SubmitCancel

Skip Header

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

Q96KR1

- ZFR_HUMAN

UniProt

Q96KR1 - ZFR_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Zinc finger RNA-binding protein

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

Functioni

Involved in postimplantation and gastrulation stages of development. Involved in the nucleocytoplasmic shuttling of STAU2. Binds to DNA and RNA By similarity.

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. poly(A) RNA binding Source: UniProtKB
  3. protein binding Source: IntAct
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. multicellular organismal development Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

DNA-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger RNA-binding protein
Short name:
hZFR
Alternative name(s):
M-phase phosphoprotein homolog
Gene namesi
Name:ZFR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:17277. ZFR.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity. Cytoplasmic granule By similarity. Chromosome By similarity
Note: Associated with chromosome foci in meiotic cells. Localizes in somatodendritic compartment of primary hippocampal neurons. Colocalizes with STAU2 in several cytosolic RNA granules By similarity.

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38219.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10741074Zinc finger RNA-binding proteinPRO_0000312719Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei509 – 5091N6-acetyllysine1 Publication
Modified residuei516 – 5161N6-acetyllysine By similarity
Modified residuei1054 – 10541Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ96KR1.
PaxDbiQ96KR1.
PRIDEiQ96KR1.

PTM databases

PhosphoSiteiQ96KR1.

Expressioni

Tissue specificityi

Expressed in lung, liver, lymphocytes, heart, pancreas, placenta, brain and kidney.1 Publication

Gene expression databases

ArrayExpressiQ96KR1.
BgeeiQ96KR1.
CleanExiHS_ZFR.
GenevestigatoriQ96KR1.

Organism-specific databases

HPAiHPA016666.

Interactioni

Subunit structurei

Found in a cytoplasmic RNP complex with STAU2. Interacts with STAU2. Does not interact with STAU1 By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
SMAD2Q157962EBI-2513582,EBI-1040141

Protein-protein interaction databases

BioGridi119667. 41 interactions.
DIPiDIP-47293N.
IntActiQ96KR1. 13 interactions.
MINTiMINT-4655113.

Structurei

3D structure databases

ProteinModelPortaliQ96KR1.
SMRiQ96KR1. Positions 722-1039.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini703 – 1073371DZFAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 302267Ala-richAdd
BLAST

Sequence similaritiesi

Contains 1 DZF domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG292385.
HOVERGENiHBG108765.
InParanoidiQ96KR1.
KOiK13203.
OMAiNNCTVNT.
OrthoDBiEOG72ZCDC.
PhylomeDBiQ96KR1.
TreeFamiTF320194.

Family and domain databases

InterProiIPR006561. DZF.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR003604. Znf_U1.
[Graphical view]
PfamiPF07528. DZF. 1 hit.
[Graphical view]
SMARTiSM00572. DZF. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
SM00451. ZnF_U1. 3 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96KR1-1 [UniParc]FASTAAdd to Basket

« Hide

MIPICPVVSF TYVPSRLGED AKMATGNYFG FTHSGAAAAA AAAQYSQQPA     50
SGVAYSHPTT VASYTVHQAP VAAHTVTAAY APAAATVAVA RPAPVAVAAA 100
ATAAAYGGYP TAHTATDYGY TQRQQEAPPP PPPATTQNYQ DSYSYVRSTA 150
PAVAYDSKQY YQQPTATAAA VAAAAQPQPS VAETYYQTAP KAGYSQGATQ 200
YTQAQQTRQV TAIKPATPSP ATTTFSIYPV SSTVQPVAAA ATVVPSYTQS 250
ATYSTTAVTY SGTSYSGYEA AVYSAASSYY QQQQQQQKQA AAAAAAAAAT 300
AAWTGTTFTK KAPFQNKQLK PKQPPKPPQI HYCDVCKISC AGPQTYKEHL 350
EGQKHKKKEA ALKASQNTSS SNSSTRGTQN QLRCELCDVS CTGADAYAAH 400
IRGAKHQKVV KLHTKLGKPI PSTEPNVVSQ ATSSTAVSAS KPTASPSSIA 450
ANNCTVNTSS VATSSMKGLT TTGNSSLNST SNTKVSAVPT NMAAKKTSTP 500
KINFVGGNKL QSTGNKAEDI KGTECVKSTP VTSAVQIPEV KQDTVSEPVT 550
PASLAALQSD VQPVGHDYVE EVRNDEGKVI RFHCKLCECS FNDPNAKEMH 600
LKGRRHRLQY KKKVNPDLQV EVKPSIRARK IQEEKMRKQM QKEEYWRRRE 650
EEERWRMEMR RYEEDMYWRR MEEEQHHWDD RRRMPDGGYP HGPPGPLGLL 700
GVRPGMPPQP QGPAPLRRPD SSDDRYVMTK HATIYPTEEE LQAVQKIVSI 750
TERALKLVSD SLSEHEKNKN KEGDDKKEGG KDRALKGVLR VGVLAKGLLL 800
RGDRNVNLVL LCSEKPSKTL LSRIAENLPK QLAVISPEKY DIKCAVSEAA 850
IILNSCVEPK MQVTITLTSP IIREENMREG DVTSGMVKDP PDVLDRQKCL 900
DALAALRHAK WFQARANGLQ SCVIIIRILR DLCQRVPTWS DFPSWAMELL 950
VEKAISSASS PQSPGDALRR VFECISSGII LKGSPGLLDP CEKDPFDTLA 1000
TMTDQQREDI TSSAQFALRL LAFRQIHKVL GMDPLPQMSQ RFNIHNNRKR 1050
RRDSDGVDGF EAEGKKDKKD YDNF 1074
Length:1,074
Mass (Da):117,012
Last modified:December 4, 2007 - v2
Checksum:i3E43654E7134E9FC
GO

