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Q92576

- PHF3_HUMAN

UniProt

Q92576 - PHF3_HUMAN

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Protein
PHD finger protein 3
Gene
PHF3, KIAA0244
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri717 – 77256PHD-type
Add
BLAST

GO - Molecular functioni

  1. zinc ion binding Source: InterPro

GO - Biological processi

  1. multicellular organismal development Source: UniProtKB
  2. transcription, DNA-templated Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
PHD finger protein 3
Gene namesi
Name:PHF3
Synonyms:KIAA0244
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:8921. PHF3.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33261.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20392039PHD finger protein 3
PRO_0000059292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei283 – 2831Phosphoserine1 Publication
Modified residuei299 – 2991Phosphoserine1 Publication
Modified residuei680 – 6801Phosphoserine1 Publication
Modified residuei1133 – 11331Phosphoserine2 Publications
Modified residuei1148 – 11481Phosphoserine1 Publication
Modified residuei1178 – 11781Phosphoserine2 Publications
Modified residuei1642 – 16421Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92576.
PaxDbiQ92576.
PeptideAtlasiQ92576.
PRIDEiQ92576.

PTM databases

PhosphoSiteiQ92576.

Expressioni

Tissue specificityi

Ubiquitous. Expression is significantly reduced or lost in glioblastomas, glioblastoma cell lines, anaplastic astrocytomas, and astrocytomas.1 Publication

Gene expression databases

ArrayExpressiQ92576.
BgeeiQ92576.
CleanExiHS_PHF3.
GenevestigatoriQ92576.

Organism-specific databases

HPAiHPA024676.
HPA025763.

Interactioni

Protein-protein interaction databases

BioGridi117031. 5 interactions.
IntActiQ92576. 3 interactions.
STRINGi9606.ENSP00000262043.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi924 – 94320
Turni944 – 9474
Helixi952 – 97019
Helixi975 – 98410
Helixi986 – 9894
Beta strandi990 – 9923
Helixi996 – 10027
Beta strandi1003 – 10053
Helixi1009 – 10124
Turni1015 – 10206
Turni1024 – 10263

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DMENMR-A923-1029[»]
ProteinModelPortaliQ92576.
SMRiQ92576. Positions 723-774, 924-1029.

Miscellaneous databases

EvolutionaryTraceiQ92576.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini927 – 1046120TFIIS central
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1797 – 186569Pro-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG255142.
HOVERGENiHBG039623.
InParanoidiQ92576.
OMAiQMPCSTV.
OrthoDBiEOG7NW685.
PhylomeDBiQ92576.
TreeFamiTF350578.

