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O43865 (SAHH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative adenosylhomocysteinase 2

Short name=AdoHcyase 2
EC=3.3.1.1
Alternative name(s):
DC-expressed AHCY-like molecule
S-adenosyl-L-homocysteine hydrolase 2
S-adenosylhomocysteine hydrolase-like protein 1
Gene names
Name:AHCYL1
Synonyms:DCAL, XPVKONA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine.

Cofactor

Binds 1 NAD per subunit. Ref.15

Pathway

Amino-acid biosynthesis; L-homocysteine biosynthesis; L-homocysteine from S-adenosyl-L-homocysteine: step 1/1.

Subunit structure

Interacts with ITPR1. Competes with IP3 for interaction with ITPR1 and attenuates IP3-induced Ca2+ release through the ITPR1 from the non-mitochondrial intracellular stores By similarity.

Subcellular location

Endoplasmic reticulum By similarity.

Tissue specificity

Expressed in dendritic cells. Ref.1

Developmental stage

Expression increases markedly during activation of blood and skin DC (Langerhans cells), but is diminished in terminally differentiated tonsil DC. Ref.1

Domain

The PEST region is essential for the interaction with ITPR1. The PDZ-binding region is required for maximal interaction with ITPR1 and is also responsible for the IP3-insensitive interaction with ITPR1 By similarity.

Sequence similarities

Belongs to the adenosylhomocysteinase family.

Sequence caution

The sequence AAC01960.1 differs from that shown. Reason: Erroneous initiation.

The sequence BI460083 differs from that shown. Reason: Frameshift at several positions.

The sequence CAB43223.2 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

tatP046085EBI-2371423,EBI-6164389From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43865-1)

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: O43865-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.
Note: Derived from EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 530529Putative adenosylhomocysteinase 2
PRO_0000116908

Regions

Nucleotide binding318 – 3225NAD
Nucleotide binding397 – 3993NAD
Region65 – 9228PEST By similarity
Region281 – 448168NAD binding By similarity
Region520 – 53011PDZ-binding By similarity

Sites

Binding site1551Substrate By similarity
Binding site2291Substrate By similarity
Binding site2541Substrate By similarity
Binding site2841Substrate By similarity
Binding site2881Substrate By similarity
Binding site3411NAD
Binding site3761NAD

Amino acid modifications

Modified residue21N-acetylserine Ref.13
Modified residue21Phosphoserine Ref.13
Modified residue401N6-acetyllysine By similarity
Modified residue3911Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 4747Missing in isoform 2.
VSP_021751

Experimental info

Sequence conflict941K → M in T19009. Ref.9
Sequence conflict991S → F in T19009. Ref.9

Secondary structure

.............................................................................. 530
Helix Strand Turn

Details...

Sequences

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

Last modified April 4, 2006. Version 2.
Checksum: 974D23361A245D04

FASTA53058,951
        10         20         30         40         50         60 
MSMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE FTKFPTKTGR 

        70         80         90        100        110        120 
RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK GSSNFCVKNI KQAEFGRREI 

       130        140        150        160        170        180 
EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG CTHITAQTAV LIETLCALGA QCRWSACNIY 

       190        200        210        220        230        240 
STQNEVAAAL AEAGVAVFAW KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK 

       250        260        270        280        290        300 
YPNVFKKIRG IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG 

       310        320        330        340        350        360 
LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA CMDGFRVVKL 

       370        380        390        400        410        420 
NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS NTEIDVTSLR TPELTWERVR 

       430        440        450        460        470        480 
SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV PTFVLSITAT TQALALIELY NAPEGRYKQD 

       490        500        510        520        530 
VYLLPKKMDE YVASLHLPSF DAHLTELTDD QAKYLGLNKN GPFKPNYYRY 

« Hide

Isoform 2 [UniParc].

Checksum: 18DFC7E74697E1D4
Show »

FASTA48353,753

References

« Hide 'large scale' references
[1]"Identification of an S-adenosylhomocysteine hydrolase-like transcript induced during dendritic cell differentiation."
Dekker J.W., Budhia S., Angel N.Z., Cooper B.J., Clark G.J., Hart D.N., Kato M.
Immunogenetics 53:993-1001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[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. 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 2).
Tissue: Kidney and Thalamus.
[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] (ISOFORM 2).
Tissue: Brain.
[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]Mural R.J., Istrail S., Sutton 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].
[6]"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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-251 (ISOFORM 2).
Tissue: Brain, Colon, Eye, Placenta, PNS and Testis.
[7]"Complementation of chromosomal instability in the xeroderma pigmentosum variant by a gene on human chromosome 1 with homology to S-adenosyl homocysteine hydrolase."
Volpe J.P.G., McDowell M., Jostes R.F., Afzal V., Sadinski W., Trask B.J., Legerski R., Cleaver J.E.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-530 (ISOFORM 1).
Tissue: Skin.
[8]"Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis."
Imabayashi H., Mori T., Gojo S., Kiyono T., Sugiyama T., Irie R., Isogai T., Hata J., Toyama Y., Umezawa A.
Exp. Cell Res. 288:35-50(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-164 (ISOFORM 2).
Tissue: Chondrocyte.
[9]"Characterization of a large population of mRNAs from human testis."
Pawlak A., Toussaint C., Levy I., Bulle F., Poyard M., Barouki R., Guellaen G.
Genomics 26:151-158(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 48-105 (ISOFORM 2).
Tissue: Testis.
[10]"Suppression and overexpression of adenosylhomocysteine hydrolase-like protein 1 (AHCYL1) influences zebrafish embryo development: a possible role for AHCYL1 in inositol phospholipid signaling."
Cooper B.J., Key B., Carter A., Angel N.Z., Hart D.N.J., Kato M.
J. Biol. Chem. 281:22471-22484(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORM 2).
[11]"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-391, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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]"Crystal structure of human s-adenosyl homocysteine hydrolase-like 1 protein."
Structural genomics consortium (SGC)
Submitted (MAY-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 89-530 IN COMPLEX WITH NAD, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF315687 mRNA. Translation: AAL26869.1.
AL036027 mRNA. No translation available.
AK303690 mRNA. Translation: BAG64680.1.
AK316110 mRNA. Translation: BAH14481.1.
AL049954 mRNA. Translation: CAB43223.2. Different initiation.
AL772411 Genomic DNA. Translation: CAH70965.1.
AL772411 Genomic DNA. Translation: CAH70966.1.
CH471122 Genomic DNA. Translation: EAW56426.1.
BC007576 mRNA. Translation: AAH07576.3.
BC010681 mRNA. Translation: AAH10681.3.
BC016942 mRNA. Translation: AAH16942.3.
BC065254 mRNA. Translation: AAH65254.2.
BC095476 mRNA. Translation: AAH95476.2.
BC110896 mRNA. Translation: AAI10897.2.
BI460083 mRNA. No translation available.
U82761 mRNA. Translation: AAC01960.1. Different initiation.
AU279527 mRNA. No translation available.
T19009 mRNA. No translation available.
BK005418 mRNA. Translation: DAA05763.1.
BK005417 mRNA. Translation: DAA05762.1.
PIRT08681.
RefSeqNP_001229602.1. NM_001242673.1.
NP_001229603.1. NM_001242674.1.
NP_001229604.1. NM_001242675.1.
NP_001229605.1. NM_001242676.1.
NP_006612.2. NM_006621.5.
UniGeneHs.743973.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MTGX-ray2.64A/B89-530[»]
ProteinModelPortalO43865.
SMRO43865. Positions 101-530.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115987. 101 interactions.
IntActO43865. 9 interactions.
STRING9606.ENSP00000358814.

PTM databases

PhosphoSiteO43865.

Proteomic databases

PaxDbO43865.
PeptideAtlasO43865.
PRIDEO43865.

Protocols and materials databases

DNASU10768.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359172; ENSP00000352092; ENSG00000168710. [O43865-2]
ENST00000369799; ENSP00000358814; ENSG00000168710. [O43865-1]
ENST00000393614; ENSP00000377238; ENSG00000168710. [O43865-2]
GeneID10768.
KEGGhsa:10768.
UCSCuc001dyx.3. human. [O43865-1]

Organism-specific databases

CTD10768.
GeneCardsGC01P110529.
HGNCHGNC:344. AHCYL1.
HPAHPA042589.
MIM607826. gene.
neXtProtNX_O43865.
PharmGKBPA24637.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0499.
HOGENOMHOG000227986.
HOVERGENHBG005041.
KOK01251.
OMAKQIQFVE.
OrthoDBEOG76739S.
PhylomeDBO43865.
TreeFamTF300415.

Enzyme and pathway databases

UniPathwayUPA00314; UER00076.

Gene expression databases

ArrayExpressO43865.
BgeeO43865.
CleanExHS_AHCYL1.
GenevestigatorO43865.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR000043. Adenosylhomocysteinase.
IPR015878. Ado_hCys_hydrolase_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR020082. S-Ado-L-homoCys_hydrolase_CS.
[Graphical view]
PANTHERPTHR23420. PTHR23420. 1 hit.
PfamPF05221. AdoHcyase. 1 hit.
PF00670. AdoHcyase_NAD. 1 hit.
[Graphical view]
PIRSFPIRSF001109. Ad_hcy_hydrolase. 1 hit.
SMARTSM00996. AdoHcyase. 1 hit.
SM00997. AdoHcyase_NAD. 1 hit.
[Graphical view]
TIGRFAMsTIGR00936. ahcY. 1 hit.
PROSITEPS00738. ADOHCYASE_1. 1 hit.
PS00739. ADOHCYASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAHCYL1. human.
EvolutionaryTraceO43865.
GeneWikiAHCYL1.
GenomeRNAi10768.
NextBio40889.
PMAP-CutDBO43865.
PROO43865.
SOURCESearch...

Entry information

Entry nameSAHH2_HUMAN
AccessionPrimary (citable) accession number: O43865
Secondary accession number(s): B4E168 expand/collapse secondary AC list , Q2TAJ6, Q502W8, Q5VSM0, Q6P171, Q96PK4, Q9UG84
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 4, 2006
Last modified: April 16, 2014
This is version 134 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 1

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