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Q8TDI0 (CHD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromodomain-helicase-DNA-binding protein 5

Short name=CHD-5
EC=3.6.4.12
Alternative name(s):
ATP-dependent helicase CHD5
Gene names
Name:CHD5
Synonyms:KIAA0444
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1954 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3. Plays a role in the development of the nervous system by activating the expression of genes promoting neuron terminal differentiation. In parallel, it may also positively regulate the trimethylation of histone H3 at 'Lys-27' thereby specifically repressing genes that promote the differentiation into non-neuronal cell lineages. Tumor suppressor, it regulates the expression of genes involved in cell proliferation and differentiation. Downstream activated genes may include CDKN2A that positively regulates the p53/TP53 pathway, which in turn, prevents cell proliferation. In spermatogenesis, it probably regulates histone hyperacetylation and the replacement of histones by transition proteins in chromatin, a crucial step in the condensation of spermatid chromatin and the production of functional spermatozoa. Ref.7

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

May be part of a nucleosome remodeling and histone deacetylation, NuRD-like, complex composed at least of GATAD2B, HDAC1, HDAC2 and MTA3 By similarity.

Subcellular location

Nucleus. Note: Associates with heterochromatin By similarity. Ref.6 Ref.7

Tissue specificity

Preferentially expressed in total brain, fetal brain, and cerebellum. It is also moderately expressed in the adrenal gland and detected in testis. Ref.1 Ref.6

Domain

The PHD domains mediate specific binding to histone H3 unmethylated at 'Lys-4' and may preferentially recruit the protein to transcriptionally inactive genes By similarity. Ref.7

The chromo domains mediate specific binding to histone H3 trimethylated at 'Lys-27' (H3K27me3) and may be required in neuron differentiation for proper gene regulation (Ref.7). Ref.7

Involvement in disease

Defects in CHD5 may be a cause of the development of cancers from epithelial, neural and hematopoietic origin. CHD5 is one of the missing genes in the del(1p36), a deletion which is extremely common in this type of cancers. A decrease of its expression, results in increased susceptibility of cells to Ras-mediated transformation in vitro and in vivo (Ref.5). Ref.5

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 2 chromo domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 2 PHD-type zinc fingers.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
Spermatogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseTumor suppressor
   DomainRepeat
Zinc-finger
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionChromatin regulator
Helicase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcerebral cortex neuron differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3-K27 trimethylation

Inferred from mutant phenotype Ref.7. Source: UniProtKB

histone H4 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of signal transduction by p53 class mediator

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription involved in cell fate commitment

Inferred from mutant phenotype Ref.7. Source: UniProtKB

spermatogenesis, exchange of chromosomal proteins

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuRD complex

Inferred from sequence or structural similarity. Source: UniProtKB

heterochromatin

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

methylated histone binding

Inferred from direct assay Ref.7. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19541954Chromodomain-helicase-DNA-binding protein 5
PRO_0000080230

Regions

Domain497 – 55458Chromo 1
Domain592 – 65362Chromo 2
Domain712 – 896185Helicase ATP-binding
Domain1028 – 1193166Helicase C-terminal
Zinc finger343 – 39048PHD-type 1
Zinc finger416 – 46348PHD-type 2
Nucleotide binding725 – 7328ATP Potential UniProtKB Q14839
Region343 – 653311Histone-binding
Motif847 – 8504DEAH box
Compositional bias49 – 11668Lys-rich

Natural variations

Natural variant451V → M in a breast cancer sample; somatic mutation. Ref.8
VAR_035475
Natural variant1191D → N in a breast cancer sample; somatic mutation. Ref.8
VAR_035476
Natural variant6671R → G in a breast cancer sample; somatic mutation. Ref.8
VAR_035477
Natural variant12531S → I.
Corresponds to variant rs6657997 [ dbSNP | Ensembl ].
VAR_048729
Natural variant15391S → P. Ref.3 Ref.4
Corresponds to variant rs2843493 [ dbSNP | Ensembl ].
VAR_048730

Experimental info

Mutagenesis5181L → A: Reduced affinity for trimethylated histone H3K27me3. Ref.7
Mutagenesis6191Y → E: Reduced affinity for trimethylated histone H3K27me3. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q8TDI0 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: E333062B5B55E71F

FASTA1,954223,050
        10         20         30         40         50         60 
MRGPVGTEEE LPRLFAEEME NEDEMSEEED GGLEAFDDFF PVEPVSLPKK KKPKKLKENK 

        70         80         90        100        110        120 
CKGKRKKKEG SNDELSENEE DLEEKSESEG SDYSPNKKKK KKLKDKKEKK AKRKKKDEDE 

       130        140        150        160        170        180 
DDNDDGCLKE PKSSGQLMAE WGLDDVDYLF SEEDYHTLTN YKAFSQFLRP LIAKKNPKIP 

       190        200        210        220        230        240 
MSKMMTVLGA KWREFSANNP FKGSSAAAAA AAVAAAVETV TISPPLAVSP PQVPQPVPIR 

