P17028 (ZNF24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zinc finger protein 24

Alternative name(s):
Retinoic acid suppression protein A
Short name=RSG-A
Zinc finger and SCAN domain-containing protein 3
Zinc finger protein 191
Zinc finger protein KOX17

Gene names

Name:	ZNF24
Synonyms:	KOX17, ZNF191, ZSCAN3

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	368 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor required for myelination of differentiated oligodendrocytes. Required for the conversion of oligodendrocytes from the premyelinating to the myelinating state. In the developing central nervous system (CNS), involved in the maintenance in the progenitor stage by promoting the cell cycle. Specifically binds to the 5'-TCAT-3' DNA sequence By similarity. Has transcription repressor activity in vitro. Ref.2
Subcellular location	Nucleus.
Tissue specificity	Expressed in many tissues except in heart.
Post-translational modification	Sumoylated. Ref.9
Sequence similarities	Belongs to the krueppel C2H2-type zinc-finger protein family. Contains 4 C2H2-type zinc fingers. Contains 1 SCAN box domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Repressor
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	myelination Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.2. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral reproduction Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	sequence-specific DNA binding Inferred from sequence or structural similarity. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APLP1	P51693	2	EBI-707773,EBI-74648
ZNF434	Q9BU74	3	EBI-707773,EBI-739949

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P17028-1)

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: P17028-2)

The sequence of this isoform differs from the canonical sequence as follows:
     190-193: DDDG → VIIP
     194-368: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 368

368

Zinc finger protein 24

PRO_0000047352

Regions

Domain

52 – 134

83

SCAN box

Zinc finger

251 – 273

23

C2H2-type 1

Zinc finger

279 – 301

23

C2H2-type 2

Zinc finger

307 – 329

23

C2H2-type 3

Zinc finger

335 – 357

23

C2H2-type 4

Amino acid modifications

Modified residue

132

1

Phosphoserine Ref.12

Modified residue

142

1

Phosphoserine Ref.13

Modified residue

274

1

Phosphoserine Ref.13

Modified residue

335

1

Phosphotyrosine Ref.10

Natural variations

Alternative sequence

190 – 193

4

DDDG → VIIP in isoform 2.

VSP_039219

Alternative sequence

194 – 368

175

Missing in isoform 2.

VSP_039220

Natural variant

220

1

N → S. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7
Corresponds to variant rs2032729 [ dbSNP | Ensembl ].

VAR_012017

Natural variant

331

1

G → W.
Corresponds to variant rs3568 [ dbSNP | Ensembl ].

VAR_012018

Experimental info

Sequence conflict

367

1

K → E in AAB37275. Ref.1

Sequence conflict

367

1

K → E in CAG29324. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

368

Helix Strand Turn

Details...

