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Protein

HMG domain-containing protein 4

Gene

HMGXB4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Negatively regulates Wnt/beta-catenin signaling during development.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi407 – 47569HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
HMG domain-containing protein 4
Alternative name(s):
HMG box-containing protein 4
High mobility group protein 2-like 1
Protein HMGBCG
Gene namesi
Name:HMGXB4
Synonyms:HMG2L1, HMGBCG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:5003. HMGXB4.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • NURF complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164720673.

Polymorphism and mutation databases

BioMutaiHMGXB4.
DMDMi61252700.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 601601HMG domain-containing protein 4PRO_0000048542Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei197 – 1971PhosphoserineCombined sources
Modified residuei497 – 4971PhosphoserineCombined sources
Modified residuei502 – 5021PhosphoserineCombined sources
Modified residuei512 – 5121PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UGU5.
MaxQBiQ9UGU5.
PaxDbiQ9UGU5.
PRIDEiQ9UGU5.

PTM databases

iPTMnetiQ9UGU5.
PhosphoSiteiQ9UGU5.

Expressioni

Gene expression databases

BgeeiQ9UGU5.
ExpressionAtlasiQ9UGU5. baseline and differential.
GenevisibleiQ9UGU5. HS.

Organism-specific databases

HPAiHPA000725.

Interactioni

Protein-protein interaction databases

BioGridi115353. 33 interactions.
DIPiDIP-60550N.
IntActiQ9UGU5. 23 interactions.
MINTiMINT-6783307.
STRINGi9606.ENSP00000216106.

Structurei

3D structure databases

ProteinModelPortaliQ9UGU5.
SMRiQ9UGU5. Positions 378-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IE16. Eukaryota.
ENOG41101FA. LUCA.
GeneTreeiENSGT00390000012436.
HOGENOMiHOG000112916.
InParanoidiQ9UGU5.
KOiK11298.
OMAiDHSFEDI.
OrthoDBiEOG789CC6.
PhylomeDBiQ9UGU5.
TreeFamiTF106404.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR025228. DUF4171.
IPR009071. HMG_box_dom.
[Graphical view]
PfamiPF13775. DUF4171. 1 hit.
PF00505. HMG_box. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UGU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYDDSVKKE DCFDGDHTFE DIGLAAGRSQ REKKRSYKDF LREEEEIAAQ
60 70 80 90 100
VRNSSKKKLK DSELYFLGTD THKKKRKHSS DDYYYGDISS LESSQKKKKK
110 120 130 140 150
SSPQSTDTAM DLLKAITSPL AAGSKPSKKT GEKSSGSSSH SESKKEHHRK
160 170 180 190 200
KVSGSSGELP LEDGGSHKSK KMKPLYVNTE TLTLREPDGL KMKLILSPKE
210 220 230 240 250
KGSSSVDEES FQYPSQQATV KKSSKKSARD EQGALLLGHE LQSFLKTARK
260 270 280 290 300
KHKSSSDAHS SPGPEGCGSD ASQFAESHSA NLDLSGLEPI LVESDSSSGG
310 320 330 340 350
ELEAGELVID DSYREIKKKK KSKKSKKKKD KEKHKEKRHS KSKRSLGLSA
360 370 380 390 400
VPVGEVTVTS GPPPSIPYAG AAAPPLPLPG LHTDGHSEKK KKKEEKDKER
410 420 430 440 450
ERGEKPKKKN MSAYQVFCKE YRVTIVADHP GIDFGELSKK LAEVWKQLPE
460 470 480 490 500
KDKLIWKQKA QYLQHKQNKA EATTVKRKAS SSEGSMKVKA SSVGVLSPQK
510 520 530 540 550
KSPPTTMLLP ASPAKAPETE PIDVAAHLQL LGESLSLIGH RLQETEGMVA
560 570 580 590 600
VSGSLSVLLD SIICALGPLA CLTTQLPELN GCPKQVLSNT LDNIAYIMPG