Family and domain databases

Gene3Di1.10.472.30. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR012921. SPOC_C.
IPR003618. TFIIS_cen_dom.
IPR017890. TFS2M.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00628. PHD. 1 hit.
PF07744. SPOC. 1 hit.
PF07500. TFIIS_M. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 1 hit.
SM00510. TFS2M. 1 hit.
[Graphical view]
SUPFAMiSSF46942. SSF46942. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51321. TFIIS_CENTRAL. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92576-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MDIVDTFNHL IPTEHLDDAL FLGSNLENEV CEDFSASQNV LEDSLKNMLS     50
DKDPMLGSAS NQFCLPVLDS NDPNFQMPCS TVVGLDDIMD EGVVKESGND 100
TIDEEELILP NRNLRDKVEE NSVRSPRKSP RLMAQEQVRS LRQSTIAKRS 150
NAAPLSNTKK ASGKTVSTAK AGVKQPERSQ VKEEVCMSLK PEYHKENRRC 200
SRNSGQIEVV PEVSVSSSHS SVSSCLEMKD EDGLDSKHKC NNPGEIDVPS 250
HELNCSLLSE TCVTIGEKKN EALMECKAKP VGSPLFKFSD KEEHEQNDSI 300
SGKTGETVVE EMIATRKVEQ DSKETVKLSH EDDHILEDAG SSDISSDAAC 350
TNPNKTENSL VGLPSCVDEV TECNLELKDT MGIADKTENT LERNKIEPLG 400
YCEDAESNRQ LESTEFNKSN LEVVDTSTFG PESNILENAI CDVPDQNSKQ 450
LNAIESTKIE SHETANLQDD RNSQSSSVSY LESKSVKSKH TKPVIHSKQN 500
MTTDAPKKIV AAKYEVIHSK TKVNVKSVKR NTDVPESQQN FHRPVKVRKK 550
QIDKEPKIQS CNSGVKSVKN QAHSVLKKTL QDQTLVQIFK PLTHSLSDKS 600
HAHPGCLKEP HHPAQTGHVS HSSQKQCHKP QQQAPAMKTN SHVKEELEHP 650
GVEHFKEEDK LKLKKPEKNL QPRQRRSSKS FSLDEPPLFI PDNIATIRRE 700
GSDHSSSFES KYMWTPSKQC GFCKKPHGNR FMVGCGRCDD WFHGDCVGLS 750
LSQAQQMGEE DKEYVCVKCC AEEDKKTEIL DPDTLENQAT VEFHSGDKTM 800
ECEKLGLSKH TTNDRTKYID DTVKHKVKIL KRESGEGRNS SDCRDNEIKK 850
WQLAPLRKMG QPVLPRRSSE EKSEKIPKES TTVTCTGEKA SKPGTHEKQE 900
MKKKKVEKGV LNVHPAASAS KPSADQIRQS VRHSLKDILM KRLTDSNLKV 950
PEEKAAKVAT KIEKELFSFF RDTDAKYKNK YRSLMFNLKD PKNNILFKKV 1000
LKGEVTPDHL IRMSPEELAS KELAAWRRRE NRHTIEMIEK EQREVERRPI 1050
TKITHKGEIE IESDAPMKEQ EAAMEIQEPA ANKSLEKPEG SEKQKEEVDS 1100
MSKDTTSQHR QHLFDLNCKI CIGRMAPPVD DLSPKKVKVV VGVARKHSDN 1150
EAESIADALS STSNILASEF FEEEKQESPK STFSPAPRPE MPGTVEVEST 1200
FLARLNFIWK GFINMPSVAK FVTKAYPVSG SPEYLTEDLP DSIQVGGRIS 1250
PQTVWDYVEK IKASGTKEIC VVRFTPVTEE DQISYTLLFA YFSSRKRYGV 1300
AANNMKQVKD MYLIPLGATD KIPHPLVPFD GPGLELHRPN LLLGLIIRQK 1350
LKRQHSACAS TSHIAETPES APPIALPPDK KSKIEVSTEE APEEENDFFN 1400
SFTTVLHKQR NKPQQNLQED LPTAVEPLME VTKQEPPKPL RFLPGVLIGW 1450
ENQPTTLELA NKPLPVDDIL QSLLGTTGQV YDQAQSVMEQ NTVKEIPFLN 1500
EQTNSKIEKT DNVEVTDGEN KEIKVKVDNI SESTDKSAEI ETSVVGSSSI 1550
SAGSLTSLSL RGKPPDVSTE AFLTNLSIQS KQEETVESKE KTLKRQLQED 1600
QENNLQDNQT SNSSPCRSNV GKGNIDGNVS CSENLVANTA RSPQFINLKR 1650
DPRQAAGRSQ PVTTSESKDG DSCRNGEKHM LPGLSHNKEH LTEQINVEEK 1700
LCSAEKNSCV QQSDNLKVAQ NSPSVENIQT SQAEQAKPLQ EDILMQNIET 1750
VHPFRRGSAV ATSHFEVGNT CPSEFPSKSI TFTSRSTSPR TSTNFSPMRP 1800
QQPNLQHLKS SPPGFPFPGP PNFPPQSMFG FPPHLPPPLL PPPGFGFAQN 1850
PMVPWPPVVH LPGQPQRMMG PLSQASRYIG PQNFYQVKDI RRPERRHSDP 1900
WGRQDQQQLD RPFNRGKGDR QRFYSDSHHL KRERHEKEWE QESERHRRRD 1950
RSQDKDRDRK SREEGHKDKE RARLSHGDRG TDGKASRDSR NVDKKPDKPK 2000
SEDYEKDKER EKSKHREGEK DRDRYHKDRD HTDRTKSKR 2039
Length:2,039
Mass (Da):229,481
Last modified:August 15, 2003 - v3
Checksum:iFDAFF00576005E9B
GO
Isoform 2 (identifier: Q92576-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-88: Missing.

Note: No experimental confirmation available.

Show »
Length:1,951
Mass (Da):219,808
Checksum:iEC2F49C1B80A2ED5
GO

Sequence cautioni

The sequence BAA13438.2 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti525 – 5251V → I.
Corresponds to variant rs34288820 [ dbSNP | Ensembl ].
VAR_051599
Natural varianti1834 – 18341H → Y.
Corresponds to variant rs3734881 [ dbSNP | Ensembl ].
VAR_022040

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8888Missing in isoform 2.
VSP_026434Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1394 – 13941E → G in CAI56715. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF091622 mRNA. Translation: AAF21292.1.
D87685 mRNA. Translation: BAA13438.2. Different initiation.
BX648268 mRNA. Translation: CAI56715.1.
AL050329, AL354719 Genomic DNA. Translation: CAM45842.1.
BC113650 mRNA. Translation: AAI13651.1.
BC113652 mRNA. Translation: AAI13653.1.
CCDSiCCDS4966.1. [Q92576-1]
RefSeqiNP_001277188.1. NM_001290259.1. [Q92576-2]
NP_001277189.1. NM_001290260.1.
NP_055968.1. NM_015153.3. [Q92576-1]
XP_005248758.1. XM_005248701.1. [Q92576-1]
XP_005248759.1. XM_005248702.1. [Q92576-2]
XP_006715489.1. XM_006715426.1. [Q92576-1]
UniGeneiHs.348921.
Hs.731957.

