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P49366 (DHYS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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:
Deoxyhypusine synthase

Short name=DHS
EC=2.5.1.46
Gene names
Name:DHPS
Synonyms:DS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.

Catalytic activity

[eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine.

Cofactor

NAD.

Pathway

Protein modification; eIF5A hypusination.

Subunit structure

Homotetramer formed by a dimer of dimers. Ref.12 Ref.17 Ref.18

Sequence similarities

Belongs to the deoxyhypusine synthase family.

Sequence caution

The sequence AL520040 differs from that shown. Reason: Frameshift at positions 329, 344 and 355.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NIF3L1Q9GZT83EBI-741925,EBI-740897
NUDT18Q6ZVK83EBI-741925,EBI-740486

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P49366-1)

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 Short (identifier: P49366-2)

The sequence of this isoform differs from the canonical sequence as follows:
     262-308: Missing.
Note: Inactive.
Isoform 3 (identifier: P49366-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: MEGSLEREAP...FGRAVQQVNA → MPIIPAFWEAEAGGSREEEFETSLAN
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Deoxyhypusine synthase
PRO_0000134469

Regions

Nucleotide binding105 – 1095NAD
Nucleotide binding131 – 1333NAD
Nucleotide binding308 – 3092NAD
Nucleotide binding342 – 3432NAD
Region136 – 1372Spermidine binding Probable
Region314 – 3163Spermidine binding Probable
Region323 – 3297Spermidine binding Probable

Sites

Active site3291Nucleophile Ref.12
Binding site1371NAD
Binding site2381NAD
Binding site2431Spermidine Probable
Binding site2831NAD; via amide nitrogen
Binding site2881Spermidine Probable

Amino acid modifications

Modified residue781Phosphoserine Ref.14 Ref.15

Natural variations

Alternative sequence1 – 6868MEGSL…QQVNA → MPIIPAFWEAEAGGSREEEF ETSLAN in isoform 3.
VSP_047564
Alternative sequence262 – 30847Missing in isoform Short.
VSP_001351
Natural variant1741E → D.
Corresponds to variant rs10425108 [ dbSNP | Ensembl ].
VAR_043005

Experimental info

Mutagenesis1061N → A: Strongly reduced NAD and spermidine binding. Reduced activity. Ref.13
Mutagenesis1091S → A: Strongly reduced spermidine binding. Reduced activity. Ref.13
Mutagenesis1371E → A: Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate. Ref.13
Mutagenesis2381D → A: Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate. Ref.13
Mutagenesis2431D → A: Reduces spermidine binding by 98%. Strongly reduced formation of covalent intermediate. Ref.13
Mutagenesis2871K → A: Reduces covalent intermediate formation and deoxyhypusine synthesis by 99.5%. Retains low spermidine cleavage activity. Ref.12
Mutagenesis2881H → A: Reduces spermidine binding by 98%. Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate. Ref.13
Mutagenesis3051Y → A: Strongly reduced NAD binding. No effect on enzyme activity. Ref.13
Mutagenesis3131D → A: Strongly reduced NAD binding. Ref.13
Mutagenesis3161D → A: Reduces spermidine binding by 98%. Loss of covalent intermediate formation and deoxyhypusine synthesis. Ref.13
Mutagenesis3171S → A: Strongly reduced NAD binding. No effect on enzyme activity. Ref.13
Mutagenesis3231E → A: Reduces spermidine binding by 98%. Strongly reduced formation of covalent intermediate. Ref.13
Mutagenesis3271W → A: Reduces spermidine binding by 98%. Loss of covalent intermediate formation and deoxyhypusine synthesis. Ref.13
Mutagenesis3291K → A or R: Loss of covalent intermediate formation and deoxyhypusine synthesis. Ref.12
Mutagenesis3421D → A: Strongly reduced NAD binding. Strongly reduced activity. Ref.13
Sequence conflict111A → R in AAB02175. Ref.3
Sequence conflict111A → R in AAB02179. Ref.3
Sequence conflict13 – 142AL → R in AAB02175. Ref.3
Sequence conflict13 – 142AL → R in AAB02179. Ref.3
Sequence conflict851A → G in AAB02175. Ref.3
Sequence conflict851A → G in AAB02179. Ref.3
Sequence conflict1961T → I in AAB02175. Ref.3
Sequence conflict1961T → I in AAB02179. Ref.3
Sequence conflict1991V → A in AAB02175. Ref.3
Sequence conflict1991V → A in AAB02179. Ref.3
Sequence conflict2201V → A in AAB02175. Ref.3
Sequence conflict2201V → A in AAB02179. Ref.3
Sequence conflict2281H → K AA sequence Ref.11
Sequence conflict296 – 2972MR → SG in AAB02179. Ref.3
Sequence conflict3111E → EE in AAB02179. Ref.3

Secondary structure

........................................................ 369
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 1996. Version 1.
Checksum: 5314FED620AC9EE7

FASTA36940,971
        10         20         30         40         50         60 
MEGSLEREAP AGALAAVLKH SSTLPPESTQ VRGYDFNRGV NYRALLEAFG TTGFQATNFG 

        70         80         90        100        110        120 
RAVQQVNAMI EKKLEPLSQD EDQHADLTQS RRPLTSCTIF LGYTSNLISS GIRETIRYLV 

       130        140        150        160        170        180 
QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE FSLRGKELRE NGINRIGNLL VPNENYCKFE 

       190        200        210        220        230        240 
DWLMPILDQM VMEQNTEGVK WTPSKMIARL GKEINNPESV YYWAQKNHIP VFSPALTDGS 

       250        260        270        280        290        300 
LGDMIFFHSY KNPGLVLDIV EDLRLINTQA IFAKCTGMII LGGGVVKHHI ANANLMRNGA 

       310        320        330        340        350        360 
DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RVDAQPVKVY ADASLVFPLL VAETFAQKMD 


AFMHEKNED 

« Hide

Isoform Short [UniParc].

Checksum: 1F44CC2AB89F7A2E
Show »

FASTA32235,916
Isoform 3 [UniParc].

Checksum: 313374BBDB63A758
Show »

FASTA32736,583

References

« Hide 'large scale' references
[1]"Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins."
Joe Y.A., Wolff E.C., Park M.H.
J. Biol. Chem. 270:22386-22392(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[2]"Molecular characterization of a cDNA encoding functional human deoxyhypusine synthase and chromosomal mapping of the corresponding gene locus."
Bevec D., Kappel B., Jaksche H., Csonga R., Hauber J., Klier H., Steinkasserer A.
FEBS Lett. 378:195-198(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Blood.
[3]"Molecular cloning and functional expression of human deoxyhypusine synthase cDNA based on expressed sequence tag information."
Yan Y.P., Tao Y., Chen K.Y.
Biochem. J. 315:429-434(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
[4]"Localization and genomic structure of human deoxyhypusine synthase gene on chromosome 19p13.2-distal 19p13.1."
Mantuano E., Trettel F., Olsen A.S., Lennin G., Frontali M., Jodice C.
Gene 215:153-157(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Tissue: Brain.
[6]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Neuroblastoma.
[7]"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 LONG).
Tissue: Placenta.
[8]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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].
[10]"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 LONG).
Tissue: Brain and Lung.
[11]"Purification and characterization of human deoxyhypusine synthase from HeLa cells."
Klier H., Csonga R., Steinkasserer A., Woehl T., Lottspeich F., Eder J.
FEBS Lett. 364:207-210(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 184-189; 192-204; 206-232 AND 278-296 (ISOFORM LONG).
Tissue: Cervix carcinoma.
[12]"Enzyme-substrate intermediate at a specific lysine residue is required for deoxyhypusine synthesis. The role of Lys329 in human deoxyhypusine synthase."
Joe Y.A., Wolff E.C., Lee Y.B., Park M.H.
J. Biol. Chem. 272:32679-32685(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-287 AND LYS-329, SUBUNIT, ACTIVE SITE.
[13]"Structure-function studies of human deoxyhypusine synthase: identification of amino acid residues critical for the binding of spermidine and NAD."
Lee C.H., Um P.Y., Park M.H.
Biochem. J. 355:841-849(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-106; SER-109; GLU-137; ASP-238; ASP-243; HIS-288; TYR-305; ASP-313; ASP-316; SER-317; GLU-323; TRP-327 AND ASP-342.
[14]"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-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"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-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site."
Liao D.-I., Wolff E.C., Park M.H., Davies D.R.
Structure 6:23-32(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
[18]"A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex."
Umland T.C., Wolff E.C., Park M.H., Davies D.R.
J. Biol. Chem. 279:28697-28705(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH NAD AND COMPETITIVE INHIBITOR, MASS SPECTROMETRY, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L39068 mRNA. Translation: AAA86282.1.
U40579 mRNA. Translation: AAA96151.1.
U32178 mRNA. Translation: AAB02179.1.
U26266 mRNA. Translation: AAB02175.1.
AJ001701 expand/collapse EMBL AC list , AJ001702, AJ001703, AJ001704 Genomic DNA. Translation: CAA04940.1.
U79262 mRNA. Translation: AAB50208.1.
AL520040 mRNA. No translation available.
AK291553 mRNA. Translation: BAF84242.1.
AC010422 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84288.1.
BC000333 mRNA. Translation: AAH00333.1.
BC014016 mRNA. Translation: AAH14016.1.
PIRS68692.
RefSeqNP_001193903.1. NM_001206974.1.
NP_001921.1. NM_001930.3.
NP_037538.1. NM_013406.2.
UniGeneHs.79064.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DHSX-ray2.20A9-369[»]
1RLZX-ray2.15A1-369[»]
1ROZX-ray2.21A/B1-369[»]
1RQDX-ray3.00A/B1-369[»]
ProteinModelPortalP49366.
SMRP49366. Positions 28-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108070. 24 interactions.
IntActP49366. 7 interactions.
MINTMINT-1436761.
STRING9606.ENSP00000210060.

Chemistry

ChEMBLCHEMBL4415.
DrugBankDB01299. Sulfadoxine.

PTM databases

PhosphoSiteP49366.

Polymorphism databases

DMDM1352267.

Proteomic databases

PaxDbP49366.
PRIDEP49366.

Protocols and materials databases

DNASU1725.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000210060; ENSP00000210060; ENSG00000095059. [P49366-1]
ENST00000351660; ENSP00000221303; ENSG00000095059. [P49366-2]
ENST00000594424; ENSP00000471886; ENSG00000095059. [P49366-3]
GeneID1725.
KEGGhsa:1725.
UCSCuc002mug.2. human. [P49366-1]
uc002mui.2. human. [P49366-2]

Organism-specific databases

CTD1725.
GeneCardsGC19M012786.
HGNCHGNC:2869. DHPS.
HPAHPA014461.
HPA029413.
MIM600944. gene.
neXtProtNX_P49366.
PharmGKBPA27329.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1899.
HOGENOMHOG000228838.
HOVERGENHBG000852.
InParanoidP49366.
KOK00809.
OMAVEIWADA.
TreeFamTF300625.

Enzyme and pathway databases

BioCycMetaCyc:HS01810-MONOMER.
ReactomeREACT_17015. Metabolism of proteins.
SABIO-RKP49366.
UniPathwayUPA00354.

Gene expression databases

ArrayExpressP49366.
BgeeP49366.
CleanExHS_DHPS.
GenevestigatorP49366.

Family and domain databases

Gene3D3.40.910.10. 1 hit.
InterProIPR002773. Deoxyhypusine_synthase.
[Graphical view]
PANTHERPTHR11703. PTHR11703. 1 hit.
PfamPF01916. DS. 1 hit.
[Graphical view]
TIGRFAMsTIGR00321. dhys. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP49366.
GeneWikiDHPS.
GenomeRNAi1725.
NextBio6975.
PROP49366.
SOURCESearch...

Entry information

Entry nameDHYS_HUMAN
AccessionPrimary (citable) accession number: P49366
Secondary accession number(s): A8K688 expand/collapse secondary AC list , M0R1I5, Q13184, Q13276, Q9UDG0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: March 19, 2014
This is version 138 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

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 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 19

Human chromosome 19: entries, gene names and cross-references to MIM