L
Length:601
Mass (Da):65,712
Last modified:March 15, 2005 - v2
Checksum:i819527F6081FBD86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011K → R in CAA08992 (PubMed:10329004).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti165 – 1651G → V.
Corresponds to variant rs1053593 [ dbSNP | Ensembl ].
VAR_049559

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL079310 mRNA. Translation: CAB45240.1. Sequence problems.
CR456504 mRNA. Translation: CAG30390.1.
AL008635 Genomic DNA. Translation: CAI21632.1.
AJ010070 mRNA. Translation: CAA08992.1.
AJ010069 mRNA. Translation: CAA08991.1.
CCDSiCCDS33641.1.
RefSeqiNP_001003681.1. NM_001003681.2.
XP_006724165.1. XM_006724102.1.
XP_011528119.1. XM_011529817.1.
UniGeneiHs.588815.

Genome annotation databases

EnsembliENST00000216106; ENSP00000216106; ENSG00000100281.
GeneIDi10042.
KEGGihsa:10042.
UCSCiuc003anl.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL079310 mRNA. Translation: CAB45240.1. Sequence problems.
CR456504 mRNA. Translation: CAG30390.1.
AL008635 Genomic DNA. Translation: CAI21632.1.
AJ010070 mRNA. Translation: CAA08992.1.
AJ010069 mRNA. Translation: CAA08991.1.
CCDSiCCDS33641.1.
RefSeqiNP_001003681.1. NM_001003681.2.
XP_006724165.1. XM_006724102.1.
XP_011528119.1. XM_011529817.1.
UniGeneiHs.588815.

3D structure databases

ProteinModelPortaliQ9UGU5.
SMRiQ9UGU5. Positions 378-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115353. 33 interactions.
DIPiDIP-60550N.
IntActiQ9UGU5. 23 interactions.
MINTiMINT-6783307.
STRINGi9606.ENSP00000216106.

PTM databases

iPTMnetiQ9UGU5.
PhosphoSiteiQ9UGU5.

Polymorphism and mutation databases

BioMutaiHMGXB4.
DMDMi61252700.

Proteomic databases

EPDiQ9UGU5.
MaxQBiQ9UGU5.
PaxDbiQ9UGU5.
PRIDEiQ9UGU5.

Protocols and materials databases

DNASUi10042.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216106; ENSP00000216106; ENSG00000100281.
GeneIDi10042.
KEGGihsa:10042.
UCSCiuc003anl.4. human.

Organism-specific databases

CTDi10042.
GeneCardsiHMGXB4.
HGNCiHGNC:5003. HMGXB4.
HPAiHPA000725.
MIMi604702. gene.
neXtProtiNX_Q9UGU5.
PharmGKBiPA164720673.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE16. Eukaryota.
ENOG41101FA. LUCA.
GeneTreeiENSGT00390000012436.
HOGENOMiHOG000112916.
InParanoidiQ9UGU5.
KOiK11298.
OMAiDHSFEDI.
OrthoDBiEOG789CC6.
PhylomeDBiQ9UGU5.
TreeFamiTF106404.

Miscellaneous databases

ChiTaRSiHMGXB4. human.
GenomeRNAii10042.
PROiQ9UGU5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UGU5.
ExpressionAtlasiQ9UGU5. baseline and differential.
GenevisibleiQ9UGU5. HS.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR025228. DUF4171.
IPR009071. HMG_box_dom.
[Graphical view]
PfamiPF13775. DUF4171. 1 hit.
PF00505. 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. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
    Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
    Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1 and encode proteins similar to the endosomal proteins HGS and STAM."
    Seroussi E., Kedra D., Kost-Alimova M., Sandberg-Nordqvist A.-C., Fransson I., Jacobs J.F.M., Fu Y., Pan H.-Q., Roe B.A., Imreh S., Dumanski J.P.
    Genomics 57:380-388(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-390 AND 406-601.
  5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "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-502 AND SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-497; SER-502 AND SER-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHMGX4_HUMAN
AccessioniPrimary (citable) accession number: Q9UGU5
Secondary accession number(s): O75672, O75673, Q9UMT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: March 15, 2005
Last modified: June 8, 2016
This is version 132 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 22
    Human chromosome 22: 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.