       250        260        270        280        290        300 
KAKTKEGKGP GVRKKIKGSK DGKKKGKGKK TAGLKFRFGG ISNKRKKGSS SEEDEREESD 

       310        320        330        340        350        360 
FDSASIHSAS VRSECSAALG KKSKRRRKKK RIDDGDGYET DHQDYCEVCQ QGGEIILCDT 

       370        380        390        400        410        420 
CPRAYHLVCL DPELEKAPEG KWSCPHCEKE GIQWEPKDDD DEEEEGGCEE EEDDHMEFCR 

       430        440        450        460        470        480 
VCKDGGELLC CDACPSSYHL HCLNPPLPEI PNGEWLCPRC TCPPLKGKVQ RILHWRWTEP 

       490        500        510        520        530        540 
PAPFMVGLPG PDVEPSLPPP KPLEGIPERE FFVKWAGLSY WHCSWVKELQ LELYHTVMYR 

       550        560        570        580        590        600 
NYQRKNDMDE PPPFDYGSGD EDGKSEKRKN KDPLYAKMEE RFYRYGIKPE WMMIHRILNH 

       610        620        630        640        650        660 
SFDKKGDVHY LIKWKDLPYD QCTWEIDDID IPYYDNLKQA YWGHRELMLG EDTRLPKRLL 

       670        680        690        700        710        720 
KKGKKLRDDK QEKPPDTPIV DPTVKFDKQP WYIDSTGGTL HPYQLEGLNW LRFSWAQGTD 

       730        740        750        760        770        780 
TILADEMGLG KTVQTIVFLY SLYKEGHSKG PYLVSAPLST IINWEREFEM WAPDFYVVTY 

       790        800        810        820        830        840 
TGDKESRSVI RENEFSFEDN AIRSGKKVFR MKKEVQIKFH VLLTSYELIT IDQAILGSIE 

       850        860        870        880        890        900 
WACLVVDEAH RLKNNQSKFF RVLNSYKIDY KLLLTGTPLQ NNLEELFHLL NFLTPERFNN 

       910        920        930        940        950        960 
LEGFLEEFAD ISKEDQIKKL HDLLGPHMLR RLKADVFKNM PAKTELIVRV ELSQMQKKYY 

       970        980        990       1000       1010       1020 
KFILTRNFEA LNSKGGGNQV SLLNIMMDLK KCCNHPYLFP VAAVEAPVLP NGSYDGSSLV 

      1030       1040       1050       1060       1070       1080 
KSSGKLMLLQ KMLKKLRDEG HRVLIFSQMT KMLDLLEDFL EYEGYKYERI DGGITGGLRQ 

      1090       1100       1110       1120       1130       1140 
EAIDRFNAPG AQQFCFLLST RAGGLGINLA TADTVIIYDS DWNPHNDIQA FSRAHRIGQN 

      1150       1160       1170       1180       1190       1200 
KKVMIYRFVT RASVEERITQ VAKRKMMLTH LVVRPGLGSK SGSMTKQELD DILKFGTEEL 

      1210       1220       1230       1240       1250       1260 
FKDDVEGMMS QGQRPVTPIP DVQSSKGGNL AASAKKKHGS TPPGDNKDVE DSSVIHYDDA 

      1270       1280       1290       1300       1310       1320 
AISKLLDRNQ DATDDTELQN MNEYLSSFKV AQYVVREEDG VEEVEREIIK QEENVDPDYW 

      1330       1340       1350       1360       1370       1380 
EKLLRHHYEQ QQEDLARNLG KGKRIRKQVN YNDASQEDQE WQDELSDNQS EYSIGSEDED 

      1390       1400       1410       1420       1430       1440 
EDFEERPEGQ SGRRQSRRQL KSDRDKPLPP LLARVGGNIE VLGFNARQRK AFLNAIMRWG 

      1450       1460       1470       1480       1490       1500 
MPPQDAFNSH WLVRDLRGKS EKEFRAYVSL FMRHLCEPGA DGAETFADGV PREGLSRQHV 

      1510       1520       1530       1540       1550       1560 
LTRIGVMSLV RKKVQEFEHV NGKYSTPDLI PEGPEGKKSG EVISSDPNTP VPASPAHLLP 

      1570       1580       1590       1600       1610       1620 
APLGLPDKME AQLGYMDEKD PGAQKPRQPL EVQALPAALD RVESEDKHES PASKERAREE 

      1630       1640       1650       1660       1670       1680 
RPEETEKAPP SPEQLPREEV LPEKEKILDK LELSLIHSRG DSSELRPDDT KAEEKEPIET 

      1690       1700       1710       1720       1730       1740 
QQNGDKEEDD EGKKEDKKGK FKFMFNIADG GFTELHTLWQ NEERAAVSSG KIYDIWHRRH 

      1750       1760       1770       1780       1790       1800 
DYWLLAGIVT HGYARWQDIQ NDPRYMILNE PFKSEVHKGN YLEMKNKFLA RRFKLLEQAL 

      1810       1820       1830       1840       1850       1860 
VIEEQLRRAA YLNMTQDPNH PAMALNARLA EVECLAESHQ HLSKESLAGN KPANAVLHKV 

