminal chain 2 By similarity UniProtKB P51610
PRO_0000016642
Chain1111 – 2045935HCF C-terminal chain 3 By similarity UniProtKB P51610
PRO_0000016643
Chain1305 – 2045741HCF C-terminal chain 4 By similarity UniProtKB P51610
PRO_0000016644
Chain1333 – 2045713HCF C-terminal chain 5 By similarity UniProtKB P51610
PRO_0000016645
Chain1433 – 2045613HCF C-terminal chain 6 By similarity UniProtKB P51610
PRO_0000016646

Regions

Repeat44 – 8946Kelch 1
Repeat93 – 14048Kelch 2
Repeat148 – 19447Kelch 3
Repeat217 – 26549Kelch 4
Repeat266 – 31348Kelch 5
Domain366 – 45792Fibronectin type-III 1
Repeat1010 – 103526HCF repeat 1
Repeat1072 – 109726HCF repeat 2
Repeat1101 – 112626HCF repeat 3
Repeat1157 – 118226HCF repeat 4; degenerate
Repeat1295 – 132026HCF repeat 5
Repeat1323 – 134826HCF repeat 6
Repeat1358 – 138326HCF repeat 7; degenerate
Repeat1423 – 144826HCF repeat 8
Domain1808 – 189891Fibronectin type-III 2
Domain1900 – 2016117Fibronectin type-III 3
Region500 – 55051Required for interaction with OGT By similarity
Region610 – 722113Interaction with SIN3A By similarity
Region750 – 902153Interaction with ZBTB17 By similarity
Region813 – 912100Interaction with GABP2 By similarity
Compositional bias574 – 1500927Thr-rich
Compositional bias1622 – 167453Ala-rich
Compositional bias1684 – 172037Gln-rich

Sites

Site1019 – 10202Cleavage; by autolysis By similarity UniProtKB P51610
Site1081 – 10822Cleavage; by autolysis By similarity UniProtKB P51610
Site1110 – 11112Cleavage; by autolysis By similarity UniProtKB P51610
Site1304 – 13052Cleavage; by autolysis By similarity UniProtKB P51610
Site1332 – 13332Cleavage; by autolysis By similarity UniProtKB P51610
Site1432 – 14332Cleavage; by autolysis By similarity UniProtKB P51610

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue61Phosphoserine By similarity
Modified residue2881N6-acetyllysine Ref.12
Modified residue4111Phosphoserine By similarity
Modified residue6661Phosphoserine By similarity
Modified residue6691Phosphoserine By similarity
Modified residue8131N6-acetyllysine By similarity
Modified residue12041Phosphoserine By similarity
Modified residue15001Phosphothreonine By similarity
Modified residue15161Phosphoserine By similarity
Modified residue20151N6-acetyllysine By similarity
Cross-link105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link244Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link363Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1817Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1818Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict4831V → R in AAB01163. Ref.1
Sequence conflict4831V → R in AAD09225. Ref.1
Sequence conflict5201P → S in CAF25305. Ref.6
Sequence conflict567 – 5682VL → AW in AAB01163. Ref.1
Sequence conflict567 – 5682VL → AW in AAD09225. Ref.1
Sequence conflict7111Q → H in AAD09225. Ref.1
Sequence conflict11041C → S in AAB01163. Ref.1
Sequence conflict11041C → S in AAD09225. Ref.1
Sequence conflict12301G → A in AAB01163. Ref.1
Sequence conflict12301G → A in AAD09225. Ref.1

Secondary structure

................... 2045
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q61191 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: AD0EC38C9DB19F22

FASTA2,045210,437
        10         20         30         40         50         60 
MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG GNEGIVDELH 

        70         80         90        100        110        120 
VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM VEYGKYSNDL YELQASRWEW 

       130        140        150        160        170        180 
KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY LFGGLANDSE DPKNNIPRYL NDLYILELRP 

       190        200        210        220        230        240 
GSGVVAWDIP ITYGVLPPPR ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIETL 

       250        260        270        280        290        300 
TWNKPSLSGV APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN 

       310        320        330        340        350        360 
LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ VCCKDLWYLE 

       370        380        390        400        410        420 
TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY DIPATAATAT SPTPNPVPSV 

       430        440        450        460        470        480 
PANPPKSPAP AAAAPAVQPL TQVGITLVPQ AATAPPSTTT IQVLPTVPGS SISVPTAART 

       490        500        510        520        530        540 
QGVPAVLKVT GPQATTGTPL VTMRPASQAG KAPVTVTSLP ASVRMVVPTQ SAQGTVIGSN 

       550        560        570        580        590        600 
PQMSGMAALA AAAAATQKIP PSSAPTVLSV PAGTTIVKTV AVTPGTTTLP ATVKVASSPV 

       610        620        630        640        650        660 
MVSNPATRML KTAAAQVGTS VSSAANTSTR PIITVHKSGT VTVAQQAQVV TTVVGGVTKT 

       670        680        690        700        710        720 
ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ ASTGPVTQII QTKGPLPAGT 

       730        740        750        760        770        780 
ILKLVTSADG KPTTIITTTQ ASGAGTKPTI LGISSVSPST TKPGTTTIIK TIPMSAIITQ 

       790        800        810        820        830        840 
AGATGVTSSP GIKSPITIIT TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG 