Helix

47 – 57

11

Helix

60 – 62

3

Beta strand

63 – 65

3

Helix

66 – 81

16

Turn

83 – 85

3

Helix

88 – 102

15

Helix

106 – 114

9

Helix

120 – 134

15

Turn

272 – 275

4

Beta strand

282 – 284

3

Beta strand

287 – 290

4

Helix

291 – 299

9

Helix

300 – 302

3

Beta strand

310 – 312

3

Beta strand

315 – 318

4

Helix

319 – 330

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 23, 2007. Version 4. Checksum: B890EDC512493E0E	FASTA	368	42,155
	10 20 30 40 50 60 MSAQSVEEDS ILIIPTPDEE EKILRVKLEE DPDGEEGSSI PWNHLPDPEI FRQRFRQFGY 70 80 90 100 110 120 QDSPGPREAV SQLRELCRLW LRPETHTKEQ ILELVVLEQF VAILPKELQT WVRDHHPENG 130 140 150 160 170 180 EEAVTVLEDL ESELDDPGQP VSLRRRKREV LVEDMVSQEE AQGLPSSELD AVENQLKWAS 190 200 210 220 230 240 WELHSLRHCD DDGRTENGAL APKQELPSAL ESHEVPGTLN MGVPQIFKYG ETCFPKGRFE 250 260 270 280 290 300 RKRNPSRKKQ HICDECGKHF SQGSALILHQ RIHSGEKPYG CVECGKAFSR SSILVQHQRV 310 320 330 340 350 360 HTGEKPYKCL ECGKAFSQNS GLINHQRIHT GEKPYECVQC GKSYSQSSNL FRHQRRHNAE KLLNVVKV
	Isoform 2 [UniParc]. Checksum: A6A9515C74EA57E0	FASTA	193	22,382
	10 20 30 40 50 60 MSAQSVEEDS ILIIPTPDEE EKILRVKLEE DPDGEEGSSI PWNHLPDPEI FRQRFRQFGY 70 80 90 100 110 120 QDSPGPREAV SQLRELCRLW LRPETHTKEQ ILELVVLEQF VAILPKELQT WVRDHHPENG 130 140 150 160 170 180 EEAVTVLEDL ESELDDPGQP VSLRRRKREV LVEDMVSQEE AQGLPSSELD AVENQLKWAS 190 WELHSLRHCV IIP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Shi S., Yu L. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANT SER-220. Tissue: Liver.
[2]	"Molecular cloning of six novel Kruppel-like zinc finger genes from hematopoietic cells and identification of a novel transregulatory domain KRNB." Han Z.-G., Zhang Q.-H., Ye M., Kan L.-X., Gu B.-W., He K.-L., Shi S.-L., Zhou J., Fu G., Mao M., Chen S.-J., Yu L., Chen Z. J. Biol. Chem. 274:35741-35748(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT SER-220. Tissue: Bone marrow.
[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 1), VARIANT SER-220.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-220.
[5]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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), VARIANT SER-220. Tissue: Lung and Testis.
[8]	"Multiple genes encoding zinc finger domains are expressed in human T cells." Thiesen H.-J. New Biol. 2:363-374(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 319-362 (ISOFORM 1). Tissue: Lymphoid tissue.
[9]	"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates." Gocke C.B., Yu H., Kang J. J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION.
[10]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-335, MASS SPECTROMETRY.
[11]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[12]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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-142 AND SER-274, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Solution structures of the C2H2 type zinc finger domain of human zinc finger protein 24." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 272-330.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U68536 mRNA. Translation: AAB37275.1.
AF016052 Genomic DNA. Translation: AAB70216.1.
AF542097 mRNA. Translation: AAN40767.1.
AF038964 mRNA. Translation: AAD19827.1.
AK291246 mRNA. Translation: BAF83935.1.
BT006658 mRNA. Translation: AAP35304.1.
CR450328 mRNA. Translation: CAG29324.1.
AC116447 Genomic DNA. No translation available.
CH471088 Genomic DNA. Translation: EAX01348.1.
CH471088 Genomic DNA. Translation: EAX01349.1.
BC003566 mRNA. Translation: AAH03566.1.
BC016801 mRNA. Translation: AAH16801.1.
X52348 mRNA. Translation: CAA36574.1.

IPI

IPI00306446.
IPI00964132.

PIR

I37956.

RefSeq

NP_008896.2. NM_006965.2.

UniGene

Hs.514802.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X6E	NMR	-	A	272-330	[»]
3LHR	X-ray	1.90	A/B	46-136	[»]

ProteinModelPortal

P17028.

ModBase

Search...

Protein-protein interaction databases

IntAct

P17028. 41 interactions.

MINT

MINT-1373684.

STRING

9606.ENSP00000261332.

PTM databases

PhosphoSite

P17028.

Polymorphism databases

DMDM

160376173.

Proteomic databases

PaxDb

P17028.

PRIDE

P17028.

Protocols and materials databases

DNASU

7572.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261332; ENSP00000261332; ENSG00000172466.
ENST00000399061; ENSP00000382015; ENSG00000172466.
ENST00000589881; ENSP00000467655; ENSG00000172466.

GeneID

7572.

KEGG

hsa:7572.

UCSC

uc002kys.2. human.
uc002kyu.1. human.

Organism-specific databases

CTD

7572.

GeneCards

GC18M032912.

HGNC

HGNC:13032. ZNF24.

HPA

CAB025642.
HPA024062.

MIM

194534. gene.

neXtProt

NX_P17028.

PharmGKB

PA37610.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5048.

HOGENOM

HOG000234619.

HOVERGEN

HBG018163.

InParanoid

P17028.

KO

K09230.

OMA

ILIIPNP.

OrthoDB

EOG4001JC.

PhylomeDB

P17028.

Gene expression databases

Bgee

P17028.

CleanEx

HS_ZNF24.

Genevestigator

P17028.

GermOnline

ENSG00000172466. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.60. 4 hits.

InterPro

IPR008916. Retrov_capsid_C.
IPR003309. Tscrpt_reg_SCAN.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Pfam

PF02023. SCAN. 1 hit.
[Graphical view]

SMART

SM00431. SCAN. 1 hit.
SM00355. ZnF_C2H2. 4 hits.
[Graphical view]

SUPFAM

SSF47353. Retrov_capsid_C. 1 hit.

PROSITE

PS50804. SCAN_BOX. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P17028.

GenomeRNAi

7572.

NextBio

29617.

PMAP-CutDB

P17028.

SOURCE

Search...

Entry information

Entry name

ZNF24_HUMAN

Accession

Primary (citable) accession number: P17028
Secondary accession number(s): O14754 , Q53YE4, Q6ICR5, Q8IZN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	October 23, 2007
Last modified:	May 1, 2013
This is version 153 of the entry and version 4 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.