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Protein

Zinc finger protein with KRAB and SCAN domains 4

Gene

ZKSCAN4

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

Functioni

May be involved in the transcriptional activation of MDM2 and EP300 genes.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri320 – 34223C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri348 – 37023C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri376 – 39823C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri404 – 42623C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri432 – 45423C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri487 – 50923C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri515 – 53723C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-212436. Generic Transcription Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein with KRAB and SCAN domains 4
Alternative name(s):
P373c6.1
Zinc finger protein 307
Zinc finger protein 427
Gene namesi
Name:ZKSCAN4
Synonyms:ZNF307, ZNF427
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:13854. ZKSCAN4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162409784.

Polymorphism and mutation databases

BioMutaiZKSCAN4.
DMDMi23396993.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 545545Zinc finger protein with KRAB and SCAN domains 4PRO_0000047525Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki26 – 26Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki178 – 178Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ969J2.
MaxQBiQ969J2.
PaxDbiQ969J2.
PRIDEiQ969J2.

PTM databases

iPTMnetiQ969J2.
PhosphoSiteiQ969J2.

Expressioni

Tissue specificityi

Expressed in adult heart, brain, placenta, lung and kidney, but not in adult liver and skeletal muscle. In 17-day old embryo, detected in liver, skeletal muscle, brain, heart and small intestine.1 Publication

Gene expression databases

BgeeiQ969J2.
CleanExiHS_ZKSCAN4.
GenevisibleiQ969J2. HS.

Organism-specific databases

HPAiHPA009637.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CABP5Q9NP863EBI-2818641,EBI-10311131
LXNQ9BS403EBI-2818641,EBI-1044504
SCAND1P570863EBI-2818641,EBI-745846
TRIM39Q9HCM93EBI-2818641,EBI-739510
ZKSCAN7Q9P0L13EBI-2818641,EBI-743851
ZNF496Q96IT13EBI-2818641,EBI-743906
ZSCAN32I3L3J23EBI-2818641,EBI-10178206

Protein-protein interaction databases

BioGridi132179. 29 interactions.
IntActiQ969J2. 8 interactions.
STRINGi9606.ENSP00000366509.

Structurei

3D structure databases

ProteinModelPortaliQ969J2.
SMRiQ969J2. Positions 49-136, 286-541.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 13583SCAN boxPROSITE-ProRule annotationAdd
BLAST
Domaini221 – 31797KRABPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 7 C2H2-type zinc fingers.PROSITE-ProRule annotation
Contains 1 KRAB domain.PROSITE-ProRule annotation
Contains 1 SCAN box domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri320 – 34223C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri348 – 37023C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri376 – 39823C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri404 – 42623C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri432 – 45423C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri487 – 50923C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri515 – 53723C2H2-type 7PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118881.
HOGENOMiHOG000234619.
HOVERGENiHBG018163.
InParanoidiQ969J2.
OMAiWESQGRT.
OrthoDBiEOG79GT5W.
PhylomeDBiQ969J2.
TreeFamiTF350830.

Family and domain databases

Gene3Di3.30.160.60. 7 hits.
InterProiIPR001909. KRAB.
IPR008916. Retrov_capsid_C.
IPR003309. SCAN_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF02023. SCAN. 1 hit.
PF00096. zf-C2H2. 5 hits.
PF13912. zf-C2H2_6. 1 hit.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
SM00431. SCAN. 1 hit.
SM00355. ZnF_C2H2. 7 hits.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
SSF47353. SSF47353. 1 hit.
PROSITEiPS50805. KRAB. 1 hit.
PS50804. SCAN_BOX. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q969J2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAREPRKNAA LDAQSAEDQT GLLTVKVEKE EASALTAEVR APCSPARGPE
60 70 80 90 100
RSRQRFRGFR YPEAAGPREA LSRLRELCGQ WLQPEMHSKE QILELLVLEQ
110 120 130 140 150
FLTILPGNLQ SWVREQHPES GEEVVVLLEY LERQLDEPAP QVPVGDQGQE
160 170 180 190 200
LLCCKMALLT QTQGSQSSQC QPMKALFKHE SLGSQPLHDR VLQVPGLAQG
210 220 230 240 250
GCCREDAMVA SRLTPGSQGL LKMEDVALTL TPGWTQLDSS QVNLYRDEKQ
260 270 280 290 300
ENHSSLVSLG GEIQTKSRDL PPVKKLPEKE HGKICHLRED IAQIPTHAEA
310 320 330 340 350
GEQEGRLQRK QKNAIGSRRH YCHECGKSFA QSSGLTKHRR IHTGEKPYEC
360 370 380 390 400
EDCGKTFIGS SALVIHQRVH TGEKPYECEE CGKVFSHSSN LIKHQRTHTG
410 420 430 440 450
EKPYECDDCG KTFSQSCSLL EHHKIHTGEK PYQCNMCGKA FRRNSHLLRH
460 470 480 490 500
QRIHGDKNVQ NPEHGESWES QGRTESQWEN TEAPVSYKCN ECERSFTRNR
510 520 530 540
SLIEHQKIHT GEKPYQCDTC GKGFTRTSYL VQHQRSHVGK KTLSQ
Length:545
Mass (Da):61,579
Last modified:December 1, 2001 - v1
Checksum:iCCFB6B5D976926ED
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331S → F.
Corresponds to variant rs9986596 [ dbSNP | Ensembl ].
VAR_059951

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY781778 mRNA. Translation: AAV41023.1.
AK315783 mRNA. Translation: BAG38129.1.
AL022393 Genomic DNA. Translation: CAC69823.1.
CH471081 Genomic DNA. Translation: EAX03142.1.
BC014031 mRNA. Translation: AAH14031.1.
CCDSiCCDS4647.1.
RefSeqiNP_061983.2. NM_019110.4.
XP_005249152.1. XM_005249095.2.
UniGeneiHs.44720.
Hs.739171.

Genome annotation databases

EnsembliENST00000377294; ENSP00000366509; ENSG00000187626.
GeneIDi387032.
UCSCiuc003nks.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY781778 mRNA. Translation: AAV41023.1.
AK315783 mRNA. Translation: BAG38129.1.
AL022393 Genomic DNA. Translation: CAC69823.1.
CH471081 Genomic DNA. Translation: EAX03142.1.
BC014031 mRNA. Translation: AAH14031.1.
CCDSiCCDS4647.1.
RefSeqiNP_061983.2. NM_019110.4.
XP_005249152.1. XM_005249095.2.
UniGeneiHs.44720.
Hs.739171.

3D structure databases

ProteinModelPortaliQ969J2.
SMRiQ969J2. Positions 49-136, 286-541.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi132179. 29 interactions.
IntActiQ969J2. 8 interactions.
STRINGi9606.ENSP00000366509.

PTM databases

iPTMnetiQ969J2.
PhosphoSiteiQ969J2.

Polymorphism and mutation databases

BioMutaiZKSCAN4.
DMDMi23396993.

Proteomic databases

EPDiQ969J2.
MaxQBiQ969J2.
PaxDbiQ969J2.
PRIDEiQ969J2.

Protocols and materials databases

DNASUi387032.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377294; ENSP00000366509; ENSG00000187626.
GeneIDi387032.
UCSCiuc003nks.2. human.

Organism-specific databases

CTDi387032.
GeneCardsiZKSCAN4.
HGNCiHGNC:13854. ZKSCAN4.
HPAiHPA009637.
MIMi611643. gene.
neXtProtiNX_Q969J2.
PharmGKBiPA162409784.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000118881.
HOGENOMiHOG000234619.
HOVERGENiHBG018163.
InParanoidiQ969J2.
OMAiWESQGRT.
OrthoDBiEOG79GT5W.
PhylomeDBiQ969J2.
TreeFamiTF350830.

Enzyme and pathway databases

ReactomeiR-HSA-212436. Generic Transcription Pathway.

Miscellaneous databases

GenomeRNAii387032.
NextBioi101110.
PROiQ969J2.
SOURCEiSearch...

Gene expression databases

BgeeiQ969J2.
CleanExiHS_ZKSCAN4.
GenevisibleiQ969J2. HS.

Family and domain databases

Gene3Di3.30.160.60. 7 hits.
InterProiIPR001909. KRAB.
IPR008916. Retrov_capsid_C.
IPR003309. SCAN_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF01352. KRAB. 1 hit.
PF02023. SCAN. 1 hit.
PF00096. zf-C2H2. 5 hits.
PF13912. zf-C2H2_6. 1 hit.
[Graphical view]
SMARTiSM00349. KRAB. 1 hit.
SM00431. SCAN. 1 hit.
SM00355. ZnF_C2H2. 7 hits.
[Graphical view]
SUPFAMiSSF109640. SSF109640. 1 hit.
SSF47353. SSF47353. 1 hit.
PROSITEiPS50805. KRAB. 1 hit.
PS50804. SCAN_BOX. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Fetal heart.
  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].
    Tissue: Trachea.
  3. "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].
  4. 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].
    Tissue: B-cell.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26 AND LYS-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZKSC4_HUMAN
AccessioniPrimary (citable) accession number: Q969J2
Secondary accession number(s): B2RE32, Q5U7L4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 134 of the entry and version 1 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 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.