Q96BD5 (PF21A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
PHD finger protein 21A

Alternative name(s):
BHC80a
BRAF35-HDAC complex protein BHC80

Gene names

Name:	PHF21A
Synonyms:	BHC80, KIAA1696
ORF Names:	BM-006

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	680 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.10
Subunit structure	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. Ref.1 Ref.8 Ref.9
Subcellular location	Nucleus By similarity.
Tissue specificity	Highly expressed in brain. Expressed at much lower level in other tissues. Ref.1
Sequence similarities	Contains 1 A.T hook DNA-binding domain. Contains 1 PHD-type zinc finger.
Sequence caution	The sequence AAF64262.1 differs from that shown. Reason: Frameshift at several positions. The sequence BAB21787.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.9. Source: MGI regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW suckling behavior Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	histone deacetylase complex Inferred from direct assay Ref.9. Source: MGI
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96BD5-1)

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.

Isoform 2 (identifier: Q96BD5-2)

Also known as: hBHC80-4;

The sequence of this isoform differs from the canonical sequence as follows:
     204-204: L → LQ
     429-483: GRPPKYNAVLGFGALTPTSPQSSHPDSPENEKTETTFTFPAPVQPVSLPSPTSTD → ANEEHWPK

Isoform 3 (identifier: Q96BD5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     204-204: L → LQ

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 680

680

PHD finger protein 21A

PRO_0000226767

Regions

DNA binding

425 – 437

13

A.T hook

Zinc finger

488 – 535

48

PHD-type

Region

486 – 680

195

Required for transcriptional repression

Coiled coil

558 – 603

46

Potential

Compositional bias

4 – 108

105

Gln-rich

Amino acid modifications

Modified residue

444

1

Phosphothreonine Ref.12

Modified residue

447

1

Phosphoserine Ref.12

Natural variations

Alternative sequence

204

1

L → LQ in isoform 2 and isoform 3.

VSP_017448

Alternative sequence

429 – 483

55

GRPPK…PTSTD → ANEEHWPK in isoform 2.

VSP_017449

Natural variant

347

1

R → H. Ref.1 Ref.3
Corresponds to variant rs3736508 [ dbSNP | Ensembl ].

VAR_025515

Experimental info

Sequence conflict

447

1

S → P in BAB13839. Ref.3

Sequence conflict

662 – 680

19

PSPSS…GEETK → LCSLPELHSEL Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

680

Helix Strand Turn

Details...