      1870       1880       1890       1900       1910       1920 
LNQLEELLSD MKADVTRLPS MLSRIPPVAA RLQMSERSIL SRLTNRAGDP TIQQGAFGSS 

      1930       1940       1950 
QMYSNNFGPN FRGPGPGGIV NYNQMPLGPY VTDI 

« Hide

References

« Hide 'large scale' references
[1]"CHD5, a new member of the chromodomain gene family, is preferentially expressed in the nervous system."
Thompson P.M., Gotoh T., Kok M., White P.S., Brodeur G.M.
Oncogene 22:1002-1011(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 567-1954, VARIANT PRO-1539.
Tissue: Testis.
[4]"Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 977-1954, VARIANT PRO-1539.
Tissue: Brain.
[5]"CHD5 is a tumor suppressor at human 1p36."
Bagchi A., Papazoglu C., Wu Y., Capurso D., Brodt M., Francis D., Bredel M., Vogel H., Mills A.A.
Cell 128:459-475(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[6]"CHD5, a brain-specific paralog of Mi2 chromatin remodeling enzymes, regulates expression of neuronal genes."
Potts R.C., Zhang P., Wurster A.L., Precht P., Mughal M.R., Wood W.H., Zhang Y., Becker K.G., Mattson M.P., Pazin M.J.
PLoS ONE 6:E24515-E24515(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]"CHD5 is required for neurogenesis and has a dual role in facilitating gene expression and polycomb gene repression."
Egan C.M., Nyman U., Skotte J., Streubel G., Turner S., O'Connell D.J., Rraklli V., Dolan M.J., Chadderton N., Hansen K., Farrar G.J., Helin K., Holmberg J., Bracken A.P.
Dev. Cell 26:223-236(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TRANSCRIPTIONAL REGULATOR, FUNCTION IN NEURON DIFFERENTIATION, INTERACTION WITH HISTONE H3K27ME3, SUBCELLULAR LOCATION, CHROMO DOMAINS, MUTAGENESIS OF LEU-518 AND TYR-619.
[8]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-45; ASN-119 AND GLY-667.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF425231 mRNA. Translation: AAL98962.1.
AL031847, AL035406 Genomic DNA. Translation: CAI19450.1.
AL035406, AL031847 Genomic DNA. Translation: CAI19891.1.
AL117491 mRNA. Translation: CAB55959.1.
AB007913 mRNA. Translation: BAA32289.1.
CCDSCCDS57.1.
PIRT17269.
RefSeqNP_056372.1. NM_015557.2.
UniGeneHs.522898.

3D structure databases

ProteinModelPortalQ8TDI0.
SMRQ8TDI0. Positions 315-468, 588-644, 943-1195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117504. 1 interaction.
IntActQ8TDI0. 1 interaction.
STRING9606.ENSP00000262450.

PTM databases

PhosphoSiteQ8TDI0.

Polymorphism databases

DMDM51701343.

Proteomic databases

MaxQBQ8TDI0.
PaxDbQ8TDI0.
PRIDEQ8TDI0.

Protocols and materials databases

DNASU26038.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262450; ENSP00000262450; ENSG00000116254.
GeneID26038.
KEGGhsa:26038.
UCSCuc001amb.2. human.

Organism-specific databases

CTD26038.
GeneCardsGC01M006161.
HGNCHGNC:16816. CHD5.
HPAHPA015809.
MIM610771. gene.
neXtProtNX_Q8TDI0.
PharmGKBPA134969178.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000231124.
HOVERGENHBG005326.
InParanoidQ8TDI0.
KOK14435.
OMAKRIDDGD.
OrthoDBEOG7C8GG7.
PhylomeDBQ8TDI0.
TreeFamTF106448.

Gene expression databases

ArrayExpressQ8TDI0.
BgeeQ8TDI0.
CleanExHS_CHD5.
GenevestigatorQ8TDI0.

Family and domain databases

Gene3D3.30.40.10. 2 hits.
3.40.50.300. 2 hits.
InterProIPR028727. CHD5.
IPR012957. CHD_C2.
IPR012958. CHD_N.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR009462. DUF1086.
IPR009463. DUF1087.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR10799:SF583. PTHR10799:SF583. 1 hit.
PfamPF08074. CHDCT2. 1 hit.
PF08073. CHDNT. 1 hit.
PF00385. Chromo. 2 hits.
PF06461. DUF1086. 1 hit.
PF06465. DUF1087. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00628. PHD. 2 hits.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00249. PHD. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 3 hits.
SSF57903. SSF57903. 1 hit.
PROSITEPS50013. CHROMO_2. 2 hits.
PS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHD5. human.
GeneWikiCHD5.
GenomeRNAi26038.
NextBio47863.
PROQ8TDI0.
SOURCESearch...

Entry information

Entry nameCHD5_HUMAN
AccessionPrimary (citable) accession number: Q8TDI0
Secondary accession number(s): O75032 expand/collapse secondary AC list , Q5TG89, Q7LGH2, Q9UFR9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM