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Protein

PR domain zinc finger protein 5

Gene

PRDM5

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

Functioni

Sequence-specific DNA-binding transcription factor. Represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1. Regulates hematopoiesis-associated protein-coding and microRNA (miRNA) genes. May regulate the expression of proteins involved in extracellular matrix development and maintenance, including fibrillar collagens, such as COL4A1 and COL11A1, connective tissue components, such as HAPLN1, and molecules regulating cell migration and adhesion, including EDIL3 and TGFB2. May caused G2/M arrest and apoptosis in cancer cells.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri167 – 19024C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri199 – 22123C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri234 – 25623C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri262 – 28726C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri295 – 31723C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri320 – 34223C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri348 – 37023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri376 – 39823C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri404 – 42623C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri432 – 45524C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri461 – 48323C2H2-type 11PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri489 – 51123C2H2-type 12PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri517 – 53923C2H2-type 13PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri545 – 56723C2H2-type 14PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri573 – 59523C2H2-type 15PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri602 – 62524C2H2-type 16PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • histone deacetylation Source: UniProtKB
  • histone H3-K9 methylation Source: UniProtKB
  • mitotic cell cycle Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
PR domain zinc finger protein 5 (EC:2.1.1.-)
Alternative name(s):
PR domain-containing protein 5
Gene namesi
Name:PRDM5
Synonyms:PFM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:9349. PRDM5.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Brittle cornea syndrome 2 (BCS2)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by extreme corneal thinning resulting in corneal rupture after minor trauma, blue sclerae, keratoconus or keratoglobus, hyperelasticity of the skin, and hypermobile joints.

See also OMIM:614170
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071Y → C in BCS2. 1 Publication
VAR_066393

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614170. phenotype.
Orphaneti90354. Brittle cornea syndrome.
PharmGKBiPA33717.

Polymorphism and mutation databases

BioMutaiPRDM5.
DMDMi212276458.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 630630PR domain zinc finger protein 5PRO_0000047761Add
BLAST

Proteomic databases

PaxDbiQ9NQX1.
PRIDEiQ9NQX1.

PTM databases

PhosphoSiteiQ9NQX1.

Expressioni

Tissue specificityi

Widely expressed with highest levels in colon and ovary. Tends to be silenced in breast, colorectal, gastric and liver cancer tissues.2 Publications

Gene expression databases

BgeeiQ9NQX1.
CleanExiHS_PRDM5.
ExpressionAtlasiQ9NQX1. baseline and differential.
GenevisibleiQ9NQX1. HS.

Organism-specific databases

HPAiHPA051406.

Interactioni

Subunit structurei

Interacts with EHMT2/G9A, GFI1 and HDAC1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EHMT2Q96KQ73EBI-4292031,EBI-744366
GFI1Q996842EBI-4292031,EBI-949368
HDAC1Q135473EBI-4292031,EBI-301834

Protein-protein interaction databases

BioGridi116287. 32 interactions.
IntActiQ9NQX1. 4 interactions.
STRINGi9606.ENSP00000264808.

Structurei

3D structure databases

ProteinModelPortaliQ9NQX1.
SMRiQ9NQX1. Positions 4-620.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 124117SETPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
Contains 16 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri167 – 19024C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri199 – 22123C2H2-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri234 – 25623C2H2-type 3; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri262 – 28726C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri295 – 31723C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri320 – 34223C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri348 – 37023C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri376 – 39823C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri404 – 42623C2H2-type 9PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri432 – 45524C2H2-type 10PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri461 – 48323C2H2-type 11PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri489 – 51123C2H2-type 12PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri517 – 53923C2H2-type 13PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri545 – 56723C2H2-type 14PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri573 – 59523C2H2-type 15PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri602 – 62524C2H2-type 16PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00780000122027.
HOGENOMiHOG000234617.
HOVERGENiHBG098380.
InParanoidiQ9NQX1.
OMAiLGCKEDY.
OrthoDBiEOG7KSX7Q.
PhylomeDBiQ9NQX1.
TreeFamiTF106478.

