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Protein

TOX high mobility group box family member 4

Gene

TOX4

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

Functioni

Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi223 – 29169HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: GO_Central
  2. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. chromatin remodeling Source: GO_Central
  2. regulation of transcription, DNA-templated Source: GO_Central
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
TOX high mobility group box family member 4
Alternative name(s):
Epidermal Langerhans cell protein LCP1
Gene namesi
Name:TOX4
Synonyms:C14orf92, KIAA0737
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20161. TOX4.

Subcellular locationi

  1. Nucleus 1 Publication

  2. Note: Associated with chromatin.

GO - Cellular componenti

  1. chromatin Source: UniProtKB
  2. nucleoplasm Source: HPA
  3. PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162406753.

Polymorphism and mutation databases

BioMutaiTOX4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 621621TOX high mobility group box family member 4PRO_0000048568Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei178 – 1781Phosphoserine2 Publications
Modified residuei182 – 1821Phosphoserine2 Publications
Modified residuei313 – 3131Phosphothreonine1 Publication
Modified residuei315 – 3151Phosphoserine1 Publication
Modified residuei533 – 5331Phosphoserine1 Publication
Modified residuei550 – 5501Phosphoserine1 Publication
Modified residuei552 – 5521Phosphoserine1 Publication
Modified residuei560 – 5601Phosphoserine1 Publication
Modified residuei562 – 5621Phosphoserine1 Publication
Modified residuei567 – 5671Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO94842.
PaxDbiO94842.
PeptideAtlasiO94842.
PRIDEiO94842.

PTM databases

PhosphoSiteiO94842.

Expressioni

Gene expression databases

BgeeiO94842.
CleanExiHS_TOX4.
ExpressionAtlasiO94842. baseline and differential.
GenevestigatoriO94842.

Organism-specific databases

HPAiHPA017880.
HPA027551.

Interactioni

Subunit structurei

Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82 and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R10/PNUTS.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BANPQ8N9N53EBI-948613,EBI-744695
FNDC3BQ53EP0-33EBI-948613,EBI-10242151
GEMIN6Q8WXD53EBI-948613,EBI-752301
MYL7Q014493EBI-948613,EBI-10222416
TBX6O959473EBI-948613,EBI-2824328
ZMYND19Q96E353EBI-948613,EBI-746595

Protein-protein interaction databases

BioGridi115209. 41 interactions.
IntActiO94842. 25 interactions.
MINTiMINT-1193640.
STRINGi9606.ENSP00000262709.

Structurei

3D structure databases

ProteinModelPortaliO94842.
SMRiO94842. Positions 219-291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi213 – 2186Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi401 – 534134Gln/Pro-richAdd
BLAST
Compositional biasi426 – 4349Poly-Ala

Sequence similaritiesi

Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG284736.
GeneTreeiENSGT00560000076898.
HOGENOMiHOG000230949.
HOVERGENiHBG051013.
InParanoidiO94842.
OMAiPPTLKMQ.
OrthoDBiEOG7R834J.
PhylomeDBiO94842.
TreeFamiTF106481.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O94842-1) [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
MEFPGGNDNY LTITGPSHPF LSGAETFHTP SLGDEEFEIP PISLDSDPSL
60 70 80 90 100
AVSDVVGHFD DLADPSSSQD GSFSAQYGVQ TLDMPVGMTH GLMEQGGGLL
110 120 130 140 150
SGGLTMDLDH SIGTQYSANP PVTIDVPMTD MTSGLMGHSQ LTTIDQSELS
160 170 180 190 200
SQLGLSLGGG TILPPAQSPE DRLSTTPSPT SSLHEDGVED FRRQLPSQKT
210 220 230 240 250
VVVEAGKKQK APKKRKKKDP NEPQKPVSAY ALFFRDTQAA IKGQNPNATF
260 270 280 290 300
GEVSKIVASM WDSLGEEQKQ VYKRKTEAAK KEYLKALAAY KDNQECQATV
310 320 330 340 350
ETVELDPAPP SQTPSPPPMA TVDPASPAPA SIEPPALSPS IVVNSTLSSY
360 370 380 390 400
VANQASSGAG GQPNITKLII TKQMLPSSIT MSQGGMVTVI PATVVTSRGL
410 420 430 440 450
QLGQTSTATI QPSQQAQIVT RSVLQAAAAA AAAASMQLPP PRLQPPPLQQ
460 470 480 490 500
MPQPPTQQQV TILQQPPPLQ AMQQPPPQKV RINLQQQPPP LQIKSVPLPT
510 520 530 540 550
LKMQTTLVPP TVESSPERPM NNSPEAHTVE APSPETICEM ITDVVPEVES
560 570 580 590 600
PSQMDVELVS GSPVALSPQP RCVRSGCENP PIVSKDWDNE YCSNECVVKH
610 620
CRDVFLAWVA SRNSNTVVFV K
Length:621
Mass (Da):66,195
Last modified:May 1, 1999 - v1
Checksum:iD5EEAE6FA4756CB1
GO
Isoform 2 (identifier: O94842-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MEFPGGNDNYLTITGPSHPFLSGA → M

Note: No experimental confirmation available.

