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Q9Y2X9 (ZN281_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein 281
Alternative name(s):
GC-box-binding zinc finger protein 1
Transcription factor ZBP-99
Zinc finger DNA-binding protein 99
Gene names
Name:ZNF281
Synonyms:GZP1, ZBP99
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length895 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription repressor that plays a role in regulation of embryonic stem cells (ESCs) differentiation. Required for ESCs differentiation and acts by mediating autorepression of NANOG in ESCs: binds to the NANOG promoter and promotes association of NANOG protein to its own promoter and recruits the NuRD complex, which deacetylates histones. Not required for establishement and maintenance of ESCs By similarity. Represses the transcription of a number of genes including GAST, ODC1 and VIM. Binds to the G-rich box in the enhancer region of these genes. Ref.1 Ref.6

Subcellular location

Nucleus Ref.1.

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family.

Contains 4 C2H2-type zinc fingers.

Sequence caution

The sequence CAB70967.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processembryonic body morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of gene expression

Inferred from direct assay Ref.6. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.2. Source: UniProtKB

stem cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functioncore promoter binding

Inferred from sequence or structural similarity. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 17314511PubMed 19147588. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay Ref.2Ref.6. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.1. Source: UniProtKB

transcription corepressor activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2X9-1)

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: Q9Y2X9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     49-84: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 895895Zinc finger protein 281
PRO_0000047505

Regions

Zinc finger261 – 28323C2H2-type 1
Zinc finger289 – 31123C2H2-type 2
Zinc finger317 – 33923C2H2-type 3
Zinc finger345 – 36723C2H2-type 4; atypical
Compositional bias4 – 3734Gly-rich
Compositional bias90 – 967Poly-Pro
Compositional bias141 – 1488Poly-His

Amino acid modifications

Modified residue3951Phosphoserine Ref.7
Modified residue4841Phosphoserine Ref.9
Modified residue7851Phosphoserine Ref.7
Modified residue8071Phosphoserine Ref.7

Natural variations

Alternative sequence49 – 8436Missing in isoform 2.
VSP_054815
Natural variant5271I → T in a breast cancer sample; somatic mutation. Ref.15
VAR_035576

Experimental info

Sequence conflict631F → L in BAG51134. Ref.3
Sequence conflict2061H → Y in AAH51905. Ref.5
Sequence conflict4821F → L in BAG51134. Ref.3
Sequence conflict6351L → I in BAG51134. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 556FAAEA8D095FB7

FASTA89596,915
        10         20         30         40         50         60 
MKIGSGFLSG GGGTGSSGGS GSGGGGSGGG GGGGSSGRRA EMEPTFPQGM VMFNHRLPPV 

        70         80         90        100        110        120 
TSFTRPAGSA APPPQCVLSS STSAAPAAEP PPPPAPDMTF KKEPAASAAA FPSQRTSWGF 

       130        140        150        160        170        180 
LQSLVSIKQE KPADPEEQQS HHHHHHHHYG GLFAGAEERS PGLGGGEGGS HGVIQDLSIL 

       190        200        210        220        230        240 
HQHVQQQPAQ HHRDVLLSSS SRTDDHHGTE EPKQDTNVKK AKRPKPESQG IKAKRKPSAS 

       250        260        270        280        290        300 
SKPSLVGDGE GAILSPSQKP HICDHCSAAF RSSYHLRRHV LIHTGERPFQ CSQCSMGFIQ 

       310        320        330        340        350        360 
KYLLQRHEKI HSREKPFGCD QCSMKFIQKY HMERHKRTHS GEKPYKCDTC QQYFSRTDRL 

       370        380        390        400        410        420 
LKHRRTCGEV IVKGATSAEP GSSNHTNMGN LAVLSQGNTS SSRRKTKSKS IAIENKEQKT 

       430        440        450        460        470        480 
GKTNESQISN NINMQSYSVE MPTVSSSGGI IGTGIDELQK RVPKLIFKKG SRKNTDKNYL 

       490        500        510        520        530        540 
NFVSPLPDIV GQKSLSGKPS GSLGIVSNNS VETIGLLQST SGKQGQISSN YDDAMQFSKK 

       550        560        570        580        590        600 
RRYLPTASSN SAFSINVGHM VSQQSVIQSA GVSVLDNEAP LSLIDSSALN AEIKSCHDKS 

       610        620        630        640        650        660 
GIPDEVLQSI LDQYSNKSES QKEDPFNIAE PRVDLHTSGE HSELVQEENL SPGTQTPSND 

