Skip Header

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

Q92576

- PHF3_HUMAN

UniProt

Q92576 - PHF3_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

PHD finger protein 3

Gene

PHF3

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-typePROSITE-ProRule annotationAdd
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 3PRO_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

BgeeiQ92576.
CleanExiHS_PHF3.
ExpressionAtlasiQ92576. baseline and differential.
GenevestigatoriQ92576.

Organism-specific databases

HPAiHPA024676.
HPA025763.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1
2039
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi924 – 94320Combined sources
Turni944 – 9474Combined sources
Helixi952 – 97019Combined sources
Helixi975 – 98410Combined sources
Helixi986 – 9894Combined sources
Beta strandi990 – 9923Combined sources
Helixi996 – 10027Combined sources
Beta strandi1003 – 10053Combined sources
Helixi1009 – 10124Combined sources
Turni1015 – 10206Combined sources
Turni1024 – 10263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DMENMR-A923-1029[»]
ProteinModelPortaliQ92576.
SMRiQ92576. Positions 723-774, 924-1029.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92576.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini927 – 1046120TFIIS centralPROSITE-ProRule annotationAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
Contains 1 TFIIS central domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri717 – 77256PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG255142.
GeneTreeiENSGT00530000063844.
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

        10         20         30         40         50
MDIVDTFNHL IPTEHLDDAL FLGSNLENEV CEDFSASQNV LEDSLKNMLS
60 70 80 90 100
DKDPMLGSAS NQFCLPVLDS NDPNFQMPCS TVVGLDDIMD EGVVKESGND
110 120 130 140 150
TIDEEELILP NRNLRDKVEE NSVRSPRKSP RLMAQEQVRS LRQSTIAKRS
160 170 180 190 200
NAAPLSNTKK ASGKTVSTAK AGVKQPERSQ VKEEVCMSLK PEYHKENRRC
210 220 230 240 250
SRNSGQIEVV PEVSVSSSHS SVSSCLEMKD EDGLDSKHKC NNPGEIDVPS
260 270 280 290 300
HELNCSLLSE TCVTIGEKKN EALMECKAKP VGSPLFKFSD KEEHEQNDSI
310 320 330 340 350
SGKTGETVVE EMIATRKVEQ DSKETVKLSH EDDHILEDAG SSDISSDAAC
360 370 380 390 400
TNPNKTENSL VGLPSCVDEV TECNLELKDT MGIADKTENT LERNKIEPLG
410 420 430 440 450
YCEDAESNRQ LESTEFNKSN LEVVDTSTFG PESNILENAI CDVPDQNSKQ
460 470 480 490 500
LNAIESTKIE SHETANLQDD RNSQSSSVSY LESKSVKSKH TKPVIHSKQN
510 520 530 540 550
MTTDAPKKIV AAKYEVIHSK TKVNVKSVKR NTDVPESQQN FHRPVKVRKK
560 570 580 590 600
QIDKEPKIQS CNSGVKSVKN QAHSVLKKTL QDQTLVQIFK PLTHSLSDKS
610 620 630 640 650
HAHPGCLKEP HHPAQTGHVS HSSQKQCHKP QQQAPAMKTN SHVKEELEHP
660 670 680 690 700
GVEHFKEEDK LKLKKPEKNL QPRQRRSSKS FSLDEPPLFI PDNIATIRRE
710 720 730 740 750
GSDHSSSFES KYMWTPSKQC GFCKKPHGNR FMVGCGRCDD WFHGDCVGLS
760 770 780 790 800
LSQAQQMGEE DKEYVCVKCC AEEDKKTEIL DPDTLENQAT VEFHSGDKTM
810 820 830 840 850
ECEKLGLSKH TTNDRTKYID DTVKHKVKIL KRESGEGRNS SDCRDNEIKK
860 870 880 890 900
WQLAPLRKMG QPVLPRRSSE EKSEKIPKES TTVTCTGEKA SKPGTHEKQE
910 920 930 940 950
MKKKKVEKGV LNVHPAASAS KPSADQIRQS VRHSLKDILM KRLTDSNLKV
960 970 980 990 1000
PEEKAAKVAT KIEKELFSFF RDTDAKYKNK YRSLMFNLKD PKNNILFKKV
1010 1020 1030 1040 1050
LKGEVTPDHL IRMSPEELAS KELAAWRRRE NRHTIEMIEK EQREVERRPI
1060 1070 1080 1090 1100
TKITHKGEIE IESDAPMKEQ EAAMEIQEPA ANKSLEKPEG SEKQKEEVDS
1110 1120 1130 1140 1150
MSKDTTSQHR QHLFDLNCKI CIGRMAPPVD DLSPKKVKVV VGVARKHSDN
1160 1170 1180 1190 1200
EAESIADALS STSNILASEF FEEEKQESPK STFSPAPRPE MPGTVEVEST
1210 1220 1230 1240 1250
FLARLNFIWK GFINMPSVAK FVTKAYPVSG SPEYLTEDLP DSIQVGGRIS
1260 1270 1280 1290 1300
PQTVWDYVEK IKASGTKEIC VVRFTPVTEE DQISYTLLFA YFSSRKRYGV
1310 1320 1330 1340 1350
AANNMKQVKD MYLIPLGATD KIPHPLVPFD GPGLELHRPN LLLGLIIRQK
1360 1370 1380 1390 1400
LKRQHSACAS TSHIAETPES APPIALPPDK KSKIEVSTEE APEEENDFFN
1410 1420 1430 1440 1450
SFTTVLHKQR NKPQQNLQED LPTAVEPLME VTKQEPPKPL RFLPGVLIGW
1460 1470 1480 1490 1500
ENQPTTLELA NKPLPVDDIL QSLLGTTGQV YDQAQSVMEQ NTVKEIPFLN
1510 1520 1530 1540 1550
EQTNSKIEKT DNVEVTDGEN KEIKVKVDNI SESTDKSAEI ETSVVGSSSI
1560 1570 1580 1590 1600
SAGSLTSLSL RGKPPDVSTE AFLTNLSIQS KQEETVESKE KTLKRQLQED
1610 1620 1630 1640 1650
QENNLQDNQT SNSSPCRSNV GKGNIDGNVS CSENLVANTA RSPQFINLKR
1660 1670 1680 1690 1700
DPRQAAGRSQ PVTTSESKDG DSCRNGEKHM LPGLSHNKEH LTEQINVEEK
1710 1720 1730 1740 1750
LCSAEKNSCV QQSDNLKVAQ NSPSVENIQT SQAEQAKPLQ EDILMQNIET
1760 1770 1780 1790 1800
VHPFRRGSAV ATSHFEVGNT CPSEFPSKSI TFTSRSTSPR TSTNFSPMRP
1810 1820 1830 1840 1850
QQPNLQHLKS SPPGFPFPGP PNFPPQSMFG FPPHLPPPLL PPPGFGFAQN
1860 1870 1880 1890 1900
PMVPWPPVVH LPGQPQRMMG PLSQASRYIG PQNFYQVKDI RRPERRHSDP
1910 1920 1930 1940 1950
WGRQDQQQLD RPFNRGKGDR QRFYSDSHHL KRERHEKEWE QESERHRRRD
1960 1970 1980 1990 2000
RSQDKDRDRK SREEGHKDKE RARLSHGDRG TDGKASRDSR NVDKKPDKPK
2010 2020 2030
SEDYEKDKER EKSKHREGEK DRDRYHKDRD HTDRTKSKR
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. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1394 – 13941E → G in CAI56715. (PubMed:17974005)Curated

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. 1 PublicationVSP_026434Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00530000063844.
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

Bgeei Q92576.
CleanExi HS_PHF3.
ExpressionAtlasi Q92576. baseline and differential.
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: November 26, 2014
This is version 124 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