       850        860        870        880        890        900 
QPGTILRTVP MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGAH 

       910        920        930        940        950        960 
STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT MQPVSQPTQV 

       970        980        990       1000       1010       1020 
TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG QGDVQPGTVT LVCSNPPCET 

      1030       1040       1050       1060       1070       1080 
HETGTTNTAT TTVVANLGGH PQPTQVQFVC DRQETAASLV TSAVGQQNGN VVRVCSNPPC 

      1090       1100       1110       1120       1130       1140 
ETHETGTTNT ATTATSNMAG QHGCSNPPCE THETGTTSTA TTAMSSMGTG QQRDTRRTTN 

      1150       1160       1170       1180       1190       1200 
TPTVVRITVA PGALERVQGT VKPQCQTQQT NMTTTTMTVQ ATGAPCSAGP LLRPSVALES 

      1210       1220       1230       1240       1250       1260 
GSHSPAFVQL ALPSVRVGLS GPSSKDMPTG RQPETYHTYT TNTPTTTRSI MVAGELGAAR 

      1270       1280       1290       1300       1310       1320 
VVPTSTYESL QASSPSSTMT MTALEALLCP SATVTQVCSN PPCETHETGT TNTATTSNAG 

      1330       1340       1350       1360       1370       1380 
SAQRVCSNPP CETHETGTTH TATTATSNGG AGQPEGGQQP ASGHPCETHQ TTSTGTTMSV 

      1390       1400       1410       1420       1430       1440 
SVGTLIPDAT SSHGTLESGL EVVAVPTVTS QAGSTLLASF PTQRVCSNPP CETHETGTTH 

      1450       1460       1470       1480       1490       1500 
TATTVTSNMS SNQDPPPAAS DQGEVASTQG DSTNITSASA ITTSVSSTLP RAVTTVTQST 

      1510       1520       1530       1540       1550       1560 
PVPGPSVPPP EELQVSPGPR QQLPPRQLLQ SASTPLMGES TEVLSASQTP ELQAAVDLSS 

      1570       1580       1590       1600       1610       1620 
TGDPSSGQEP TTSAVVATVV VQPPPPTQSE VDQLSLPQEL MAEAQAGTTT LMVTGLTPEE 

      1630       1640       1650       1660       1670       1680 
LAVTAAAEAA AQAAATEEAQ ALAIQAVLQA AQQAVMGTGE PMDTSEAAAA VTQAELGHLS 

      1690       1700       1710       1720       1730       1740 
AEGQEGQATT IPIVLTQQEL AALVQQQQQL QEAQAQAQQQ HHLPTEALAP ADSLNDPSIE 

      1750       1760       1770       1780       1790       1800 
SNCLNELASA VPSTVALLPS TATESLAPSN TFVAPQPVVA SPAKMQAAAT LTEVANGIES 

      1810       1820       1830       1840       1850       1860 
LGVKPDLPPP PSKAPVKKEN QWFDVGVIKG TSVMVTHYFL PPDDAVQSDD DSGTVPDYNQ 

      1870       1880       1890       1900       1910       1920 
LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS KSPDGAHLTW 

      1930       1940       1950       1960       1970       1980 
EPPSVTSGKI IEYSVYLAIQ SSQASGEPKS STPAQLAFMR VYCGPSPSCL VQSSSLSNAH 

      1990       2000       2010       2020       2030       2040 
IDYTTKPAII FRIAARNEKG YGPATQVRWL QETSKDSSGT KPASKRPMSS PEMKSAPKKS 


KADGQ 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Erratum
Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F., Songyang Z., Thomson J.A., Zwaka T.P.
Cell 134:692-692(2008)
[11]"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.
[12]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_032250.2. NM_008224.3.
UniGeneMm.439140.
Mm.491126.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M26NMR-A1896-2020[»]
ProteinModelPortalQ61191.
SMRQ61191. Positions 360-400, 1821-2020.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200248. 8 interactions.
IntActQ61191. 4 interactions.
MINTMINT-4097262.
STRING10090.ENSMUSP00000110012.

PTM databases

PhosphoSiteQ61191.

Proteomic databases

PaxDbQ61191.
PRIDEQ61191.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033761; ENSMUSP00000033761; ENSMUSG00000031386.
GeneID15161.
KEGGmmu:15161.
UCSCuc009tnm.1. mouse.

Organism-specific databases

CTD3054.
MGIMGI:105942. Hcfc1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00720000108539.
HOGENOMHOG000293192.
HOVERGENHBG051888.
KOK14966.
OrthoDBEOG790G05.
TreeFamTF314757.

Gene expression databases

ArrayExpressQ61191.
BgeeQ61191.
CleanExMM_HCFC1.
GenevestigatorQ61191.

Family and domain databases

Gene3D2.120.10.80. 2 hits.
2.60.40.10. 2 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
[Graphical view]
PfamPF01344. Kelch_1. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
PROSITEPS50853. FN3. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHCFC1. mouse.
NextBio287652.
PROQ61191.
SOURCESearch...

Entry information

Entry nameHCFC1_MOUSE
AccessionPrimary (citable) accession number: Q61191
Secondary accession number(s): B1AUX1 expand/collapse secondary AC list , Q684R1, Q7TSB0, Q8C2D0, Q9QWH2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot