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Q6ICH7

- ASPH2_HUMAN

UniProt

Q6ICH7 - ASPH2_HUMAN

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Protein

Aspartate beta-hydroxylase domain-containing protein 2

Gene

ASPHD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

May function as 2-oxoglutarate-dependent dioxygenase.By similarity

Cofactori

Fe cationBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei228 – 22812-oxoglutarateBy similarity
Binding sitei272 – 27212-oxoglutarateBy similarity
Metal bindingi283 – 2831IronBy similarity
Metal bindingi328 – 3281IronBy similarity
Binding sitei341 – 34112-oxoglutarateBy similarity

GO - Molecular functioni

  1. dioxygenase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. peptidyl-amino acid modification Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate beta-hydroxylase domain-containing protein 2 (EC:1.14.11.-)
Gene namesi
Name:ASPHD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:30437. ASPHD2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5858CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei59 – 7921HelicalSequence AnalysisAdd
BLAST
Topological domaini80 – 369290LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485314.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Aspartate beta-hydroxylase domain-containing protein 2PRO_0000254162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ6ICH7.
PaxDbiQ6ICH7.
PRIDEiQ6ICH7.

PTM databases

PhosphoSiteiQ6ICH7.

Expressioni

Gene expression databases

BgeeiQ6ICH7.
CleanExiHS_ASPHD2.
ExpressionAtlasiQ6ICH7. baseline and differential.
GenevestigatoriQ6ICH7.

Organism-specific databases

HPAiHPA000820.

Interactioni

Protein-protein interaction databases

BioGridi121421. 5 interactions.
STRINGi9606.ENSP00000215906.

Structurei

3D structure databases

ProteinModelPortaliQ6ICH7.
SMRiQ6ICH7. Positions 188-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni292 – 29432-oxoglutarate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3555.
GeneTreeiENSGT00530000063281.
HOGENOMiHOG000233597.
HOVERGENiHBG079419.
InParanoidiQ6ICH7.
OMAiEWVTFYL.
OrthoDBiEOG7JMGDJ.
PhylomeDBiQ6ICH7.
TreeFamiTF312799.

Family and domain databases

Gene3Di2.60.120.330. 1 hit.
InterProiIPR007803. Asp_Arg_Pro-Hydrxlase.
IPR027443. IPNS-like.
[Graphical view]
PfamiPF05118. Asp_Arg_Hydrox. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6ICH7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVWAPLGPPR TDCLTLLHTP SKDSPKMSLE WLVAWSWSLD GLRDCIATGI
60 70 80 90 100
QSVRDCDTTA VITVACLLVL FVWYCYHVGR EQPRPYVSVN SLMQAADANG
110 120 130 140 150
LQNGYVYCQS PECVRCTHNE GLNQKLYHNL QEYAKRYSWS GMGRIHKGIR
160 170 180 190 200
EQGRYLNSRP SIQKPEVFFL PDLPTTPYFS RDAQKHDVEV LERNFQTILC
210 220 230 240 250
EFETLYKAFS NCSLPQGWKM NSTPSGEWFT FYLVNQGVCV PRNCRKCPRT
260 270 280 290 300
YRLLGSLRTC IGNNVFGNAC ISVLSPGTVI TEHYGPTNIR IRCHLGLKTP
310 320 330 340 350
NGCELVVGGE PQCWAEGRCL LFDDSFLHAA FHEGSAEDGP RVVFMVDLWH
360
PNVAAAERQA LDFIFAPGR
Length:369
Mass (Da):41,699
Last modified:July 5, 2004 - v1
Checksum:iAE28ED71AC770ACF
GO

Sequence cautioni

The sequence AAH36753.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG37570.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti235 – 2351N → S.
Corresponds to variant rs34902186 [ dbSNP | Ensembl ].
VAR_060123

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR456391 mRNA. Translation: CAG30277.1.
AK315112 mRNA. Translation: BAG37570.1. Different initiation.
Z99714 Genomic DNA. Translation: CAI17879.1.
BC036753 mRNA. Translation: AAH36753.1. Different initiation.
AL161993 mRNA. Translation: CAB82325.1.
CCDSiCCDS13834.2.
PIRiT47148.
RefSeqiNP_065170.2. NM_020437.4.
UniGeneiHs.567547.

Genome annotation databases

EnsembliENST00000215906; ENSP00000215906; ENSG00000128203.
GeneIDi57168.
KEGGihsa:57168.
UCSCiuc003acg.2. human.

Polymorphism databases

DMDMi74757726.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR456391 mRNA. Translation: CAG30277.1 .
AK315112 mRNA. Translation: BAG37570.1 . Different initiation.
Z99714 Genomic DNA. Translation: CAI17879.1 .
BC036753 mRNA. Translation: AAH36753.1 . Different initiation.
AL161993 mRNA. Translation: CAB82325.1 .
CCDSi CCDS13834.2.
PIRi T47148.
RefSeqi NP_065170.2. NM_020437.4.
UniGenei Hs.567547.

3D structure databases

ProteinModelPortali Q6ICH7.
SMRi Q6ICH7. Positions 188-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121421. 5 interactions.
STRINGi 9606.ENSP00000215906.

PTM databases

PhosphoSitei Q6ICH7.

Polymorphism databases

DMDMi 74757726.

Proteomic databases

MaxQBi Q6ICH7.
PaxDbi Q6ICH7.
PRIDEi Q6ICH7.

Protocols and materials databases

DNASUi 57168.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215906 ; ENSP00000215906 ; ENSG00000128203 .
GeneIDi 57168.
KEGGi hsa:57168.
UCSCi uc003acg.2. human.

Organism-specific databases

CTDi 57168.
GeneCardsi GC22P026825.
HGNCi HGNC:30437. ASPHD2.
HPAi HPA000820.
neXtProti NX_Q6ICH7.
PharmGKBi PA143485314.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3555.
GeneTreei ENSGT00530000063281.
HOGENOMi HOG000233597.
HOVERGENi HBG079419.
InParanoidi Q6ICH7.
OMAi EWVTFYL.
OrthoDBi EOG7JMGDJ.
PhylomeDBi Q6ICH7.
TreeFami TF312799.

Miscellaneous databases

GenomeRNAii 57168.
NextBioi 63181.
PROi Q6ICH7.

Gene expression databases

Bgeei Q6ICH7.
CleanExi HS_ASPHD2.
ExpressionAtlasi Q6ICH7. baseline and differential.
Genevestigatori Q6ICH7.

Family and domain databases

Gene3Di 2.60.120.330. 1 hit.
InterProi IPR007803. Asp_Arg_Pro-Hydrxlase.
IPR027443. IPNS-like.
[Graphical view ]
Pfami PF05118. Asp_Arg_Hydrox. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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.
    , 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].
    Tissue: Cerebellum.
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-369.
    Tissue: Amygdala.

Entry informationi

Entry nameiASPH2_HUMAN
AccessioniPrimary (citable) accession number: Q6ICH7
Secondary accession number(s): B2RCH3, Q7L0W3, Q9NSN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 84 of the entry and version 1 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 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3