Family and domain databases

Gene3Di3.30.160.60. 14 hits.
InterProiIPR001214. SET_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
IPR022755. Znf_C2H2_jaz.
IPR017125. Znf_PRDM5.
[Graphical view]
PANTHERiPTHR24409:SF17. PTHR24409:SF17. 1 hit.
PfamiPF00096. zf-C2H2. 3 hits.
PF12171. zf-C2H2_jaz. 1 hit.
[Graphical view]
PIRSFiPIRSF037162. PRDM. 1 hit.
SMARTiSM00317. SET. 1 hit.
SM00355. ZnF_C2H2. 16 hits.
[Graphical view]
PROSITEiPS50280. SET. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 14 hits.
PS50157. ZINC_FINGER_C2H2_2. 16 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NQX1-1) [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
MLGMYVPDRF SLKSSRVQDG MGLYTARRVR KGEKFGPFAG EKRMPEDLDE
60 70 80 90 100
NMDYRLMWEV RGSKGEVLYI LDATNPRHSN WLRFVHEAPS QEQKNLAAIQ
110 120 130 140 150
EGENIFYLAV EDIETDTELL IGYLDSDMEA EEEEQQIMTV IKEGEVENSR
160 170 180 190 200
RQSTAGRKDR LGCKEDYACP QCESSFTSED ILAEHLQTLH QKPTEEKEFK
210 220 230 240 250
CKNCGKKFPV KQALQRHVLQ CTAKSSLKES SRSFQCSVCN SSFSSASSFE
260 270 280 290 300
QHQETCRGDA RFVCKADSCG KRLKSKDALK RHQENVHTGD PKKKLICSVC
310 320 330 340 350
NKKCSSASSL QEHRKIHEIF DCQECMKKFI SANQLKRHMI THSEKRPYNC
360 370 380 390 400
EICNKSFKRL DQVGAHKVIH SEDKPYKCKL CGKGFAHRNV YKNHKKTHSE
410 420 430 440 450
ERPFQCEECK ALFRTPFSLQ RHLLIHNSER TFKCHHCDAT FKRKDTLNVH
460 470 480 490 500
VQVVHERHKK YRCELCNKAF VTPSVLRSHK KTHTGEKEKI CPYCGQKFAS
510 520 530 540 550
SGTLRVHIRS HTGERPYQCP YCEKGFSKND GLKMHIRTHT REKPYKCSEC
560 570 580 590 600
SKAFSQKRGL DEHKRTHTGE KPFQCDVCDL AFSLKKMLIR HKMTHNPNRP
610 620 630
LAECQFCHKK FTRNDYLKVH MDNIHGVADS
Length:630
Mass (Da):73,090
Last modified:November 4, 2008 - v2
Checksum:iD16AF81AB5A34398
GO
Isoform 2 (identifier: Q9NQX1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     218-248: Missing.

Show »
Length:599
Mass (Da):69,862
Checksum:i567E937469373B58
GO
Isoform 3 (identifier: Q9NQX1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     101-111: EGENIFYLAVE → DKNLGPAEWRG
     112-630: Missing.

Show »
Length:111
Mass (Da):12,874
Checksum:iF0568A1C8495EC01
GO
Isoform 4 (identifier: Q9NQX1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     218-248: Missing.
     515-532: RPYQCPYCEKGFSKNDGL → AVQVLRVQQGLQPEARPG
     533-630: Missing.

Note: No experimental confirmation available.
Show »
Length:501
Mass (Da):58,124
Checksum:i5560F041B4F4B3E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611R → K in AAF78077 (PubMed:15077163).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071Y → C in BCS2. 1 Publication
VAR_066393

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei101 – 11111EGENIFYLAVE → DKNLGPAEWRG in isoform 3. 2 PublicationsVSP_035652Add
BLAST
Alternative sequencei112 – 630519Missing in isoform 3. 2 PublicationsVSP_035653Add
BLAST
Alternative sequencei218 – 24831Missing in isoform 2 and isoform 4. 1 PublicationVSP_035654Add
BLAST
Alternative sequencei515 – 53218RPYQC…KNDGL → AVQVLRVQQGLQPEARPG in isoform 4. 1 PublicationVSP_054395Add
BLAST
Alternative sequencei533 – 63098Missing in isoform 4. 1 PublicationVSP_054396Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF272897 mRNA. Translation: AAF78077.1.
AK056352 mRNA. Translation: BAG51686.1.
AC025741 Genomic DNA. No translation available.
AC104068 Genomic DNA. No translation available.
AC104795 Genomic DNA. No translation available.
BC066942 mRNA. Translation: AAH66942.1.
BC121037 mRNA. Translation: AAI21038.1.
BC121038 mRNA. Translation: AAI21039.1.
CCDSiCCDS3716.1. [Q9NQX1-1]
CCDS75187.1. [Q9NQX1-4]
CCDS75188.1. [Q9NQX1-2]
RefSeqiNP_001287752.1. NM_001300823.1. [Q9NQX1-2]
NP_001287753.1. NM_001300824.1. [Q9NQX1-4]
NP_061169.2. NM_018699.3. [Q9NQX1-1]
UniGeneiHs.666782.

