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Protein

Diphosphoinositol polyphosphate phosphohydrolase 2

Gene

NUDT4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphate Ap6A, but not Ap5A. The major reaction products are ADP and p4a from Ap6A. Also able to hydrolyze 5-phosphoribose 1-diphosphate. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA.1 Publication

Catalytic activityi

Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.2 Publications

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 3 Mg(2+) or Mn2+ ions per subunit.By similarity

Kineticsi

  1. KM=4.2 nM for PP-InsP51 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101SubstrateBy similarity
Binding sitei41 – 411SubstrateBy similarity
Metal bindingi50 – 501Magnesium 1; via carbonyl oxygenBy similarity
Metal bindingi66 – 661Magnesium 2By similarity
Metal bindingi66 – 661Magnesium 3By similarity
Active sitei69 – 691Proton acceptorBy similarity
Metal bindingi70 – 701Magnesium 1By similarity

GO - Molecular functioni

  1. diphosphoinositol-polyphosphate diphosphatase activity Source: UniProtKB
  2. inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity Source: UniProtKB-EC
  3. inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity Source: UniProtKB-EC
  4. inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
  5. inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity Source: UniProtKB-EC
  6. inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
  7. inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
  8. inositol diphosphate tetrakisphosphate diphosphatase activity Source: Reactome
  9. metal ion binding Source: UniProtKB-KW
  10. snoRNA binding Source: UniProtKB

GO - Biological processi

  1. calcium-mediated signaling Source: UniProtKB
  2. cyclic-nucleotide-mediated signaling Source: UniProtKB
  3. cyclic nucleotide metabolic process Source: ProtInc
  4. inositol phosphate metabolic process Source: Reactome
  5. intracellular signal transduction Source: UniProtKB
  6. intracellular transport Source: UniProtKB
  7. regulation of RNA export from nucleus Source: UniProtKB
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS10696-MONOMER.
ReactomeiREACT_150188. Synthesis of pyrophosphates in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Diphosphoinositol polyphosphate phosphohydrolase 2 (EC:3.6.1.52)
Short name:
DIPP-2
Alternative name(s):
Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2 (EC:3.6.1.-)
Nucleoside diphosphate-linked moiety X motif 4
Short name:
Nudix motif 4
Gene namesi
Name:NUDT4
Synonyms:DIPP2, KIAA0487
ORF Names:HDCMB47P
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:8051. NUDT4.

Subcellular locationi

  1. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. intracellular Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31835.

Polymorphism and mutation databases

BioMutaiNUDT4.
DMDMi68565946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180Diphosphoinositol polyphosphate phosphohydrolase 2PRO_0000057058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NZJ9.
PRIDEiQ9NZJ9.

PTM databases

PhosphoSiteiQ9NZJ9.

Expressioni

Tissue specificityi

Expressed in heart and, at lower level in skeletal muscle, pancreas and kidney.1 Publication

Gene expression databases

BgeeiQ9NZJ9.
CleanExiHS_NUDT4.
ExpressionAtlasiQ9NZJ9. baseline and differential.
GenevestigatoriQ9NZJ9.

Organism-specific databases

HPAiHPA017593.
HPA047027.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KEAP1Q141453EBI-4280066,EBI-751001

Protein-protein interaction databases

BioGridi116334. 2 interactions.
IntActiQ9NZJ9. 1 interaction.
MINTiMINT-2819936.

Structurei

3D structure databases

ProteinModelPortaliQ9NZJ9.
SMRiQ9NZJ9. Positions 9-146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 144127Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 203Substrate bindingBy similarity
Regioni89 – 913Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi51 – 7222Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family. DIPP subfamily.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000012928.
HOVERGENiHBG053341.
InParanoidiQ9NZJ9.
KOiK07766.
OMAiVMNVTQE.
OrthoDBiEOG7T7GVQ.
PhylomeDBiQ9NZJ9.
TreeFamiTF106349.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NZJ9-1) [UniParc]FASTAAdd to basket

Also known as: Alpha, DIPP2alpha

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.

« Hide

        10         20         30         40         50
MMKFKPNQTR TYDREGFKKR AACLCFRSEQ EDEVLLVSSS RYPDQWIVPG
60 70 80 90 100
GGMEPEEEPG GAAVREVYEE AGVKGKLGRL LGIFENQDRK HRTYVYVLTV
110 120 130 140 150
TEILEDWEDS VNIGRKREWF KVEDAIKVLQ CHKPVHAEYL EKLKLGCSPA
160 170 180
NGNSTVPSLP DNNALFVTAA QTSGLPSSVR
Length:180
Mass (Da):20,306
Last modified:July 5, 2005 - v2
Checksum:i86D766F8F5B22D13
GO
Isoform 2 (identifier: Q9NZJ9-2) [UniParc]FASTAAdd to basket

Also known as: Beta, DIPP2beta

The sequence of this isoform differs from the canonical sequence as follows:
     85-85: E → EQ

Show »
Length:181
Mass (Da):20,434
Checksum:iCB3C131FAD21A4AA
GO
Isoform 3 (identifier: Q9NZJ9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.
     85-85: E → EQ

Show »
Length:129
Mass (Da):14,395
Checksum:i2A8C483085B2D4D3
GO

Sequence cautioni

The sequence AAF75563.1 differs from that shown. Reason: Erroneous termination at position 181. Translated as stop.Curated
The sequence BAE16985.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161G → D in AAF68857 (PubMed:10777568).Curated
Sequence conflicti41 – 411R → Q in BAD97217 (Ref. 7) Curated
Sequence conflicti73 – 731V → D in AAF75563 (Ref. 3) Curated
Sequence conflicti164 – 1641A → V in AAF68857 (PubMed:10777568).Curated
Sequence conflicti177 – 1771S → P in AAF68858 (PubMed:10777568).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5252Missing in isoform 3. 3 PublicationsVSP_014269Add
BLAST
Alternative sequencei85 – 851E → EQ in isoform 2 and isoform 3. 6 PublicationsVSP_014270

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191649 mRNA. Translation: AAF68855.1.
AF191650 mRNA. Translation: AAF68856.1.
AF191651 mRNA. Translation: AAF68857.1.
AF191652 mRNA. Translation: AAF68858.2.
AF191653 mRNA. Translation: AAF68859.1.
AB007956 mRNA. Translation: BAE16985.1. Different initiation.
AF067803 mRNA. Translation: AAF75563.1. Sequence problems.
CR749445 mRNA. Translation: CAH18283.1.
BT020109 mRNA. Translation: AAV38912.1.
BT020110 mRNA. Translation: AAV38913.1.
AK304296 mRNA. Translation: BAH14152.1.
AK223497 mRNA. Translation: BAD97217.1.
BC012069 mRNA. Translation: AAH12069.1.
BC051310 mRNA. Translation: AAH51310.1.
CCDSiCCDS44952.1. [Q9NZJ9-1]
CCDS73504.1. [Q9NZJ9-3]
CCDS9044.1. [Q9NZJ9-2]
RefSeqiNP_001287951.1. NM_001301022.1. [Q9NZJ9-3]
NP_001287952.1. NM_001301023.1.
NP_001287953.1. NM_001301024.1.
NP_061967.3. NM_019094.5. [Q9NZJ9-1]
NP_950241.1. NM_199040.3. [Q9NZJ9-2]
UniGeneiHs.506325.

Genome annotation databases

EnsembliENST00000337179; ENSP00000338352; ENSG00000173598. [Q9NZJ9-2]
ENST00000415493; ENSP00000406612; ENSG00000173598. [Q9NZJ9-1]
ENST00000547014; ENSP00000448032; ENSG00000173598. [Q9NZJ9-3]
GeneIDi11163.
KEGGihsa:11163.
UCSCiuc001tcm.3. human. [Q9NZJ9-1]
uc010sup.2. human. [Q9NZJ9-2]
uc010suq.2. human. [Q9NZJ9-3]

Polymorphism and mutation databases

BioMutaiNUDT4.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF191649 mRNA. Translation: AAF68855.1.
AF191650 mRNA. Translation: AAF68856.1.
AF191651 mRNA. Translation: AAF68857.1.
AF191652 mRNA. Translation: AAF68858.2.
AF191653 mRNA. Translation: AAF68859.1.
AB007956 mRNA. Translation: BAE16985.1. Different initiation.
AF067803 mRNA. Translation: AAF75563.1. Sequence problems.
CR749445 mRNA. Translation: CAH18283.1.
BT020109 mRNA. Translation: AAV38912.1.
BT020110 mRNA. Translation: AAV38913.1.
AK304296 mRNA. Translation: BAH14152.1.
AK223497 mRNA. Translation: BAD97217.1.
BC012069 mRNA. Translation: AAH12069.1.
BC051310 mRNA. Translation: AAH51310.1.
CCDSiCCDS44952.1. [Q9NZJ9-1]
CCDS73504.1. [Q9NZJ9-3]
CCDS9044.1. [Q9NZJ9-2]
RefSeqiNP_001287951.1. NM_001301022.1. [Q9NZJ9-3]
NP_001287952.1. NM_001301023.1.
NP_001287953.1. NM_001301024.1.
NP_061967.3. NM_019094.5. [Q9NZJ9-1]
NP_950241.1. NM_199040.3. [Q9NZJ9-2]
UniGeneiHs.506325.

3D structure databases

ProteinModelPortaliQ9NZJ9.
SMRiQ9NZJ9. Positions 9-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116334. 2 interactions.
IntActiQ9NZJ9. 1 interaction.
MINTiMINT-2819936.

PTM databases

PhosphoSiteiQ9NZJ9.

Polymorphism and mutation databases

BioMutaiNUDT4.
DMDMi68565946.

Proteomic databases

MaxQBiQ9NZJ9.
PRIDEiQ9NZJ9.

Protocols and materials databases

DNASUi11163.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337179; ENSP00000338352; ENSG00000173598. [Q9NZJ9-2]
ENST00000415493; ENSP00000406612; ENSG00000173598. [Q9NZJ9-1]
ENST00000547014; ENSP00000448032; ENSG00000173598. [Q9NZJ9-3]
GeneIDi11163.
KEGGihsa:11163.
UCSCiuc001tcm.3. human. [Q9NZJ9-1]
uc010sup.2. human. [Q9NZJ9-2]
uc010suq.2. human. [Q9NZJ9-3]

Organism-specific databases

CTDi11163.
GeneCardsiGC12P093771.
HGNCiHGNC:8051. NUDT4.
HPAiHPA017593.
HPA047027.
MIMi609229. gene.
neXtProtiNX_Q9NZJ9.
PharmGKBiPA31835.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00390000012928.
HOVERGENiHBG053341.
InParanoidiQ9NZJ9.
KOiK07766.
OMAiVMNVTQE.
OrthoDBiEOG7T7GVQ.
PhylomeDBiQ9NZJ9.
TreeFamiTF106349.

Enzyme and pathway databases

BioCyciMetaCyc:HS10696-MONOMER.
ReactomeiREACT_150188. Synthesis of pyrophosphates in the cytosol.

Miscellaneous databases

ChiTaRSiNUDT4. human.
GeneWikiiNUDT4.
GenomeRNAii11163.
NextBioi42469.
PROiQ9NZJ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NZJ9.
CleanExiHS_NUDT4.
ExpressionAtlasiQ9NZJ9. baseline and differential.
GenevestigatoriQ9NZJ9.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. The expanding NUDT family."
    Caffrey J.J., Safrany S.T., Yang X., Shears S.B.
    J. Biol. Chem. 275:12730-12736(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Tissue: Cerebellum.
  2. "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] (ISOFORM 1).
    Tissue: Brain.
  3. "Novel gene identified from dendritic cells."
    Zhao Z., Huang X., Li N., Zhu X., Cao X.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Retina.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  6. "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.
    , 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 3).
    Tissue: Trachea.
  7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Lymph and Placenta.
  9. "Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases."
    Leslie N.R., McLennan A.G., Safrany S.T.
    BMC Biochem. 3:20-20(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Nudix hydrolases that degrade dinucleoside and diphosphoinositol polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP) pyrophosphatase activity that generates the glycolytic activator ribose 1,5-bisphosphate."
    Fisher D.I., Safrany S.T., Strike P., McLennan A.G., Cartwright J.L.
    J. Biol. Chem. 277:47313-47317(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNUDT4_HUMAN
AccessioniPrimary (citable) accession number: Q9NZJ9
Secondary accession number(s): B7Z916
, Q4AEJ6, Q53EZ2, Q68DD7, Q9NPC5, Q9NS30, Q9NZK0, Q9NZK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 5, 2005
Last modified: April 29, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.