Turn

492 – 494

3

Beta strand

504 – 507

4

Helix

512 – 514

3

Beta strand

515 – 517

3

Helix

530 – 538

9

Turn

539 – 542

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: C7AF87EB2984A796	FASTA	680	74,854
	10 20 30 40 50 60 MELQTLQEAL KVEIQVHQKL VAQMKQDPQN ADLKKQLHEL QAKITALSEK QKRVVEQLRK 70 80 90 100 110 120 NLIVKQEQPD KFQIQPLPQS ENKLQTAQQQ PLQQLQQQQQ YHHHHAQQSA AASPNLTASQ 130 140 150 160 170 180 KTVTTASMIT TKTLPLVLKA ATATMPASVV GQRPTIAMVT AINSQKAVLS TDVQNTPVNL 190 200 210 220 230 240 QTSSKVTGPG AEAVQIVAKN TVTLVQATPP QPIKVPQFIP PPRLTPRPNF LPQVRPKPVA 250 260 270 280 290 300 QNNIPIAPAP PPMLAAPQLI QRPVMLTKFT PTTLPTSQNS IHPVRVVNGQ TATIAKTFPM 310 320 330 340 350 360 AQLTSIVIAT PGTRLAGPQT VQLSKPSLEK QTVKSHTETD EKQTESRTIT PPAAPKPKRE 370 380 390 400 410 420 ENPQKLAFMV SLGLVTHDHL EEIQSKRQER KRRTTANPVY SGAVFEPERK KSAVTYLNST 430 440 450 460 470 480 MHPGTRKRGR PPKYNAVLGF GALTPTSPQS SHPDSPENEK TETTFTFPAP VQPVSLPSPT 490 500 510 520 530 540 STDGDIHEDF CSVCRKSGQL LMCDTCSRVY HLDCLDPPLK TIPKGMWICP RCQDQMLKKE 550 560 570 580 590 600 EAIPWPGTLA IVHSYIAYKA AKEEEKQKLL KWSSDLKQER EQLEQKVKQL SNSISKCMEM 610 620 630 640 650 660 KNTILARQKE MHSSLEKVKQ LIRLIHGIDL SKPVDSEATV GAISNGPDCT PPANAATSTP 670 680 APSPSSQSCT ANCNQGEETK
	Isoform 2 (hBHC80-4) [UniParc]. Checksum: B1F247CD92D7D411	FASTA	634	70,210
	10 20 30 40 50 60 MELQTLQEAL KVEIQVHQKL VAQMKQDPQN ADLKKQLHEL QAKITALSEK QKRVVEQLRK 70 80 90 100 110 120 NLIVKQEQPD KFQIQPLPQS ENKLQTAQQQ PLQQLQQQQQ YHHHHAQQSA AASPNLTASQ 130 140 150 160 170 180 KTVTTASMIT TKTLPLVLKA ATATMPASVV GQRPTIAMVT AINSQKAVLS TDVQNTPVNL 190 200 210 220 230 240 QTSSKVTGPG AEAVQIVAKN TVTLQVQATP PQPIKVPQFI PPPRLTPRPN FLPQVRPKPV 250 260 270 280 290 300 AQNNIPIAPA PPPMLAAPQL IQRPVMLTKF TPTTLPTSQN SIHPVRVVNG QTATIAKTFP 310 320 330 340 350 360 MAQLTSIVIA TPGTRLAGPQ TVQLSKPSLE KQTVKSHTET DEKQTESRTI TPPAAPKPKR 370 380 390 400 410 420 EENPQKLAFM VSLGLVTHDH LEEIQSKRQE RKRRTTANPV YSGAVFEPER KKSAVTYLNS 430 440 450 460 470 480 TMHPGTRKRA NEEHWPKGDI HEDFCSVCRK SGQLLMCDTC SRVYHLDCLD PPLKTIPKGM 490 500 510 520 530 540 WICPRCQDQM LKKEEAIPWP GTLAIVHSYI AYKAAKEEEK QKLLKWSSDL KQEREQLEQK 550 560 570 580 590 600 VKQLSNSISK CMEMKNTILA RQKEMHSSLE KVKQLIRLIH GIDLSKPVDS EATVGAISNG 610 620 630 PDCTPPANAA TSTPAPSPSS QSCTANCNQG EETK
	Isoform 3 [UniParc]. Checksum: F95DC57A1D3C0FEC	FASTA	681	74,982
	10 20 30 40 50 60 MELQTLQEAL KVEIQVHQKL VAQMKQDPQN ADLKKQLHEL QAKITALSEK QKRVVEQLRK 70 80 90 100 110 120 NLIVKQEQPD KFQIQPLPQS ENKLQTAQQQ PLQQLQQQQQ YHHHHAQQSA AASPNLTASQ 130 140 150 160 170 180 KTVTTASMIT TKTLPLVLKA ATATMPASVV GQRPTIAMVT AINSQKAVLS TDVQNTPVNL 190 200 210 220 230 240 QTSSKVTGPG AEAVQIVAKN TVTLQVQATP PQPIKVPQFI PPPRLTPRPN FLPQVRPKPV 250 260 270 280 290 300 AQNNIPIAPA PPPMLAAPQL IQRPVMLTKF TPTTLPTSQN SIHPVRVVNG QTATIAKTFP 310 320 330 340 350 360 MAQLTSIVIA TPGTRLAGPQ TVQLSKPSLE KQTVKSHTET DEKQTESRTI TPPAAPKPKR 370 380 390 400 410 420 EENPQKLAFM VSLGLVTHDH LEEIQSKRQE RKRRTTANPV YSGAVFEPER KKSAVTYLNS 430 440 450 460 470 480 TMHPGTRKRG RPPKYNAVLG FGALTPTSPQ SSHPDSPENE KTETTFTFPA PVQPVSLPSP 490 500 510 520 530 540 TSTDGDIHED FCSVCRKSGQ LLMCDTCSRV YHLDCLDPPL KTIPKGMWIC PRCQDQMLKK 550 560 570 580 590 600 EEAIPWPGTL AIVHSYIAYK AAKEEEKQKL LKWSSDLKQE REQLEQKVKQ LSNSISKCME 610 620 630 640 650 660 MKNTILARQK EMHSSLEKVK QLIRLIHGID LSKPVDSEAT VGAISNGPDC TPPANAATST 670 680 PAPSPSSQSC TANCNQGEET K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes." Hakimi M.-A., Bochar D.A., Chenoweth J., Lane W.S., Mandel G., Shiekhattar R. Proc. Natl. Acad. Sci. U.S.A. 99:7420-7425(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1; HDAC2; HMG20B; KDM1A AND RCOR1, TISSUE SPECIFICITY, VARIANT HIS-347.
[2]	"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O. DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-456 (ISOFORM 3), VARIANT HIS-347. Tissue: Embryo and Teratocarcinoma.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Uterus.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-680 (ISOFORM 1). Tissue: Fetal kidney.
[7]	"A novel gene expressed in human bone marrow." Zhao M., Song H., Li N., Peng Y., Han Z., Chen Z. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-672 (ISOFORMS 2/3). Tissue: Bone marrow.
[8]	"A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes." Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R. J. Biol. Chem. 278:7234-7239(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1; HDAC2; HMG20B; KDM1A; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
[9]	"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: INTERACTION WITH HDAC1; HDAC2; HMG20B; KDM1A AND RCOR1.
[10]	"Regulation of LSD1 histone demethylase activity by its associated factors." Shi Y.-J., Matson C., Lan F., Iwase S., Baba T., Shi Y. Mol. Cell 19:857-864(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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 THR-444 AND SER-447, MASS SPECTROMETRY. 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"Solution structure of the PHD domain in PHD finger protein 21A." RIKEN structural genomics initiative (RSGI) Submitted (MAR-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 487-535.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY090777 mRNA. Translation: AAM09095.1.
AB051483 mRNA. Translation: BAB21787.1. Different initiation.
AK021530 mRNA. Translation: BAB13839.1.
AK023258 mRNA. Translation: BAB14492.1.
CH471064 Genomic DNA. Translation: EAW68012.1.
CH471064 Genomic DNA. Translation: EAW68013.1.
CH471064 Genomic DNA. Translation: EAW68015.1.
CH471064 Genomic DNA. Translation: EAW68017.1.
BC015714 mRNA. Translation: AAH15714.1.
BX648236 mRNA. Translation: CAH10542.1.
AF208848 mRNA. Translation: AAF64262.1. Frameshift.