Genome annotation databases

EnsembliENST00000262043; ENSP00000262043; ENSG00000118482. [Q92576-1]
ENST00000393387; ENSP00000377048; ENSG00000118482. [Q92576-1]
GeneIDi23469.
KEGGihsa:23469.
UCSCiuc003pen.2. human. [Q92576-1]

Polymorphism databases

DMDMi34098662.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF091622 mRNA. Translation: AAF21292.1 .
D87685 mRNA. Translation: BAA13438.2 . Different initiation.
BX648268 mRNA. Translation: CAI56715.1 .
AL050329 , AL354719 Genomic DNA. Translation: CAM45842.1 .
BC113650 mRNA. Translation: AAI13651.1 .
BC113652 mRNA. Translation: AAI13653.1 .
CCDSi CCDS4966.1. [Q92576-1 ]
RefSeqi NP_001277188.1. NM_001290259.1. [Q92576-2 ]
NP_001277189.1. NM_001290260.1.
NP_055968.1. NM_015153.3. [Q92576-1 ]
XP_005248758.1. XM_005248701.1. [Q92576-1 ]
XP_005248759.1. XM_005248702.1. [Q92576-2 ]
XP_006715489.1. XM_006715426.1. [Q92576-1 ]
UniGenei Hs.348921.
Hs.731957.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DME NMR - A 923-1029 [» ]
ProteinModelPortali Q92576.
SMRi Q92576. Positions 723-774, 924-1029.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117031. 5 interactions.
IntActi Q92576. 3 interactions.
STRINGi 9606.ENSP00000262043.

PTM databases

PhosphoSitei Q92576.

Polymorphism databases

DMDMi 34098662.

Proteomic databases

MaxQBi Q92576.
PaxDbi Q92576.
PeptideAtlasi Q92576.
PRIDEi Q92576.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262043 ; ENSP00000262043 ; ENSG00000118482 . [Q92576-1 ]
ENST00000393387 ; ENSP00000377048 ; ENSG00000118482 . [Q92576-1 ]
GeneIDi 23469.
KEGGi hsa:23469.
UCSCi uc003pen.2. human. [Q92576-1 ]

Organism-specific databases

CTDi 23469.
GeneCardsi GC06P064403.
HGNCi HGNC:8921. PHF3.
HPAi HPA024676.
HPA025763.
MIMi 607789. gene.
neXtProti NX_Q92576.
PharmGKBi PA33261.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG255142.
HOVERGENi HBG039623.
InParanoidi Q92576.
OMAi QMPCSTV.
OrthoDBi EOG7NW685.
PhylomeDBi Q92576.
TreeFami TF350578.

Miscellaneous databases

ChiTaRSi PHF3. human.
EvolutionaryTracei Q92576.
GeneWikii PHF3.
GenomeRNAii 23469.
NextBioi 45797.
PROi Q92576.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92576.
Bgeei Q92576.
CleanExi HS_PHF3.
Genevestigatori Q92576.

Family and domain databases

Gene3Di 1.10.472.30. 1 hit.
3.30.40.10. 1 hit.
InterProi IPR012921. SPOC_C.
IPR003618. TFIIS_cen_dom.
IPR017890. TFS2M.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF00628. PHD. 1 hit.
PF07744. SPOC. 1 hit.
PF07500. TFIIS_M. 1 hit.
[Graphical view ]
SMARTi SM00249. PHD. 1 hit.
SM00510. TFS2M. 1 hit.
[Graphical view ]
SUPFAMi SSF46942. SSF46942. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEi PS51321. TFIIS_CENTRAL. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "PHF3 expression is frequently reduced in glioma."
    Fischer U., Struss A.-K., Hemmer D., Michel A., Henn W., Steudel W.-I., Meese E.
    Cytogenet. Cell Genet. 94:131-136(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal kidney.
  5. "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].
  6. "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] (ISOFORM 1).
    Tissue: Cerebellum.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. "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-1178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-299; SER-680; SER-1133; SER-1178 AND SER-1642, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Solution structure of the TFIIS domain II of human PHD finger protein 3."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 923-1029.

Entry informationi

Entry nameiPHF3_HUMAN
AccessioniPrimary (citable) accession number: Q92576
Secondary accession number(s): A3KFI8
, Q14CR5, Q5CZI1, Q5T1T6, Q9NQ16, Q9UI45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: August 15, 2003
Last modified: July 9, 2014
This is version 121 of the entry and version 3 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

3D-structure, 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
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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