Genome annotation databases

EnsembliENST00000264808; ENSP00000264808; ENSG00000138738. [Q9NQX1-1]
ENST00000394435; ENSP00000377955; ENSG00000138738. [Q9NQX1-3]
ENST00000428209; ENSP00000404832; ENSG00000138738. [Q9NQX1-2]
ENST00000515109; ENSP00000422309; ENSG00000138738. [Q9NQX1-4]
GeneIDi11107.
KEGGihsa:11107.
UCSCiuc003idn.3. human. [Q9NQX1-1]
uc003ido.3. human. [Q9NQX1-2]
uc003idp.1. human. [Q9NQX1-3]
uc010ine.3. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF272897 mRNA. Translation: AAF78077.1.
AK056352 mRNA. Translation: BAG51686.1.
AC025741 Genomic DNA. No translation available.
AC104068 Genomic DNA. No translation available.
AC104795 Genomic DNA. No translation available.
BC066942 mRNA. Translation: AAH66942.1.
BC121037 mRNA. Translation: AAI21038.1.
BC121038 mRNA. Translation: AAI21039.1.
CCDSiCCDS3716.1. [Q9NQX1-1]
CCDS75187.1. [Q9NQX1-4]
CCDS75188.1. [Q9NQX1-2]
RefSeqiNP_001287752.1. NM_001300823.1. [Q9NQX1-2]
NP_001287753.1. NM_001300824.1. [Q9NQX1-4]
NP_061169.2. NM_018699.3. [Q9NQX1-1]
UniGeneiHs.666782.

3D structure databases

ProteinModelPortaliQ9NQX1.
SMRiQ9NQX1. Positions 4-620.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116287. 32 interactions.
IntActiQ9NQX1. 4 interactions.
STRINGi9606.ENSP00000264808.

PTM databases

PhosphoSiteiQ9NQX1.

Polymorphism and mutation databases

BioMutaiPRDM5.
DMDMi212276458.

Proteomic databases

PaxDbiQ9NQX1.
PRIDEiQ9NQX1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264808; ENSP00000264808; ENSG00000138738. [Q9NQX1-1]
ENST00000394435; ENSP00000377955; ENSG00000138738. [Q9NQX1-3]
ENST00000428209; ENSP00000404832; ENSG00000138738. [Q9NQX1-2]
ENST00000515109; ENSP00000422309; ENSG00000138738. [Q9NQX1-4]
GeneIDi11107.
KEGGihsa:11107.
UCSCiuc003idn.3. human. [Q9NQX1-1]
uc003ido.3. human. [Q9NQX1-2]
uc003idp.1. human. [Q9NQX1-3]
uc010ine.3. human.

Organism-specific databases

CTDi11107.
GeneCardsiGC04M121613.
HGNCiHGNC:9349. PRDM5.
HPAiHPA051406.
MIMi614161. gene.
614170. phenotype.
neXtProtiNX_Q9NQX1.
Orphaneti90354. Brittle cornea syndrome.
PharmGKBiPA33717.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00780000122027.
HOGENOMiHOG000234617.
HOVERGENiHBG098380.
InParanoidiQ9NQX1.
OMAiLGCKEDY.
OrthoDBiEOG7KSX7Q.
PhylomeDBiQ9NQX1.
TreeFamiTF106478.

Miscellaneous databases

GenomeRNAii11107.
NextBioi42230.
PROiQ9NQX1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NQX1.
CleanExiHS_PRDM5.
ExpressionAtlasiQ9NQX1. baseline and differential.
GenevisibleiQ9NQX1. HS.

Family and domain databases

Gene3Di3.30.160.60. 14 hits.
InterProiIPR001214. SET_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
IPR022755. Znf_C2H2_jaz.
IPR017125. Znf_PRDM5.
[Graphical view]
PANTHERiPTHR24409:SF17. PTHR24409:SF17. 1 hit.
PfamiPF00096. zf-C2H2. 3 hits.
PF12171. zf-C2H2_jaz. 1 hit.
[Graphical view]
PIRSFiPIRSF037162. PRDM. 1 hit.
SMARTiSM00317. SET. 1 hit.
SM00355. ZnF_C2H2. 16 hits.
[Graphical view]
PROSITEiPS50280. SET. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 14 hits.
PS50157. ZINC_FINGER_C2H2_2. 16 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PRDM5 is silenced in human cancers and has growth suppressive activities."
    Deng Q., Huang S.
    Oncogene 23:4903-4910(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "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 3).
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 2; 3 AND 4).
    Tissue: Brain.
  5. Cited for: TISSUE SPECIFICITY.
  6. "Epigenetic regulation of protein-coding and microRNA genes by the Gfi1-interacting tumor suppressor PRDM5."
    Duan Z., Person R.E., Lee H.-H., Huang S., Donadieu J., Badolato R., Grimes H.L., Papayannopoulou T., Horwitz M.S.
    Mol. Cell. Biol. 27:6889-6902(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EHMT2; GFI1 AND HDAC1, SUBCELLULAR LOCATION.
  7. Cited for: VARIANT BCS2 CYS-107, FUNCTION.

Entry informationi

Entry nameiPRDM5_HUMAN
AccessioniPrimary (citable) accession number: Q9NQX1
Secondary accession number(s): Q0VAI9, Q0VAJ0, Q6NXQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 4, 2008
Last modified: June 24, 2015
This is version 131 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.