Show »
Length:598
Mass (Da):63,821
Checksum:iF157F071E5DEF8ED
GO
Isoform 3 (identifier: O94842-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     82-107: Missing.

Note: No experimental confirmation available.

Show »
Length:595
Mass (Da):63,595
Checksum:i4DF14D609C22E234
GO

Sequence cautioni

The sequence BAA34457.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711V → I in BAG61682 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424MEFPG…FLSGA → M in isoform 2. 1 PublicationVSP_053873Add
BLAST
Alternative sequencei82 – 10726Missing in isoform 3. 1 PublicationVSP_055512Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018280 mRNA. Translation: BAA34457.2. Different initiation.
AK298555 mRNA. Translation: BAG60750.1.
AK299807 mRNA. Translation: BAG61682.1.
BC013689 mRNA. Translation: AAH13689.1.
CCDSiCCDS32043.1. [O94842-1]
RefSeqiNP_055643.1. NM_014828.3. [O94842-1]
UniGeneiHs.555910.

Genome annotation databases

EnsembliENST00000448790; ENSP00000393080; ENSG00000092203. [O94842-1]
ENST00000613569; ENSP00000477868; ENSG00000092203. [O94842-1]
GeneIDi9878.
KEGGihsa:9878.
UCSCiuc001way.3. human. [O94842-1]
uc010tlu.2. human.

Polymorphism and mutation databases

BioMutaiTOX4.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018280 mRNA. Translation: BAA34457.2. Different initiation.
AK298555 mRNA. Translation: BAG60750.1.
AK299807 mRNA. Translation: BAG61682.1.
BC013689 mRNA. Translation: AAH13689.1.
CCDSiCCDS32043.1. [O94842-1]
RefSeqiNP_055643.1. NM_014828.3. [O94842-1]
UniGeneiHs.555910.

3D structure databases

ProteinModelPortaliO94842.
SMRiO94842. Positions 219-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115209. 41 interactions.
IntActiO94842. 25 interactions.
MINTiMINT-1193640.
STRINGi9606.ENSP00000262709.

PTM databases

PhosphoSiteiO94842.

Polymorphism and mutation databases

BioMutaiTOX4.

Proteomic databases

MaxQBiO94842.
PaxDbiO94842.
PeptideAtlasiO94842.
PRIDEiO94842.

Protocols and materials databases

DNASUi9878.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000448790; ENSP00000393080; ENSG00000092203. [O94842-1]
ENST00000613569; ENSP00000477868; ENSG00000092203. [O94842-1]
GeneIDi9878.
KEGGihsa:9878.
UCSCiuc001way.3. human. [O94842-1]
uc010tlu.2. human.

Organism-specific databases

CTDi9878.
GeneCardsiGC14P021944.
HGNCiHGNC:20161. TOX4.
HPAiHPA017880.
HPA027551.
MIMi614032. gene.
neXtProtiNX_O94842.
PharmGKBiPA162406753.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG284736.
GeneTreeiENSGT00560000076898.
HOGENOMiHOG000230949.
HOVERGENiHBG051013.
InParanoidiO94842.
OMAiPPTLKMQ.
OrthoDBiEOG7R834J.
PhylomeDBiO94842.
TreeFamiTF106481.

Miscellaneous databases

ChiTaRSiTOX4. human.
GeneWikiiTOX4.
GenomeRNAii9878.
NextBioi35474003.
PROiO94842.
SOURCEiSearch...

Gene expression databases

BgeeiO94842.
CleanExiHS_TOX4.
ExpressionAtlasiO94842. baseline and differential.
GenevestigatoriO94842.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
[Graphical view]
PfamiPF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  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] (ISOFORMS 2 AND 3).
    Tissue: Brain.
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [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] (ISOFORM 1).
    Tissue: Lung.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Identification and characterization of a novel human PP1 phosphatase complex."
    Lee J.H., You J., Dobrota E., Skalnik D.G.
    J. Biol. Chem. 285:24466-24476(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP1R10/PNUTS.
  8. "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 THR-313 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-182; SER-533; SER-550; SER-552; SER-560; SER-562 AND SER-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTOX4_HUMAN
AccessioniPrimary (citable) accession number: O94842
Secondary accession number(s): B4DPY8, B4DSM0, E7EV69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: May 1, 1999
Last modified: April 29, 2015
This is version 123 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.