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Protein
Submitted name:

Zinc finger protein ubi-d4

Gene

DPF2

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Submitted name:
Zinc finger protein ubi-d4Imported
Gene namesi
Name:DPF2Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9964. DPF2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

EPDiJ3KMZ8.
MaxQBiJ3KMZ8.
PaxDbiJ3KMZ8.
PRIDEiJ3KMZ8.

Expressioni

Gene expression databases

ExpressionAtlasiJ3KMZ8. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000436901.

Structurei

3D structure databases

ProteinModelPortaliJ3KMZ8.
SMRiJ3KMZ8. Positions 203-248, 285-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini284 – 34461PHD-typeInterPro annotationAdd
BLAST
Domaini341 – 39151PHD-typeInterPro annotationAdd
BLAST

Keywords - Domaini

Zinc-fingerSAAS annotation

Phylogenomic databases

eggNOGiKOG1244. Eukaryota.
ENOG410YDAG. LUCA.
GeneTreeiENSGT00530000063194.
OMAiPINDETS.
PhylomeDBiJ3KMZ8.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR025750. Requiem/DPF_N_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
PF14051. Requiem_N. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

J3KMZ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVVENVVK LLGEQYYKDA MEQCHNYNAR LCAERSVRLP FLDSQTGVAQ
60 70 80 90 100
SNCYIWMEKR HRGPGLASGQ LYSYPARRWR KKRRAHPPED PRLSFPSIKP
110 120 130 140 150
DTDQTLKKEG LISQDGSSLE ALLRTDPLEK RGAPDPRVDD DSLGEFPVTN
160 170 180 190 200
SRARKRILEP DDFLDDLDDE DYEEDTPKRR GKGKSKGKGV GSARKKLDAS
210 220 230 240 250
ILEDRDKPYA CDNSFKQKHT SKAPQRVCGK RYKNRPGLSY HYAHSHLAEE
260 270 280 290 300
EGEDKEDSQP PTPVSQRSEE QKSKKGPDGL ALPNNYCDFC LGDSKINKKT
310 320 330 340 350
GQPEELVSCS DCGRSGHPSC LQFTPVMMAA VKTYRWQCIE CKCCNICGTS
360 370 380 390 400
ENDDQLLFCD DCDRGYHMYC LTPSMSEPPE GSWSCHLCLD LLKEKASIYQ

NQNSS
Length:405
Mass (Da):45,780
Last modified:October 3, 2012 - v1
Checksum:iEF4C5A781BAD84B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP000944 Genomic DNA. No translation available.
RefSeqiXP_005274206.1. XM_005274149.1.
UniGeneiHs.13495.

Genome annotation databases

EnsembliENST00000252268; ENSP00000252268; ENSG00000133884.
GeneIDi5977.
UCSCiuc058din.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP000944 Genomic DNA. No translation available.
RefSeqiXP_005274206.1. XM_005274149.1.
UniGeneiHs.13495.

3D structure databases

ProteinModelPortaliJ3KMZ8.
SMRiJ3KMZ8. Positions 203-248, 285-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000436901.

Proteomic databases

EPDiJ3KMZ8.
MaxQBiJ3KMZ8.
PaxDbiJ3KMZ8.
PRIDEiJ3KMZ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252268; ENSP00000252268; ENSG00000133884.
GeneIDi5977.
UCSCiuc058din.1. human.

Organism-specific databases

CTDi5977.
HGNCiHGNC:9964. DPF2.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1244. Eukaryota.
ENOG410YDAG. LUCA.
GeneTreeiENSGT00530000063194.
OMAiPINDETS.
PhylomeDBiJ3KMZ8.

Miscellaneous databases

ChiTaRSiDPF2. human.
GenomeRNAii5977.

Gene expression databases

ExpressionAtlasiJ3KMZ8. baseline and differential.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR025750. Requiem/DPF_N_dom.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
PF14051. Requiem_N. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "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].
  4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Ensembl
    Submitted (AUG-2012) to UniProtKB
    Cited for: IDENTIFICATION.
  9. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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].
  11. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurethsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiJ3KMZ8_HUMAN
AccessioniPrimary (citable) accession number: J3KMZ8
Entry historyi
Integrated into UniProtKB/TrEMBL: October 3, 2012
Last sequence update: October 3, 2012
Last modified: June 8, 2016
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.