URFB1_HUMAN
ID URFB1_HUMAN Reviewed; 1440 AA.
AC Q6BDS2; Q9NXE0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=UHRF1-binding protein 1;
DE AltName: Full=ICBP90-binding protein 1;
DE AltName: Full=Ubiquitin-like containing PHD and RING finger domains 1-binding protein 1;
GN Name=UHRF1BP1; Synonyms=C6orf107;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP INTERACTION WITH UHRF1, SUBUNIT, AND FUNCTION.
RX PubMed=15361834; DOI=10.1038/sj.onc.1208053;
RA Unoki M., Nishidate T., Nakamura Y.;
RT "ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through
RT its SRA domain.";
RL Oncogene 23:7601-7610(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-678.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-446; SER-755;
RP SER-758; SER-988; SER-1103 AND SER-1106, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May act as a negative regulator of cell growth.
CC {ECO:0000269|PubMed:15361834}.
CC -!- SUBUNIT: Homodimer (Potential). Interacts with UHRF1.
CC {ECO:0000269|PubMed:15361834, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91074.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; AB126777; BAD32740.1; -; mRNA.
DR EMBL; AL139100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL033520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK000309; BAA91074.1; ALT_SEQ; mRNA.
DR CCDS; CCDS43455.1; -.
DR RefSeq; NP_060224.3; NM_017754.3.
DR AlphaFoldDB; Q6BDS2; -.
DR SMR; Q6BDS2; -.
DR BioGRID; 120235; 72.
DR IntAct; Q6BDS2; 34.
DR MINT; Q6BDS2; -.
DR STRING; 9606.ENSP00000192788; -.
DR GlyGen; Q6BDS2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6BDS2; -.
DR PhosphoSitePlus; Q6BDS2; -.
DR BioMuta; UHRF1BP1; -.
DR DMDM; 67462038; -.
DR EPD; Q6BDS2; -.
DR jPOST; Q6BDS2; -.
DR MassIVE; Q6BDS2; -.
DR MaxQB; Q6BDS2; -.
DR PaxDb; Q6BDS2; -.
DR PeptideAtlas; Q6BDS2; -.
DR PRIDE; Q6BDS2; -.
DR ProteomicsDB; 66219; -.
DR Antibodypedia; 49429; 68 antibodies from 22 providers.
DR DNASU; 54887; -.
DR Ensembl; ENST00000192788.6; ENSP00000192788.5; ENSG00000065060.18.
DR GeneID; 54887; -.
DR KEGG; hsa:54887; -.
DR MANE-Select; ENST00000192788.6; ENSP00000192788.5; NM_017754.4; NP_060224.3.
DR UCSC; uc003oju.5; human.
DR CTD; 54887; -.
DR DisGeNET; 54887; -.
DR GeneCards; UHRF1BP1; -.
DR HGNC; HGNC:21216; UHRF1BP1.
DR HPA; ENSG00000065060; Low tissue specificity.
DR MIM; 619570; gene.
DR neXtProt; NX_Q6BDS2; -.
DR OpenTargets; ENSG00000065060; -.
DR PharmGKB; PA162408530; -.
DR VEuPathDB; HostDB:ENSG00000065060; -.
DR eggNOG; KOG2955; Eukaryota.
DR GeneTree; ENSGT00600000084428; -.
DR InParanoid; Q6BDS2; -.
DR OMA; WDEFQTK; -.
DR OrthoDB; 64302at2759; -.
DR PhylomeDB; Q6BDS2; -.
DR TreeFam; TF314874; -.
DR PathwayCommons; Q6BDS2; -.
DR SignaLink; Q6BDS2; -.
DR BioGRID-ORCS; 54887; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; UHRF1BP1; human.
DR GenomeRNAi; 54887; -.
DR Pharos; Q6BDS2; Tbio.
DR PRO; PR:Q6BDS2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6BDS2; protein.
DR Bgee; ENSG00000065060; Expressed in left ventricle myocardium and 190 other tissues.
DR ExpressionAtlas; Q6BDS2; baseline and differential.
DR Genevisible; Q6BDS2; HS.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR InterPro; IPR026728; UHRF1BP1-like.
DR InterPro; IPR026854; VPS13-like_N.
DR PANTHER; PTHR22774; PTHR22774; 1.
DR Pfam; PF12624; Chorein_N; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..1440
FT /note="UHRF1-binding protein 1"
FT /id="PRO_0000065723"
FT DOMAIN 3..95
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT REGION 267..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 837..860
FT /evidence="ECO:0000255"
FT COILED 1401..1435
FT /evidence="ECO:0000255"
FT COMPBIAS 284..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 988
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT VARIANT 404
FT /note="K -> N (in dbSNP:rs16894945)"
FT /id="VAR_051474"
FT VARIANT 454
FT /note="Q -> R (in dbSNP:rs11755393)"
FT /id="VAR_051475"
FT VARIANT 854
FT /note="K -> E (in dbSNP:rs3734265)"
FT /id="VAR_051476"
FT VARIANT 984
FT /note="Q -> H (in dbSNP:rs9469913)"
FT /id="VAR_051477"
FT VARIANT 1098
FT /note="M -> T (in dbSNP:rs13205210)"
FT /id="VAR_051478"
SQ SEQUENCE 1440 AA; 159485 MW; F6A5585274C33FA9 CRC64;
MAGIIKKQIL KHLSRFTKNL SPDKINLSTL KGEGQLTNLE LDEEVLQNVL ELPTWLAITR
VYCNRASIRI QWTKLKTHPI CLCLDKVEVE MKTCEDPRPP NGQSPIALAS GQSEYGFAEK
VVEGMFIIVN SITIKIHSKA FHASFELWQL QGYSVNPNWQ QSDLRLTRIT DPCRGEVLTF
KEITWQTLRI EADATDNGDQ DPVTTPLRLI TNQGRIQIAL KRRTKDCNVI SSKLMFLLDD
LLWVLTDSQL KAMMKYAESL SEAMEKSAHQ RKSLAPEPVQ ITPPAPSAQQ SWAQAFGGSQ
GNSNSSSSRL SQYFEKFDVK ESSYHLLISR LDLHICDDSQ SREPGVSANR LMGGAMQLTF
RKMAFDYYPF HWAGDSCKHW VRHCEAMETR GQWAQKLVME FQSKMEKWHE ETGLKPPWHL
GVDSLFRRKA DSLSSPRKNP LERSPSQGRQ PAFQPPAWNR LRSSCMVVRV DDLDIHQVST
AGQPSKKPST LLSCSRKLHN LPTQVSAIHI EFTEYYFPDN QELPVPCPNL YIQLNGLTFT
MDPVSLLWGN LFCLDLYRSL EQFKAIYKLE DSSQKDEHLD IRLDAFWLKV SFPLEKRERA
ELHRPQALVF SASGMIATNT RHAPHCSCSD LQSLFRGFAA AEFFHSNYDH FPKVPGGFSL
LHMLFLHHAF QMDSCLPQPN TLPPQRPKAS WDLWSVHFTQ ISLDFEGTEN FKGHTLNFVA
PFPLSIWACL PLRWQQAQAR KLLLASEGRL KPSASFGSPV QSEALAPDSM SHPRSKTEHD
LKSLSGLTEV MEILKEGSSG MDNKGPLTEL EDVADVHMLV HSPAHVRVRL DHYQYLALLR
LKEVLQRLQE QLTKDTESMT GSPLQNQTAC IGVLFPSAEV ALLMHPAPGA VDADSAGSDS
TSLVDSELSP SEDRELKSDA SSDQGPASPE KVLEESSIEN QDVSQERPHS NGELQDSGPL
AQQLAGKGHE AVESLQAKKL SRTQASSSPA ALKPPAGRET AVNGQGELIP LKNIEGELSS
AIHMTKDATK EALHATMDLT KEAVSLTKDA FSLGRDRMTS TMHKMLSLPP AKEPMAKTDE
GVAAPVSGGA ARLRFFSMKR TVSQQSFDGV SLDSSGPEDR ISVDSDGSDS FVMLLESESG
PESVPPGSLS NVSDNAGVQG SPLVNNYGQG SPAANSSVSP SGEDLIFHPV SVLVLKVNEV
SFGIEVRGED LTVALQAEEL TLQQLGTVGL WQFLHGQCPG TCFQESSTLK TGHIRPAVGL
RFEVGPGAAV HSPLASQNGF LHLLLHGCDL ELLTSVLSGL GPFLEDEEIP VVVPMQIELL
NSSITLKDDI PPIYPTSPGP IPITLAMEHV VLKRSDDGVF HIGAAAQDKP SAEVLKSEKR
QPPKEQVFLV PTGEVFEQQV KELPILQKEL IETKQALANA NQDKEKLLQE IRKYNPFFEL
