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Q6ZPK0

- PF21A_MOUSE

UniProt

Q6ZPK0 - PF21A_MOUSE

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Protein

PHD finger protein 21A

Gene

Phf21a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it may act as a scaffold. Inhibits KDM1A-mediated demethylation of 'Lys-4' of histone H3 in vitro, suggesting a role in demethylation regulation (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi405 – 41713A.T hookBy similarityAdd
BLAST
Zinc fingeri468 – 51548PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. DNA binding Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: UniProtKB-KW
  3. suckling behavior Source: MGI
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
PHD finger protein 21A
Alternative name(s):
BHC80a
BRAF35-HDAC complex protein BHC80
Short name:
mBHC80
Gene namesi
Name:Phf21a
Synonyms:Bhc80, Kiaa1696, Pftf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:2384756. Phf21a.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 659659PHD finger protein 21APRO_0000226768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei424 – 4241PhosphothreonineBy similarity
Modified residuei427 – 4271PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6ZPK0.
PaxDbiQ6ZPK0.
PRIDEiQ6ZPK0.

PTM databases

PhosphoSiteiQ6ZPK0.

Expressioni

Tissue specificityi

Expressed in the brain and testis. Weakly or not expressed in other tissues tested. Localized throughout the central nervous system (CNS) in brain, including the cerebellum, hippocampus, and cortex. Notably present in neuronal cells of granular cell layer and dentate gyrus in cerebellum and hippocampus, respectively. In the seminiferous tubules, the signals it is present strongly in spermatocytes, and weakly in spermatogonia and round spermatids. In some cases, it is also observed solely in spermatocytes (at protein level).1 Publication

Gene expression databases

CleanExiMM_PHF21A.
GenevestigatoriQ6ZPK0.

Interactioni

Subunit structurei

Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. In the complex, it interacts directly with HDAC1, HDAC2, HMG20B/BRAF35, KDM1A and RCOR1/CoREST (By similarity).By similarity

Protein-protein interaction databases

BioGridi228685. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ6ZPK0.
SMRiQ6ZPK0. Positions 466-523.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili538 – 58245Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 116113Gln-richAdd
BLAST

Sequence similaritiesi

Contains 1 A.T hook DNA-binding domain.Curated
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri468 – 51548PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG310379.
HOGENOMiHOG000231466.
HOVERGENiHBG080293.
InParanoidiQ6ZPK0.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02178. AT_hook. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00384. AT_hook. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6ZPK0-1) [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
MELQTLQEAL KVEIQVHQKL VAQMKQDPQN ADLKKQLHEL QAKITALSEK
60 70 80 90 100
QKRVVEQLRK NLIVKQEQPD KFQIQPLSQS ENKLQTAQQQ PLQPLQQQQP
110 120 130 140 150
QQPQQQQQQQ QQHAQQSAAA PPSLTASQKT VTTASMITTK TLPLVLKAAT
160 170 180 190 200
ATMPASVVGQ RPTIAMVTAI NSQKAVLSTD VQNTPVNLQT SSKVTGPGAE
210 220 230 240 250
AVQIVAKNTV TLQVQATPPQ PIKVPQFIPP PRLTPRPNFL PQVRPKPVAQ
260 270 280 290 300
NNIPIAPAPP PMLAAPQLIQ RPVMLTKFTP TTLPTSQNSI HPVRVVNGQT
310 320 330 340 350
ATIAKTFPMA QLTSIVIATP GTRLAGPQTV QLSKPSLEKQ LNPTQKQRKN
360 370 380 390 400
KQGLVTHDHL EEIQSKRQER KRRTTANPVY SGAVFEPERK KSAVTYLNST
410 420 430 440 450
MHPGTRKRGR PPKYNAVLGF GALTPTSPPS SHPDSPENEK TETTFTFPAP
460 470 480 490 500
VQPVSLPSPT STDGDIHEDF CSVCRKSGQL LMCDTCSRVY HLDCLEPPLK
510 520 530 540 550
TIPKGMWICP RCQDQMLKKE EAIPWPGTLA IVHSYIAYKA AKEEEKQKLL
560 570 580 590 600
KWSSDLKQER EQLEQKVKEL SSSISKCMEM KSSILARQKE MRSSLDKVKR
610 620 630 640 650
LIRLVHGVDL CRPVDSEATA GALSNGPDCT PPANAASTPA PSPSSQSCTA