Sequence cautioni

The sequence AAH30540.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAI07418.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence CAC40818.1 differs from that shown. Reason: Frameshift at position 1057.
The sequence AAD40385.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAB15147.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAC40818.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti461 – 4611V → I.1 Publication
Corresponds to variant rs4867440 [ dbSNP | Ensembl ].
VAR_037554
Natural varianti520 – 5201I → T.1 Publication
Corresponds to variant rs1051489 [ dbSNP | Ensembl ].
VAR_037555

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71V → I in AAI07418. 1 Publication
Sequence conflicti643 – 6431E → L in AAD40385. 1 Publication
Sequence conflicti659 – 6591M → I in CAC40818. 1 Publication
Sequence conflicti794 – 7941L → F in AAD40385. 1 Publication
Sequence conflicti834 – 8341V → F in AAD40385. 1 Publication
Sequence conflicti913 – 9131Q → QE in CAC40818. 1 Publication
Sequence conflicti1016 – 10161F → K in CAC40818. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ314790 mRNA. Translation: CAC40818.1. Sequence problems.
AC008949 Genomic DNA. No translation available.
BC030540 mRNA. Translation: AAH30540.1. Sequence problems.
BC051893 mRNA. Translation: AAH51893.1.
BC062986 mRNA. Translation: AAH62986.1.
BC107417 mRNA. Translation: AAI07418.1. Sequence problems.
BC137084 mRNA. Translation: AAI37085.1.
AF100742 mRNA. Translation: AAD40385.1. Different initiation.
AK025481 mRNA. Translation: BAB15147.1. Different initiation.
AL137258 mRNA. Translation: CAB70659.1.
CCDSiCCDS34139.1.
PIRiT46329.
RefSeqiNP_057191.2. NM_016107.3.
UniGeneiHs.435231.

Genome annotation databases

EnsembliENST00000265069; ENSP00000265069; ENSG00000056097.
GeneIDi51663.
KEGGihsa:51663.
UCSCiuc003jhr.1. human.

Polymorphism databases

DMDMi162416228.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ314790 mRNA. Translation: CAC40818.1 . Sequence problems.
AC008949 Genomic DNA. No translation available.
BC030540 mRNA. Translation: AAH30540.1 . Sequence problems.
BC051893 mRNA. Translation: AAH51893.1 .
BC062986 mRNA. Translation: AAH62986.1 .
BC107417 mRNA. Translation: AAI07418.1 . Sequence problems.
BC137084 mRNA. Translation: AAI37085.1 .
AF100742 mRNA. Translation: AAD40385.1 . Different initiation.
AK025481 mRNA. Translation: BAB15147.1 . Different initiation.
AL137258 mRNA. Translation: CAB70659.1 .
CCDSi CCDS34139.1.
PIRi T46329.
RefSeqi NP_057191.2. NM_016107.3.
UniGenei Hs.435231.

3D structure databases

ProteinModelPortali Q96KR1.
SMRi Q96KR1. Positions 722-1039.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119667. 41 interactions.
DIPi DIP-47293N.
IntActi Q96KR1. 13 interactions.
MINTi MINT-4655113.

PTM databases

PhosphoSitei Q96KR1.

Polymorphism databases

DMDMi 162416228.

Proteomic databases

MaxQBi Q96KR1.
PaxDbi Q96KR1.
PRIDEi Q96KR1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265069 ; ENSP00000265069 ; ENSG00000056097 .
GeneIDi 51663.
KEGGi hsa:51663.
UCSCi uc003jhr.1. human.

Organism-specific databases

CTDi 51663.
GeneCardsi GC05M032354.
H-InvDB HIX0004787.
HGNCi HGNC:17277. ZFR.
HPAi HPA016666.
MIMi 615635. gene.
neXtProti NX_Q96KR1.
PharmGKBi PA38219.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292385.
HOVERGENi HBG108765.
InParanoidi Q96KR1.
KOi K13203.
OMAi NNCTVNT.
OrthoDBi EOG72ZCDC.
PhylomeDBi Q96KR1.
TreeFami TF320194.

Miscellaneous databases

ChiTaRSi ZFR. human.
GenomeRNAii 51663.
NextBioi 55646.
PROi Q96KR1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96KR1.
Bgeei Q96KR1.
CleanExi HS_ZFR.
Genevestigatori Q96KR1.

Family and domain databases

InterProi IPR006561. DZF.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR003604. Znf_U1.
[Graphical view ]
Pfami PF07528. DZF. 1 hit.
[Graphical view ]
SMARTi SM00572. DZF. 1 hit.
SM00355. ZnF_C2H2. 3 hits.
SM00451. ZnF_U1. 3 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the human single copy homologue of the mouse zinc finger protein zfr."
    Kleines M., Gaertner A., Ritter K., Schaade L.
    Gene 275:157-162(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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], VARIANTS ILE-461 AND THR-520.
    Tissue: Bone marrow, Duodenum, Eye, Lung and Uterus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 643-1074.
    Tissue: Pituitary.
  5. "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 744-1074.
    Tissue: Hepatoma.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 970-1074.
    Tissue: Testis.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "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-1054, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-509, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZFR_HUMAN
AccessioniPrimary (citable) accession number: Q96KR1
Secondary accession number(s): B2RNR5
, Q05C08, Q3B7X5, Q6P5A3, Q86UA0, Q9H6V4, Q9NTI1, Q9Y687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: September 3, 2014
This is version 101 of the entry and version 2 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 5
    Human chromosome 5: 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
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi