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Reviewed, UniProtKB/Swiss-Prot P19419 (ELK1_HUMAN)

Last modified February 9, 2010. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ETS domain-containing protein Elk-1
Gene names
Name: ELK1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Stimulates transcription. Binds to purine-rich DNA sequences. Can form a ternary complex with the serum response factor and the ETS and SRF motifs of the fos serum response element.

Subunit structure

Interacts in its sumoylated form with PIAS2/PIASX which enhances its transcriptional activator activity. Ref.14

Subcellular location

Nucleus.

Tissue specificity

Lung and testis.

Post-translational modification

Sumoylation represses transcriptional activator activity as it results in recruitment of HDAC2 to target gene promoters which leads to decreased histone acetylation and reduced transactivator activity. It also regulates nuclear retention.

On mitogenic stimulation, phosphorylated on C-terminal serine and threonine residues by MAPK1. Ser-383 and Ser-389 are the preferred sites for MAPK1. In vitro, phosphorylation by MAPK1 potentiates ternary complex formation with the serum responses factors, SRE and SRF. Phosphorylation leads to loss of sumoylation and restores transcriptional activator activity. Ref.9 Ref.15

Sequence similarities

Belongs to the ETS family.

Contains 1 ETS DNA-binding domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAPK1P284821EBI-726632,EBI-959949
Mapk1P630851EBI-726632,EBI-397697From a different organism.
MAPK3P273611EBI-726632,EBI-73995

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P19419-1)

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: P19419-2)

Also known as: ELKV;

The sequence of this isoform differs from the canonical sequence as follows:
     91-95: VAGCS → SHCAP
     96-428: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428ETS domain-containing protein Elk-1
PRO_0000204095

Regions

DNA binding5 – 8682ETS

Amino acid modifications

Modified residue3241Phosphoserine; by MAPK1 Ref.9 Ref.15
Modified residue3361Phosphothreonine; by MAPK1 Ref.9
Modified residue3831Phosphoserine; by MAPK1 Ref.9
Modified residue3891Phosphoserine; by MAPK1 Ref.9
Modified residue4221Phosphoserine; by MAPK1 Ref.9 Ref.15
Cross-link230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.12
Cross-link249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.12 Ref.11
Cross-link254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.12

Natural variations

Alternative sequence91 – 955VAGCS → SHCAP in isoform 2.
VSP_001466
Alternative sequence96 – 428333Missing in isoform 2.
VSP_001467
Natural variant1441G → S: dbSNP rs1997639.
VAR_017108
Natural variant1831S → N: dbSNP rs1059579. Ref.1
VAR_017109

Experimental info

Mutagenesis2301K → R: 9-fold increase in transcriptional activator activity; when associated with R-249. Reduction in sumoylation. Ref.12 Ref.11
Mutagenesis2491K → R: 9-fold increase in transcriptional activator activity; when associated with R-230. Reduction in sumoylation. Ref.12 Ref.11
Mutagenesis2541K → R: Reduction in sumoylation. Ref.12
Mutagenesis3241S → A: No effect on ternary complex formation. Ref.9
Mutagenesis3361T → A: No effect on ternary complex formation. Ref.9
Mutagenesis3531T → A: No effect on ternary complex formation. Ref.9
Mutagenesis3631T → A: No effect on ternary complex formation. Ref.9
Mutagenesis3681T → A: No effect on ternary complex formation. Ref.9
Mutagenesis3831S → A: 17% reduction in ternary complex formation. Ref.9
Mutagenesis3891S → A: 34% reduction in ternary complex formation. Ref.9
Mutagenesis4171T → A: No effect on ternary complex formation. Ref.9
Mutagenesis4221S → A: Slight reduction in ternary complex formation. Ref.9

Secondary structure

.................. 428
Helix Strand Turn

Details...

Sequences

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

Last modified January 24, 2001. Version 2.
Checksum: 68F71F8ADB9D38CA

FASTA42844,888
        10         20         30         40         50         60 
MDPSVTLWQF LLQLLREQGN GHIISWTSRD GGEFKLVDAE EVARLWGLRK NKTNMNYDKL 

        70         80         90        100        110        120 
SRALRYYYDK NIIRKVSGQK FVYKFVSYPE VAGCSTEDCP PQPEVSVTST MPNVAPAAIH 

       130        140        150        160        170        180 
AAPGDTVSGK PGTPKGAGMA GPGGLARSSR NEYMRSGLYS TFTIQSLQPQ PPPHPRPAVV 

       190        200        210        220        230        240 
LPSAAPAGAA APPSGSRSTS PSPLEACLEA EEAGLPLQVI LTPPEAPNLK SEELNVEPGL 

       250        260        270        280        290        300 
GRALPPEVKV EGPKEELEVA GERGFVPETT KAEPEVPPQE GVPARLPAVV MDTAGQAGGH 

       310        320        330        340        350        360 
AASSPEISQP QKGRKPRDLE LPLSPSLLGG PGPERTPGSG SGSGLQAPGP ALTPSLLPTH 

       370        380        390        400        410        420 
TLTPVLLTPS SLPPSIHFWS TLSPIAPRSP AKLSFQFPSS GSAQVHIPSI SVDGLSTPVV 


LSPGPQKP 

« Hide

Isoform 2 (ELKV).

Checksum: 8347760EEE65634F
Show »

FASTA9511,217

References

« Hide 'large scale' references
[1]"elk, tissue-specific ets-related genes on chromosomes X and 14 near translocation breakpoints."
Rao V.N., Huebner K., Isobe M., Ar-Rushdi A., Croce C.M., Reddy E.S.P.
Science 244:66-70(1989) [PubMed: 2539641] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-183.
[2]"The human elk-1 gene family: the functional gene and two processed pseudogenes embedded in the IgH locus."
Harindranath N., Mills F.C., Mitchell M.P., Meindl A., Max E.E.
Gene 221:215-224(1998) [PubMed: 9795224] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[3]"Novel family members HuER71, ELFR, and ELKv among ETS-related genes coexpressed with EWS-FLI1 in Ewing tumor cell lines."
Aryee D.N.T., Kovar H.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
[4]"Structural organization of the human ELK1 gene and its processed pseudogene ELK2 genes."
Yamauchi T., Toko M., Suga M., Hatakeyama T., Isobe M.
DNA Res. 6:21-27(1999) [PubMed: 10231026] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Tissue: Hippocampus.
[5]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Urinary bladder.
[6]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[9]"ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation."
Gille H., Kortenjann M., Thomae O., Moomaw C., Slaughter C., Cobb M.H., Shaw P.E.
EMBO J. 14:951-962(1995) [PubMed: 7889942] [Abstract]
Cited for: PROTEIN SEQUENCE OF 318-331; 336-364 AND 380-408, PHOSPHORYLATION AT SER-324; THR-336; SER-383; SER-389 AND SER-422, MUTAGENESIS OF SER-324; THR-336; THR-353; THR-363; THR-368; SER-383; SER-389; THR-417 AND SER-422.
[10]"Elk-1 protein domains required for direct and SRF-assisted DNA-binding."
Janknecht R., Nordheim A.
Nucleic Acids Res. 20:3317-3324(1992) [PubMed: 1630903] [Abstract]
Cited for: DOMAINS.
[11]"Dynamic interplay of the SUMO and ERK pathways in regulating Elk-1 transcriptional activity."
Yang S.-H., Jaffray E., Hay R.T., Sharrocks A.D.
Mol. Cell 12:63-74(2003) [PubMed: 12887893] [Abstract]
Cited for: SUMOYLATION AT LYS-249, MUTAGENESIS OF LYS-230 AND LYS-249.
[12]"SUMOylation regulates nucleo-cytoplasmic shuttling of Elk-1."
Salinas S., Briancon-Marjollet A., Bossis G., Lopez M.-A., Piechaczyk M., Jariel-Encontre I., Debant A., Hipskind R.A.
J. Cell Biol. 165:767-773(2004) [PubMed: 15210726] [Abstract]
Cited for: SUMOYLATION AT LYS-230; LYS-249 AND LYS-254, MUTAGENESIS OF LYS-230; LYS-249 AND LYS-254.
[13]"SUMO promotes HDAC-mediated transcriptional repression."
Yang S.-H., Sharrocks A.D.
Mol. Cell 13:611-617(2004) [PubMed: 14992729] [Abstract]
Cited for: SUMOYLATION.
[14]"PIASx acts as an Elk-1 coactivator by facilitating derepression."
Yang S.-H., Sharrocks A.D.
EMBO J. 24:2161-2171(2005) [PubMed: 15920481] [Abstract]
Cited for: INTERACTION WITH PIAS2.
[15]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-422, MASS SPECTROMETRY.
Tissue: T-cell.
[16]"Structure of the elk-1-DNA complex reveals how DNA-distal residues affect ETS domain recognition of DNA."
Mo Y., Vaessen B., Johnston K., Marmorstein R.
Nat. Struct. Biol. 7:292-297(2000) [PubMed: 10742173] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-94.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25269 mRNA. Translation: AAA52384.1.
AF080616 Genomic DNA. Translation: AAC82466.1.
AF000672 mRNA. Translation: AAD00862.1.
AB016193 mRNA. Translation: BAA36616.1.
AB016194 Genomic DNA. Translation: BAA36617.1.
AK312984 mRNA. Translation: BAG35821.1.
AL009172 Genomic DNA. Translation: CAA15659.1.
CH471164 Genomic DNA. Translation: EAW59321.1.
BC056150 mRNA. Translation: AAH56150.1.
IPIIPI00220075.
IPI00301527.
PIRTVHUEK. A41354.
RefSeqNP_001107595.1.
NP_005220.2.
UniGeneHs.181128