NCNQGEETK
Length:659
Mass (Da):72,521
Last modified:March 7, 2006 - v2
Checksum:iE0EECD3F02CCFF78
GO
Isoform 2 (identifier: Q6ZPK0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     129-212: Missing.
     341-352: LNPTQKQRKNKQ → TVKSHPEAEEKQAESRTVTPPAAPKPKREENPQKLAFMVSL

Show »
Length:604
Mass (Da):67,037
Checksum:i7665C91ED1BAC6A8
GO
Isoform 3 (identifier: Q6ZPK0-3) [UniParc]FASTAAdd to Basket

Also known as: BHC80-6(AIF2+5)

The sequence of this isoform differs from the canonical sequence as follows:
     129-129: Missing.

Show »
Length:658
Mass (Da):72,393
Checksum:iF5903B7237BBBA86
GO
Isoform 4 (identifier: Q6ZPK0-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     128-212: Missing.
     341-352: LNPTQKQRKNKQ → TVKSHPEAEEKQAESRTVTPPAAPKPKREENPQKLAFMVSL
     409-463: GRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQPVSLPSPTSTD → ANEEHWPK

Show »
Length:556
Mass (Da):62,168
Checksum:i764F551F8AD5720F
GO
Isoform 5 (identifier: Q6ZPK0-5) [UniParc]FASTAAdd to Basket

Also known as: BHC80-1(AIF1+3)

The sequence of this isoform differs from the canonical sequence as follows:
     128-212: Missing.
     409-463: GRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQPVSLPSPTSTD → ANEEHWPK

Show »
Length:527
Mass (Da):59,092
Checksum:iCC4E08129A9721E8
GO
Isoform 6 (identifier: Q6ZPK0-6) [UniParc]FASTAAdd to Basket

Also known as: BHC80-4(AIF2+3)

The sequence of this isoform differs from the canonical sequence as follows:
     129-129: Missing.
     409-463: GRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQPVSLPSPTSTD → ANEEHWPK

Show »
Length:611
Mass (Da):67,652
Checksum:iA7BB50EF790E4540
GO
Isoform 7 (identifier: Q6ZPK0-7) [UniParc]FASTAAdd to Basket

Also known as: BHC80-2(AIF1+4)

The sequence of this isoform differs from the canonical sequence as follows:
     128-212: Missing.
     409-452: GRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQ → ANEEHWPK

Show »
Length:538
Mass (Da):60,174
Checksum:i0F9B23394047C9EB
GO
Isoform 8 (identifier: Q6ZPK0-8) [UniParc]FASTAAdd to Basket

Also known as: BHC80-5(AIF2+4)

The sequence of this isoform differs from the canonical sequence as follows:
     129-129: Missing.
     409-452: GRPPKYNAVLGFGALTPTSPPSSHPDSPENEKTETTFTFPAPVQ → ANEEHWPK

Show »
Length:622
Mass (Da):68,734
Checksum:i1D5A57648E4DDA9B
GO
Isoform 9 (identifier: Q6ZPK0-9) [UniParc]FASTAAdd to Basket

Also known as: BHC80-3(AIF1+5)

The sequence of this isoform differs from the canonical sequence as follows:
     128-212: Missing.

Show »
Length:574
Mass (Da):63,833
Checksum:iC115A3BB54D6E748
GO

Sequence cautioni

The sequence BAC98234.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti325 – 3251A → P in BAC65327. (PubMed:15325272)Curated
Sequence conflicti325 – 3251A → P in BAC29735. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei128 – 21285Missing in isoform 4, isoform 5, isoform 7 and isoform 9. 2 PublicationsVSP_017450Add
BLAST
Alternative sequencei129 – 21284Missing in isoform 2. 1 PublicationVSP_017451Add
BLAST
Alternative sequencei129 – 1291Missing in isoform 3, isoform 6 and isoform 8. 2 PublicationsVSP_017452
Alternative sequencei341 – 35212LNPTQ…RKNKQ → TVKSHPEAEEKQAESRTVTP PAAPKPKREENPQKLAFMVS L in isoform 2 and isoform 4. 3 PublicationsVSP_017453Add
BLAST
Alternative sequencei409 – 46355GRPPK…PTSTD → ANEEHWPK in isoform 4, isoform 5 and isoform 6. 2 PublicationsVSP_017454Add
BLAST
Alternative sequencei409 – 45244GRPPK…PAPVQ → ANEEHWPK in isoform 7 and isoform 8. 1 PublicationVSP_017455Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB105178 mRNA. Translation: BAC65327.1.
AK129424 Transcribed RNA. Translation: BAC98234.1. Different initiation.
AK037174 mRNA. Translation: BAC29735.1.
BC019181 mRNA. Translation: AAH19181.1.
AY206982 mRNA. Translation: AAP43962.1.
CCDSiCCDS16442.1. [Q6ZPK0-4]
CCDS50645.1. [Q6ZPK0-2]
RefSeqiNP_001103161.1. NM_001109691.1.
NP_620094.2. NM_138755.2.
XP_006499043.1. XM_006498980.1.
UniGeneiMm.330408.

Genome annotation databases

GeneIDi192285.
KEGGimmu:192285.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB105178 mRNA. Translation: BAC65327.1 .
AK129424 Transcribed RNA. Translation: BAC98234.1 . Different initiation.
AK037174 mRNA. Translation: BAC29735.1 .
BC019181 mRNA. Translation: AAH19181.1 .
AY206982 mRNA. Translation: AAP43962.1 .
CCDSi CCDS16442.1. [Q6ZPK0-4 ]
CCDS50645.1. [Q6ZPK0-2 ]
RefSeqi NP_001103161.1. NM_001109691.1.
NP_620094.2. NM_138755.2.
XP_006499043.1. XM_006498980.1.
UniGenei Mm.330408.

3D structure databases

ProteinModelPortali Q6ZPK0.
SMRi Q6ZPK0. Positions 466-523.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 228685. 1 interaction.

PTM databases

PhosphoSitei Q6ZPK0.

Proteomic databases

MaxQBi Q6ZPK0.
PaxDbi Q6ZPK0.
PRIDEi Q6ZPK0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 192285.
KEGGi mmu:192285.

Organism-specific databases

CTDi 51317.
MGIi MGI:2384756. Phf21a.
Rougei Search...

Phylogenomic databases

eggNOGi NOG310379.
HOGENOMi HOG000231466.
HOVERGENi HBG080293.
InParanoidi Q6ZPK0.

Miscellaneous databases

ChiTaRSi Phf21a. mouse.
NextBioi 371282.
PROi Q6ZPK0.
SOURCEi Search...

Gene expression databases

CleanExi MM_PHF21A.
Genevestigatori Q6ZPK0.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR017956. AT_hook_DNA-bd_motif.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF02178. AT_hook. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00384. AT_hook. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of BHC80 in BRAF-HDAC complex, involved in neuron-specific gene repression."
    Iwase S., Januma A., Miyamoto K., Shono N., Honda A., Yanagisawa J., Baba T.
    Biochem. Biophys. Res. Commun. 322:601-608(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5; 6; 7; 8 AND 9), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryonic tail.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Skin.
  4. "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 4).
    Strain: FVB/N-3.
    Tissue: Mammary tumor.
  5. "Mouse ovary and testis gene cohorts and RNA and protein developmental markers from microarray expression profiling."
    Herrera L., Ottolenghi C., Forabosco A., Schlessinger D.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 119-303 (ISOFORM 3).
    Strain: C57BL/6.

Entry informationi

Entry nameiPF21A_MOUSE
AccessioniPrimary (citable) accession number: Q6ZPK0
Secondary accession number(s): Q6XVG0
, Q80Z33, Q8CAZ4, Q8VEC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 7, 2006
Last modified: November 26, 2014
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3