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Protein

Aspartyl/asparaginyl beta-hydroxylase

Gene

Asph

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Isoform 1: specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.1 Publication

Catalytic activityi

Peptide L-aspartate + 2-oxoglutarate + O2 = peptide 3-hydroxy-L-aspartate + succinate + CO2.1 Publication

Cofactori

Fe cationBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei608 – 60812-oxoglutarateBy similarity
Binding sitei651 – 65112-oxoglutarateBy similarity
Metal bindingi662 – 6621IronBy similarity
Metal bindingi708 – 7081IronBy similarity
Binding sitei718 – 71812-oxoglutarateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi99 – 11113By similarityAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: MGI
  • peptide-aspartate beta-dioxygenase activity Source: MGI

GO - Biological processi

  • activation of cysteine-type endopeptidase activity Source: MGI
  • activation of store-operated calcium channel activity Source: MGI
  • calcium ion transmembrane transport Source: MGI
  • cellular response to calcium ion Source: MGI
  • face morphogenesis Source: MGI
  • limb morphogenesis Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • palate development Source: MGI
  • pattern specification process Source: MGI
  • peptidyl-aspartic acid hydroxylation Source: MGI
  • positive regulation of calcium ion transport into cytosol Source: MGI
  • positive regulation of intracellular protein transport Source: MGI
  • positive regulation of proteolysis Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: MGI
  • regulation of protein depolymerization Source: BHF-UCL
  • regulation of protein stability Source: BHF-UCL
  • response to ATP Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Calcium, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.161 Publication)
Alternative name(s):
Aspartate beta-hydroxylase
Short name:
ASP beta-hydroxylase
Peptide-aspartate beta-dioxygenase
Gene namesi
Name:Asph
Synonyms:Bah
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1914186. Asph.

Subcellular locationi

Isoform 1 :
Isoform 2 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6262CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei63 – 8321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini84 – 741658LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Selective disruption of isoform 1 abolishes liver aspartyl beta-hydroxylase activity, but does not affect the expression of isoform 2. Mice lacking isoform 1 have normal blood chemistry, do not present blood coagulation defects and appear more or less normal, except for shorter snouts, mild defects of the palate ridges, syndactily due to fusion of soft tissues and reduced litter size from mutant females, while male fertiliy appears normal. Mice lacking isoform 2 show no visible phenotype.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 741741Aspartyl/asparaginyl beta-hydroxylasePRO_0000254161Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphoserineBy similarity
Glycosylationi453 – 4531N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi624 ↔ 631By similarity
Glycosylationi689 – 6891N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8BSY0.
PaxDbiQ8BSY0.
PRIDEiQ8BSY0.

PTM databases

PhosphoSiteiQ8BSY0.

Expressioni

Tissue specificityi

Isoform 1 is detected in heart, liver and ovary (at protein level). Detected in heart ventricle. Isoform 1 is widely expressed. Isoform 2 is detected in heart and skeletal muscle.3 Publications

Developmental stagei

Strongly expressed in the snout, limbs and eye of embryonic day 11.5 (E11.5) and E12. Strong localization of the protein in the lens of the developing eye at all three stages.1 Publication

Gene expression databases

BgeeiQ8BSY0.
CleanExiMM_ASPH.
ExpressionAtlasiQ8BSY0. baseline and differential.
GenevisibleiQ8BSY0. MM.

Interactioni

Subunit structurei

Monomer. Isoform 2 interacts with CASQ2.By similarity

Protein-protein interaction databases

BioGridi211167. 2 interactions.
IntActiQ8BSY0. 5 interactions.
MINTiMINT-4112262.
STRINGi10090.ENSMUSP00000077273.

Structurei

3D structure databases

ProteinModelPortaliQ8BSY0.
SMRiQ8BSY0. Positions 331-369, 445-503, 545-741.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati324 – 35734TPR 1Add
BLAST
Repeati365 – 39834TPR 2Add
BLAST
Repeati437 – 47034TPR 3Add
BLAST
Repeati472 – 50433TPR 4Add
BLAST
Repeati508 – 54033TPR 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni671 – 67332-oxoglutarate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 6153Gly-richAdd
BLAST
Compositional biasi14 – 3825Ser-richAdd
BLAST
Compositional biasi310 – 3156Poly-Lys

Sequence similaritiesi

Contains 5 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, TPR repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3555.
GeneTreeiENSGT00530000063281.
HOGENOMiHOG000231625.
HOVERGENiHBG004290.
InParanoidiQ8BSY0.
KOiK00476.
OMAiRNENACK.
OrthoDBiEOG715Q44.
PhylomeDBiQ8BSY0.
TreeFamiTF312799.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.60.120.330. 1 hit.
InterProiIPR007943. Asp-B-hydro/Triadin_dom.
IPR007803. Asp_Arg_Pro-Hydrxlase.
IPR027443. IPNS-like.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF05279. Asp-B-Hydro_N. 1 hit.
PF05118. Asp_Arg_Hydrox. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BSY0-1) [UniParc]FASTAAdd to basket

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
MAPRKNAKGG GGNSSSSGSG SGSGSGSPST GSSGSSSSPG ARREAKHGGH
60 70 80 90 100
KNGRRGGISG GSFFTWFMVI ALLGVWTSVA VVWFDLVDYE EVLGKLGVYD
110 120 130 140 150
ADGDGDFDVD DAKVLLGLKE RSPSERTFPP EEEAETHAEL EEQAPEGADI
160 170 180 190 200
QNVEDEVKEQ IQSLLQESVH TDHDLEADGL AGEPQPEVED FLTVTDSDDR
210 220 230 240 250
FEDLEPGTVH EEIEDTYHVE DTASQNHPND MEEMTNEQEN SDPSEAVTDA
260 270 280 290 300
GVLLPHAEEV RHQDYDEPVY EPSEHEGVAI SDNTIDDSSI ISEEINVASV
310 320 330 340 350
EEQQDTPPVK KKKPKLLNKF DKTIKAELDA AEKLRKRGKI EEAVNAFEEL
360 370 380 390 400
VRKYPQSPRA RYGKAQCEDD LAEKQRSNEV LRRAIETYQE AADLPDAPTD
410 420 430 440 450
LVKLSLKRRS ERQQFLGHMR GSLLTLQRLV QLFPSDTTLK NDLGVGYLLL
460 470 480 490 500
GDNDSAKKVY EEVLNVTPND GFAKVHYGFI LKAQNKISES IPYLKEGIES
510 520 530 540 550
GDPGTDDGRF YFHLGDAMQR VGNKEAYKWY ELGHKRGHFA SVWQRSLYNV
560 570 580 590 600
NGLKAQPWWT PRETGYTELV KSLERNWKLI RDEGLMVMDK AKGLFLPEDE
610 620 630 640 650
NLREKGDWSQ FTLWQQGRKN ENACKGAPKT CALLEKFSET TGCRRGQIKY
660 670 680 690 700
SIMHPGTHVW PHTGPTNCRL RMHLGLVIPK EGCKIRCANE TRTWEEGKVL
710 720 730 740
IFDDSFEHEV WQDASSFRLI FIVDVWHPEL TPQQRRSLPA I
Length:741
Mass (Da):83,042
Last modified:March 1, 2003 - v1
Checksum:i0660A6A5E34418C8
GO
Isoform 2 (identifier: Q8BSY0-2) [UniParc]FASTAAdd to basket

Also known as: Junctin

The sequence of this isoform differs from the canonical sequence as follows:
     1-43: MAPRKNAKGGGGNSSSSGSGSGSGSGSPSTGSSGSSSSPGARR → MAEDK
     117-245: GLKERSPSER...NEQENSDPSE → EGPGGLAKRK...SKENGQKRKN
     246-741: Missing.

Show »
Length:207
Mass (Da):22,757
Checksum:i37A13D30E49CD67C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1322Missing in AAG40808 (PubMed:10956665).Curated
Sequence conflicti131 – 1322Missing in AAG40809 (PubMed:10956665).Curated
Sequence conflicti279 – 2791A → E in AAG40808 (PubMed:10956665).Curated
Sequence conflicti279 – 2791A → E in AAG40809 (PubMed:10956665).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4343MAPRK…PGARR → MAEDK in isoform 2. CuratedVSP_056792Add
BLAST
Alternative sequencei117 – 245129GLKER…SDPSE → EGPGGLAKRKTKAKAKEPIK EELKKERGKAVPSKNEERRQ GKKEQEDRGKGRKKPDSDTS QKASAAGKRDRDKEKASSDK SSKSKESWKKAVETKAVSSK VAARDKDRRGRSSSGHAHVS KENGQKRKN in isoform 2. CuratedVSP_056793Add
BLAST
Alternative sequencei246 – 741496Missing in isoform 2. CuratedVSP_056794Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF221854 mRNA. Translation: AAK00614.1.
AF289486 mRNA. Translation: AAG40808.1.
AF289487 mRNA. Translation: AAG40809.1.
AF289490 mRNA. Translation: AAG40812.1.
AF223413 mRNA. Translation: AAN87549.1.
AK030293 mRNA. Translation: BAC26882.1.
BC128299 mRNA. Translation: AAI28300.1.
BC152365 mRNA. Translation: AAI52366.1.
CCDSiCCDS17959.1. [Q8BSY0-2]
CCDS38690.1. [Q8BSY0-1]
RefSeqiNP_001171321.1. NM_001177850.1.
NP_001171323.1. NM_001177852.1.
NP_001171324.1. NM_001177853.1.
NP_001171325.1. NM_001177854.1.
NP_001171326.1. NM_001177855.1.
NP_001277296.1. NM_001290367.1.
NP_075553.2. NM_023066.3. [Q8BSY0-1]
UniGeneiMm.222206.
Mm.412008.

Genome annotation databases

EnsembliENSMUST00000078139; ENSMUSP00000077273; ENSMUSG00000028207. [Q8BSY0-1]
GeneIDi65973.
KEGGimmu:65973.
UCSCiuc008ryf.2. mouse. [Q8BSY0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF221854 mRNA. Translation: AAK00614.1.
AF289486 mRNA. Translation: AAG40808.1.
AF289487 mRNA. Translation: AAG40809.1.
AF289490 mRNA. Translation: AAG40812.1.
AF223413 mRNA. Translation: AAN87549.1.
AK030293 mRNA. Translation: BAC26882.1.
BC128299 mRNA. Translation: AAI28300.1.
BC152365 mRNA. Translation: AAI52366.1.
CCDSiCCDS17959.1. [Q8BSY0-2]
CCDS38690.1. [Q8BSY0-1]
RefSeqiNP_001171321.1. NM_001177850.1.
NP_001171323.1. NM_001177852.1.
NP_001171324.1. NM_001177853.1.
NP_001171325.1. NM_001177854.1.
NP_001171326.1. NM_001177855.1.
NP_001277296.1. NM_001290367.1.
NP_075553.2. NM_023066.3. [Q8BSY0-1]
UniGeneiMm.222206.
Mm.412008.

3D structure databases

ProteinModelPortaliQ8BSY0.
SMRiQ8BSY0. Positions 331-369, 445-503, 545-741.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211167. 2 interactions.
IntActiQ8BSY0. 5 interactions.
MINTiMINT-4112262.
STRINGi10090.ENSMUSP00000077273.

PTM databases

PhosphoSiteiQ8BSY0.

Proteomic databases

MaxQBiQ8BSY0.
PaxDbiQ8BSY0.
PRIDEiQ8BSY0.

Protocols and materials databases

DNASUi65973.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000078139; ENSMUSP00000077273; ENSMUSG00000028207. [Q8BSY0-1]
GeneIDi65973.
KEGGimmu:65973.
UCSCiuc008ryf.2. mouse. [Q8BSY0-1]

Organism-specific databases

CTDi444.
MGIiMGI:1914186. Asph.

Phylogenomic databases

eggNOGiCOG3555.
GeneTreeiENSGT00530000063281.
HOGENOMiHOG000231625.
HOVERGENiHBG004290.
InParanoidiQ8BSY0.
KOiK00476.
OMAiRNENACK.
OrthoDBiEOG715Q44.
PhylomeDBiQ8BSY0.
TreeFamiTF312799.

Miscellaneous databases

NextBioi320434.
PROiQ8BSY0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BSY0.
CleanExiMM_ASPH.
ExpressionAtlasiQ8BSY0. baseline and differential.
GenevisibleiQ8BSY0. MM.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
2.60.120.330. 1 hit.
InterProiIPR007943. Asp-B-hydro/Triadin_dom.
IPR007803. Asp_Arg_Pro-Hydrxlase.
IPR027443. IPNS-like.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF05279. Asp-B-Hydro_N. 1 hit.
PF05118. Asp_Arg_Hydrox. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, primary structure, and immunological characterization of the 26-kDa calsequestrin binding protein (junctin) from cardiac junctional sarcoplasmic reticulum."
    Jones L.R., Zhang L., Sanborn K., Jorgensen A.O., Kelley J.
    J. Biol. Chem. 270:30787-30796(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Heart muscle.
  2. "Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved isoform of Asph missing the catalytic domain share exons with junctin."
    Dinchuk J.E., Henderson N.L., Burn T.C., Huber R., Ho S.P., Link J., O'Neil K.T., Focht R.J., Scully M.S., Hollis J.M., Hollis G.F., Friedman P.A.
    J. Biol. Chem. 275:39543-39554(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Liver.
  3. "Mouse junctin-1 mRNA."
    Hong C., Kim D.H.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: BALB/c.
    Tissue: Heart.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  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 2).
  6. "Absence of post-translational aspartyl beta-hydroxylation of epidermal growth factor domains in mice leads to developmental defects and an increased incidence of intestinal neoplasia."
    Dinchuk J.E., Focht R.J., Kelley J.A., Henderson N.L., Zolotarjova N.I., Wynn R., Neff N.T., Link J., Huber R.M., Burn T.C., Rupar M.J., Cunningham M.R., Selling B.H., Ma J., Stern A.A., Hollis G.F., Stein R.B., Friedman P.A.
    J. Biol. Chem. 277:12970-12977(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  7. "Triadin/junctin double null mouse reveals a differential role for triadin and junctin in anchoring CASQ to the jSR and regulating Ca(2+) homeostasis."
    Boncompagni S., Thomas M., Lopez J.R., Allen P.D., Yuan Q., Kranias E.G., Franzini-Armstrong C., Perez C.F.
    PLoS ONE 7:E39962-E39962(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  8. "Mutations in ASPH cause facial dysmorphism, lens dislocation, anterior-segment abnormalities, and spontaneous filtering blebs, or Traboulsi syndrome."
    Patel N., Khan A.O., Mansour A., Mohamed J.Y., Al-Assiri A., Haddad R., Jia X., Xiong Y., Megarbane A., Traboulsi E.I., Alkuraya F.S.
    Am. J. Hum. Genet. 94:755-759(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiASPH_MOUSE
AccessioniPrimary (citable) accession number: Q8BSY0
Secondary accession number(s): Q9EPA6, Q9EQ64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.