Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

UHRF1-binding protein 1

Gene

UHRF1BP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May act as a negative regulator of cell growth.1 Publication

GO - Molecular functioni

  • histone deacetylase binding Source: BHF-UCL
  • identical protein binding Source: BHF-UCL
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
UHRF1-binding protein 1
Alternative name(s):
ICBP90-binding protein 1
Ubiquitin-like containing PHD and RING finger domains 1-binding protein 1
Gene namesi
Name:UHRF1BP1
Synonyms:C6orf107
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21216. UHRF1BP1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162408530.

Polymorphism and mutation databases

BioMutaiUHRF1BP1.
DMDMi67462038.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14401440UHRF1-binding protein 1PRO_0000065723Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1106 – 11061PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6BDS2.
MaxQBiQ6BDS2.
PaxDbiQ6BDS2.
PeptideAtlasiQ6BDS2.
PRIDEiQ6BDS2.

PTM databases

iPTMnetiQ6BDS2.
PhosphoSiteiQ6BDS2.

Expressioni

Gene expression databases

BgeeiQ6BDS2.
CleanExiHS_UHRF1BP1.
ExpressionAtlasiQ6BDS2. baseline and differential.
GenevisibleiQ6BDS2. HS.

Organism-specific databases

HPAiHPA032099.
HPA032100.

Interactioni

Subunit structurei

Homodimer (Potential). Interacts with UHRF1.Curated1 Publication

GO - Molecular functioni

  • histone deacetylase binding Source: BHF-UCL
  • identical protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi120235. 26 interactions.
IntActiQ6BDS2. 17 interactions.
STRINGi9606.ENSP00000192788.

Structurei

3D structure databases

ProteinModelPortaliQ6BDS2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili837 – 86024Sequence analysisAdd
BLAST
Coiled coili1401 – 143535Sequence analysisAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2955. Eukaryota.
ENOG410XQGP. LUCA.
GeneTreeiENSGT00600000084428.
HOGENOMiHOG000154771.
HOVERGENiHBG061128.
InParanoidiQ6BDS2.
OMAiNGDQDPV.
OrthoDBiEOG7J445Z.
PhylomeDBiQ6BDS2.
TreeFamiTF314874.

Family and domain databases

InterProiIPR026728. UHRF1BP1-like.
IPR026854. VPS13_N.
[Graphical view]
PANTHERiPTHR22774. PTHR22774. 1 hit.
PfamiPF12624. Chorein_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6BDS2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGIIKKQIL KHLSRFTKNL SPDKINLSTL KGEGQLTNLE LDEEVLQNVL
60 70 80 90 100
ELPTWLAITR VYCNRASIRI QWTKLKTHPI CLCLDKVEVE MKTCEDPRPP
110 120 130 140 150
NGQSPIALAS GQSEYGFAEK VVEGMFIIVN SITIKIHSKA FHASFELWQL
160 170 180 190 200
QGYSVNPNWQ QSDLRLTRIT DPCRGEVLTF KEITWQTLRI EADATDNGDQ
210 220 230 240 250
DPVTTPLRLI TNQGRIQIAL KRRTKDCNVI SSKLMFLLDD LLWVLTDSQL
260 270 280 290 300
KAMMKYAESL SEAMEKSAHQ RKSLAPEPVQ ITPPAPSAQQ SWAQAFGGSQ
310 320 330 340 350
GNSNSSSSRL SQYFEKFDVK ESSYHLLISR LDLHICDDSQ SREPGVSANR
360 370 380 390 400
LMGGAMQLTF RKMAFDYYPF HWAGDSCKHW VRHCEAMETR GQWAQKLVME
410 420 430 440 450
FQSKMEKWHE ETGLKPPWHL GVDSLFRRKA DSLSSPRKNP LERSPSQGRQ
460 470 480 490 500
PAFQPPAWNR LRSSCMVVRV DDLDIHQVST AGQPSKKPST LLSCSRKLHN
510 520 530 540 550
LPTQVSAIHI EFTEYYFPDN QELPVPCPNL YIQLNGLTFT MDPVSLLWGN
560 570 580 590 600
LFCLDLYRSL EQFKAIYKLE DSSQKDEHLD IRLDAFWLKV SFPLEKRERA
610 620 630 640 650
ELHRPQALVF SASGMIATNT RHAPHCSCSD LQSLFRGFAA AEFFHSNYDH
660 670 680 690 700
FPKVPGGFSL LHMLFLHHAF QMDSCLPQPN TLPPQRPKAS WDLWSVHFTQ
710 720 730 740 750
ISLDFEGTEN FKGHTLNFVA PFPLSIWACL PLRWQQAQAR KLLLASEGRL
760 770 780 790 800
KPSASFGSPV QSEALAPDSM SHPRSKTEHD LKSLSGLTEV MEILKEGSSG
810 820 830 840 850
MDNKGPLTEL EDVADVHMLV HSPAHVRVRL DHYQYLALLR LKEVLQRLQE
860 870 880 890 900
QLTKDTESMT GSPLQNQTAC IGVLFPSAEV ALLMHPAPGA VDADSAGSDS
910 920 930 940 950
TSLVDSELSP SEDRELKSDA SSDQGPASPE KVLEESSIEN QDVSQERPHS
960 970 980 990 1000
NGELQDSGPL AQQLAGKGHE AVESLQAKKL SRTQASSSPA ALKPPAGRET
1010 1020 1030 1040 1050
AVNGQGELIP LKNIEGELSS AIHMTKDATK EALHATMDLT KEAVSLTKDA
1060 1070 1080 1090 1100
FSLGRDRMTS TMHKMLSLPP AKEPMAKTDE GVAAPVSGGA ARLRFFSMKR
1110 1120 1130 1140 1150
TVSQQSFDGV SLDSSGPEDR ISVDSDGSDS FVMLLESESG PESVPPGSLS
1160 1170 1180 1190 1200
NVSDNAGVQG SPLVNNYGQG SPAANSSVSP SGEDLIFHPV SVLVLKVNEV
1210 1220 1230 1240 1250
SFGIEVRGED LTVALQAEEL TLQQLGTVGL WQFLHGQCPG TCFQESSTLK
1260 1270 1280 1290 1300
TGHIRPAVGL RFEVGPGAAV HSPLASQNGF LHLLLHGCDL ELLTSVLSGL
1310 1320 1330 1340 1350
GPFLEDEEIP VVVPMQIELL NSSITLKDDI PPIYPTSPGP IPITLAMEHV
1360 1370 1380 1390 1400
VLKRSDDGVF HIGAAAQDKP SAEVLKSEKR QPPKEQVFLV PTGEVFEQQV
1410 1420 1430 1440
KELPILQKEL IETKQALANA NQDKEKLLQE IRKYNPFFEL
Length:1,440
Mass (Da):159,485
Last modified:September 13, 2004 - v1
Checksum:iF6A5585274C33FA9
GO

Sequence cautioni

The sequence BAA91074.1 differs from that shown.Chimeric cDNA.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti404 – 4041K → N.
Corresponds to variant rs16894945 [ dbSNP | Ensembl ].
VAR_051474
Natural varianti454 – 4541Q → R.
Corresponds to variant rs11755393 [ dbSNP | Ensembl ].
VAR_051475
Natural varianti854 – 8541K → E.
Corresponds to variant rs3734265 [ dbSNP | Ensembl ].
VAR_051476
Natural varianti984 – 9841Q → H.
Corresponds to variant rs9469913 [ dbSNP | Ensembl ].
VAR_051477
Natural varianti1098 – 10981M → T.
Corresponds to variant rs13205210 [ dbSNP | Ensembl ].
VAR_051478

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB126777 mRNA. Translation: BAD32740.1.
AL139100, AL033520 Genomic DNA. Translation: CAI20353.1.
AL033520, AL139100 Genomic DNA. Translation: CAI20282.1.
AK000309 mRNA. Translation: BAA91074.1. Sequence problems.
CCDSiCCDS43455.1.
RefSeqiNP_060224.3. NM_017754.3.
UniGeneiHs.700656.

Genome annotation databases

EnsembliENST00000192788; ENSP00000192788; ENSG00000065060.
GeneIDi54887.
KEGGihsa:54887.
UCSCiuc003oju.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB126777 mRNA. Translation: BAD32740.1.
AL139100, AL033520 Genomic DNA. Translation: CAI20353.1.
AL033520, AL139100 Genomic DNA. Translation: CAI20282.1.
AK000309 mRNA. Translation: BAA91074.1. Sequence problems.
CCDSiCCDS43455.1.
RefSeqiNP_060224.3. NM_017754.3.
UniGeneiHs.700656.

3D structure databases

ProteinModelPortaliQ6BDS2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120235. 26 interactions.
IntActiQ6BDS2. 17 interactions.
STRINGi9606.ENSP00000192788.

PTM databases

iPTMnetiQ6BDS2.
PhosphoSiteiQ6BDS2.

Polymorphism and mutation databases

BioMutaiUHRF1BP1.
DMDMi67462038.

Proteomic databases

EPDiQ6BDS2.
MaxQBiQ6BDS2.
PaxDbiQ6BDS2.
PeptideAtlasiQ6BDS2.
PRIDEiQ6BDS2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000192788; ENSP00000192788; ENSG00000065060.
GeneIDi54887.
KEGGihsa:54887.
UCSCiuc003oju.5. human.

Organism-specific databases

CTDi54887.
GeneCardsiUHRF1BP1.
HGNCiHGNC:21216. UHRF1BP1.
HPAiHPA032099.
HPA032100.
neXtProtiNX_Q6BDS2.
PharmGKBiPA162408530.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2955. Eukaryota.
ENOG410XQGP. LUCA.
GeneTreeiENSGT00600000084428.
HOGENOMiHOG000154771.
HOVERGENiHBG061128.
InParanoidiQ6BDS2.
OMAiNGDQDPV.
OrthoDBiEOG7J445Z.
PhylomeDBiQ6BDS2.
TreeFamiTF314874.

Miscellaneous databases

ChiTaRSiUHRF1BP1. human.
GenomeRNAii54887.
PROiQ6BDS2.

Gene expression databases

BgeeiQ6BDS2.
CleanExiHS_UHRF1BP1.
ExpressionAtlasiQ6BDS2. baseline and differential.
GenevisibleiQ6BDS2. HS.

Family and domain databases

InterProiIPR026728. UHRF1BP1-like.
IPR026854. VPS13_N.
[Graphical view]
PANTHERiPTHR22774. PTHR22774. 1 hit.
PfamiPF12624. Chorein_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain."
    Unoki M., Nishidate T., Nakamura Y.
    Oncogene 23:7601-7610(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH UHRF1, SUBUNIT, FUNCTION.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-678.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiURFB1_HUMAN
AccessioniPrimary (citable) accession number: Q6BDS2
Secondary accession number(s): Q9NXE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: September 13, 2004
Last modified: June 8, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations

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.