       670        680        690        700        710        720 
KASMLQEYSK YLQQAFEKST NASFTLGHGF QFVSLSSPLH NHTLFPEKQI YTTSPLECGF 

       730        740        750        760        770        780 
GQSVTSVLPS SLPKPPFGML FGSQPGLYLS ALDATHQQLT PSQELDDLID SQKNLETSSA 

       790        800        810        820        830        840 
FQSSSQKLTS QKEQKNLESS TGFQIPSQEL ASQIDPQKDI EPRTTYQIEN FAQAFGSQFK 

       850        860        870        880        890 
SGSRVPMTFI TNSNGEVDHR VRTSVSDFSG YTNMMSDVSE PCSTRVKTPT SQSYR 

« Hide

Isoform 2 [UniParc].

Checksum: 180A44DE154DD4FD
Show »

FASTA85993,232

References

« Hide 'large scale' references
[1]"ZBP-99 defines a conserved family of transcription factors and regulates ornithine decarboxylase gene expression."
Law D.J., Du M., Law G.L., Merchant J.L.
Biochem. Biophys. Res. Commun. 262:113-120(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
[2]"Identification of human GC-box-binding zinc finger protein, a new Krueppel-like zinc finger protein, by the yeast one-hybrid screening with a GC-rich target sequence."
Lisowsky T., Loguercio Polosa P., Sagliano A., Roberti M., Gadaleta M.N., Cantatore P.
FEBS Lett. 453:369-374(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[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. expand/collapse author list , 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).
[4]"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].
[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] (ISOFORM 1).
Tissue: Placenta and Skin.
[6]"ZBP-89 represses vimentin gene transcription by interacting with the transcriptional activator, Sp1."
Zhang X., Diab I.H., Zehner Z.E.
Nucleic Acids Res. 31:2900-2914(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-785 AND SER-807, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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: VARIANT [LARGE SCALE ANALYSIS] THR-527.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF125158 mRNA. Translation: AAD21084.1.
AJ132591 mRNA. Translation: CAB70967.1. Different initiation.
AJ132592 mRNA. Translation: CAB70968.1.
AK022916 mRNA. Translation: BAG51134.1.
AC104461 Genomic DNA. No translation available.
BC051905 mRNA. Translation: AAH51905.1.
BC060820 mRNA. Translation: AAH60820.1.
CCDSCCDS1402.1.
PIRJC7089.
RefSeqNP_001268222.1. NM_001281293.1. [Q9Y2X9-1]
NP_001268223.1. NM_001281294.1. [Q9Y2X9-2]
NP_036614.1. NM_012482.4. [Q9Y2X9-1]
UniGeneHs.59757.
Hs.703449.
Hs.735801.

3D structure databases

ProteinModelPortalQ9Y2X9.
SMRQ9Y2X9. Positions 223-366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117074. 19 interactions.
IntActQ9Y2X9. 8 interactions.
STRING9606.ENSP00000294740.

PTM databases

PhosphoSiteQ9Y2X9.

Polymorphism databases

DMDM13124664.

Proteomic databases

MaxQBQ9Y2X9.
PaxDbQ9Y2X9.
PRIDEQ9Y2X9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294740; ENSP00000294740; ENSG00000162702.
ENST00000367352; ENSP00000356321; ENSG00000162702.
ENST00000367353; ENSP00000356322; ENSG00000162702.
GeneID23528.
KEGGhsa:23528.
UCSCuc001gve.3. human. [Q9Y2X9-1]

Organism-specific databases

CTD23528.
GeneCardsGC01M200375.
HGNCHGNC:13075. ZNF281.
HPAHPA051228.
neXtProtNX_Q9Y2X9.
PharmGKBPA37651.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000293204.
HOVERGENHBG055321.
InParanoidQ9Y2X9.
OMAQKDIEPR.
OrthoDBEOG7VDXNJ.
PhylomeDBQ9Y2X9.
TreeFamTF331779.

Gene expression databases

ArrayExpressQ9Y2X9.
BgeeQ9Y2X9.
CleanExHS_ZNF281.
GenevestigatorQ9Y2X9.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiZNF281.
GenomeRNAi23528.
NextBio35462517.
PROQ9Y2X9.

Entry information

Entry nameZN281_HUMAN
AccessionPrimary (citable) accession number: Q9Y2X9
Secondary accession number(s): A6NF48 expand/collapse secondary AC list , B3KMX2, Q5RKW5, Q9NY92
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 126 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

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