IPI

IPI00041959.
IPI00054460.
IPI00737174.

RefSeq

NP_001095272.1. NM_001101802.1.
NP_057705.3. NM_016621.3.

UniGene

Hs.502458.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PUY	X-ray	1.43	A/B	486-543	[»]
2YQL	NMR	-	A	487-535	[»]

ProteinModelPortal

Q96BD5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96BD5. 7 interactions.

MINT

MINT-1469147.

STRING

9606.ENSP00000398824.

PTM databases

PhosphoSite

Q96BD5.

Polymorphism databases

DMDM

74731224.

Proteomic databases

PaxDb

Q96BD5.

PRIDE

Q96BD5.

Protocols and materials databases

DNASU

51317.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000257821; ENSP00000257821; ENSG00000135365.
ENST00000323180; ENSP00000323152; ENSG00000135365.
ENST00000418153; ENSP00000398824; ENSG00000135365.

GeneID

51317.

KEGG

hsa:51317.

UCSC

uc001ncb.4. human.
uc001ncc.4. human.
uc001nce.2. human.

Organism-specific databases

CTD

51317.

GeneCards

GC11M045950.

HGNC

HGNC:24156. PHF21A.

HPA

HPA023580.

MIM

608325. gene.

neXtProt

NX_Q96BD5.

Orphanet

52022. Potocki-Shaffer syndrome.

PharmGKB

PA134977844.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG310379.

HOVERGEN

HBG080293.

InParanoid

Q96BD5.

OMA

SCTVNCN.

OrthoDB

EOG4KWJSH.

PhylomeDB

Q96BD5.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q96BD5.

Bgee

Q96BD5.

CleanEx

HS_PHF21A.

Genevestigator

Q96BD5.

GermOnline

ENSG00000135365. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

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]

Pfam

PF02178. AT_hook. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]

SMART

SM00384. AT_hook. 1 hit.
SM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q96BD5.

GenomeRNAi

51317.

NextBio

54681.

SOURCE

Search...

Entry information

Entry name

PF21A_HUMAN

Accession

Primary (citable) accession number: Q96BD5
Secondary accession number(s): D3DQP5 , Q6AWA2, Q9C0G7, Q9H8V9, Q9HAK6, Q9NZE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	December 1, 2001
Last modified:	May 29, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.