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DUXX-ray2.10C/F1-94[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP19419. 4 interactions.
STRINGP19419.

PTM databases

PhosphoSiteP19419.

Proteomic databases

PRIDEP19419.

Genome annotation databases

EnsemblENST00000247161; ENSP00000247161; ENSG00000126767; Homo sapiens. [Genome view]
ENST00000376983; ENSP00000366182; ENSG00000126767; Homo sapiens. [Genome view]
GeneID2002.
KEGGhsa:2002.
UCSCuc004dik.2. human.

Organism-specific databases

CTD2002.
GeneCardsGC0XM047379.
HGNCHGNC:3321. ELK1.
HPACAB003808.
MIM311040. gene.
PharmGKBPA27749.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12359.
HOVERGENP19419.
PhylomeDBP19419.

Enzyme and pathway databases

Pathway_Interaction_DBangiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
bcr_5pathway. BCR signaling pathway.
cd8tcrdownstreampathway. Downstream signaling in naive CD8+ T cells.
pdgfrapathway. PDGFR-alpha signaling pathway.
tcrraspathway. Ras signaling in the CD4+ TCR pathway.
s1p_s1p2_pathway. S1P2 pathway.
met_pathway. Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
mapktrkpathway. Trk receptor signaling mediated by the MAPK pathway.
ReactomeREACT_11061. Signalling by NGF.

Gene expression databases

ArrayExpressP19419.
BgeeP19419.
CleanExHS_ELK1.
GenevestigatorP19419.
GermOnlineENSG00000126767. Homo sapiens.

Family and domain databases

InterProIPR000418. Ets.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF00178. Ets. 1 hit.
[Graphical view]
PRINTSPR00454. ETSDOMAIN.
SMARTSM00413. ETS. 1 hit.
[Graphical view]
PROSITEPS00345. ETS_DOMAIN_1. 1 hit.
PS00346. ETS_DOMAIN_2. 1 hit.
PS50061. ETS_DOMAIN_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio8101.
SOURCESearch...

Entry information

Entry nameELK1_HUMAN
AccessionPrimary (citable) accession number: P19419
Secondary accession number(s): B2R7H4 expand/collapse secondary AC list , O75606, O95058, Q969X8, Q9UJM4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 24, 2001
Last modified: February 9, 2010
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents