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Q9NR63

- CP26B_HUMAN

UniProt

Q9NR63 - CP26B_HUMAN

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Protein

Cytochrome P450 26B1

Gene

CYP26B1

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

Functioni

Involved in the metabolism of retinoic acid (RA), rendering this classical morphogen inactive through oxidation. Involved in the specific inactivation of all-trans-retinoic acid (all-trans-RA), with a preference for the following substrates: all-trans-RA > 9-cis-RA > 13-cis-RA. Generates several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH-RA. Esential for postnatal survival. Plays a central role in germ cell development: acts by degrading RA in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints.2 Publications

Cofactori

Heme group.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi441 – 4411Iron (heme axial ligand)Sequence Analysis

GO - Molecular functioni

  1. heme binding Source: BHF-UCL
  2. iron ion binding Source: InterPro
  3. retinoic acid 4-hydroxylase activity Source: BHF-UCL
  4. retinoic acid binding Source: BHF-UCL

GO - Biological processi

  1. bone morphogenesis Source: UniProtKB
  2. cell fate determination Source: BHF-UCL
  3. cellular response to retinoic acid Source: Ensembl
  4. cornification Source: Ensembl
  5. embryonic limb morphogenesis Source: BHF-UCL
  6. establishment of skin barrier Source: Ensembl
  7. male meiosis Source: BHF-UCL
  8. negative regulation of retinoic acid receptor signaling pathway Source: BHF-UCL
  9. oxidation-reduction process Source: BHF-UCL
  10. positive regulation of gene expression Source: Ensembl
  11. positive regulation of tongue muscle cell differentiation Source: Ensembl
  12. proximal/distal pattern formation Source: BHF-UCL
  13. retinoic acid catabolic process Source: BHF-UCL
  14. retinoic acid receptor signaling pathway Source: Ensembl
  15. small molecule metabolic process Source: Reactome
  16. spermatogenesis Source: BHF-UCL
  17. tongue morphogenesis Source: Ensembl
  18. vitamin metabolic process Source: Reactome
  19. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_13450. Vitamins.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 26B1 (EC:1.14.-.-)
Alternative name(s):
Cytochrome P450 26A2
Cytochrome P450 retinoic acid-inactivating 2
Short name:
Cytochrome P450RAI-2
Retinoic acid-metabolizing cytochrome
Gene namesi
Name:CYP26B1
Synonyms:CYP26A2, P450RAI2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:20581. CYP26B1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Involvement in diseasei

Radiohumeral fusions with other skeletal and craniofacial anomalies (RHFCA) [MIM:614416]: A disease characterized by craniofacial malformations, occipital encephalocele, radiohumeral fusions, oligodactyly, advanced osseous maturation, and calvarial mineralization defects.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461S → P in RHFCA. 1 Publication
Corresponds to variant rs281875232 [ dbSNP | Ensembl ].
VAR_067923
Natural varianti363 – 3631R → L in RHFCA. 1 Publication
Corresponds to variant rs281875231 [ dbSNP | Ensembl ].
VAR_067924

Keywords - Diseasei

Craniosynostosis, Disease mutation

Organism-specific databases

MIMi614416. phenotype.
Orphaneti293925. Lethal occipital encephalocele-skeletal dysplasia syndrome.
PharmGKBiPA134879191.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Cytochrome P450 26B1PRO_0000051985Add
BLAST

Proteomic databases

MaxQBiQ9NR63.
PaxDbiQ9NR63.
PRIDEiQ9NR63.

PTM databases

PhosphoSiteiQ9NR63.

Expressioni

Tissue specificityi

Highly expressed in brain, particularly in the cerebellum and pons.1 Publication

Inductioni

By retinoic acid.

Gene expression databases

BgeeiQ9NR63.
CleanExiHS_CYP26B1.
ExpressionAtlasiQ9NR63. baseline and differential.
GenevestigatoriQ9NR63.

Organism-specific databases

HPAiHPA012567.

Interactioni

Protein-protein interaction databases

BioGridi121153. 2 interactions.
STRINGi9606.ENSP00000001146.

Structurei

3D structure databases

ProteinModelPortaliQ9NR63.
SMRiQ9NR63. Positions 32-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00660000095370.
HOGENOMiHOG000220829.
HOVERGENiHBG051099.
InParanoidiQ9NR63.
KOiK12664.
OMAiWSSQPEA.
OrthoDBiEOG7F24SP.
PhylomeDBiQ9NR63.
TreeFamiTF105093.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00465. EP450IV.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NR63) [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
MLFEGLDLVS ALATLAACLV SVTLLLAVSQ QLWQLRWAAT RDKSCKLPIP
60 70 80 90 100
KGSMGFPLIG ETGHWLLQGS GFQSSRREKY GNVFKTHLLG RPLIRVTGAE
110 120 130 140 150
NVRKILMGEH HLVSTEWPRS TRMLLGPNTV SNSIGDIHRN KRKVFSKIFS
160 170 180 190 200
HEALESYLPK IQLVIQDTLR AWSSHPEAIN VYQEAQKLTF RMAIRVLLGF
210 220 230 240 250
SIPEEDLGHL FEVYQQFVDN VFSLPVDLPF SGYRRGIQAR QILQKGLEKA
260 270 280 290 300
IREKLQCTQG KDYLDALDLL IESSKEHGKE MTMQELKDGT LELIFAAYAT
310 320 330 340 350
TASASTSLIM QLLKHPTVLE KLRDELRAHG ILHSGGCPCE GTLRLDTLSG
360 370 380 390 400
LRYLDCVIKE VMRLFTPISG GYRTVLQTFE LDGFQIPKGW SVMYSIRDTH
410 420 430 440 450
DTAPVFKDVN VFDPDRFSQA RSEDKDGRFH YLPFGGGVRT CLGKHLAKLF
460 470 480 490 500
LKVLAVELAS TSRFELATRT FPRITLVPVL HPVDGLSVKF FGLDSNQNEI
510
LPETEAMLSA TV
Length:512
Mass (Da):57,513
Last modified:October 1, 2000 - v1
Checksum:iA06D1D9944E6726F
GO
Isoform 2 (identifier: Q9NR63-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     69-143: Missing.

Show »
Length:437
Mass (Da):49,007
Checksum:i85CA080EB0045520
GO
Isoform 3 (identifier: Q9NR63-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: MLFEGLDLVS...LIGETGHWLL → MKNKTCVLVC...TLRETRVWLP

Note: No experimental confirmation available.

Show »
Length:495
Mass (Da):55,756
Checksum:iF5BBD7200E20573B
GO

Sequence cautioni

The sequence BAH12154.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti265 – 2651D → G in BAH11930. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461S → P in RHFCA. 1 Publication
Corresponds to variant rs281875232 [ dbSNP | Ensembl ].
VAR_067923
Natural varianti181 – 1811V → M.1 Publication
VAR_038722
Natural varianti185 – 1851A → V.1 Publication
VAR_038723
Natural varianti191 – 1911R → H.1 Publication
Corresponds to variant rs76025186 [ dbSNP | Ensembl ].
VAR_038724
Natural varianti227 – 2271D → N.1 Publication
VAR_038725
Natural varianti264 – 2641L → S.3 Publications
Corresponds to variant rs2241057 [ dbSNP | Ensembl ].
VAR_024383
Natural varianti363 – 3631R → L in RHFCA. 1 Publication
Corresponds to variant rs281875231 [ dbSNP | Ensembl ].
VAR_067924
Natural varianti380 – 3801E → K.1 Publication
Corresponds to variant rs2286965 [ dbSNP | Ensembl ].
VAR_038726
Natural varianti420 – 4201A → G.1 Publication
Corresponds to variant rs7568553 [ dbSNP | Ensembl ].
VAR_038727
Natural varianti473 – 4731R → C.1 Publication
Corresponds to variant rs61751056 [ dbSNP | Ensembl ].
VAR_038728
Natural varianti479 – 4791V → I.1 Publication
Corresponds to variant rs148075682 [ dbSNP | Ensembl ].
VAR_038729

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6767MLFEG…GHWLL → MKNKTCVLVCVSVFGGERGQ VTVPRVGVRRPSLAGPLQKC TLRETRVWLP in isoform 3. 1 PublicationVSP_042967Add
BLAST
Alternative sequencei69 – 14375Missing in isoform 2. 2 PublicationsVSP_042968Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF252297 mRNA. Translation: AAF76003.1.
FJ467289 mRNA. Translation: ACR19332.1.
AK294814 mRNA. Translation: BAH11892.1.
AK294933 mRNA. Translation: BAH11930.1.
AK295683 mRNA. Translation: BAH12154.1. Different initiation.
AK313433 mRNA. Translation: BAG36224.1.
AC007002 Genomic DNA. Translation: AAY14690.1.
BC069443 mRNA. Translation: AAH69443.1.
BC109205 mRNA. Translation: AAI09206.1.
CCDSiCCDS1919.1. [Q9NR63-1]
CCDS62934.1. [Q9NR63-2]
RefSeqiNP_001264671.1. NM_001277742.1. [Q9NR63-2]
NP_063938.1. NM_019885.3. [Q9NR63-1]
UniGeneiHs.91546.

Genome annotation databases

EnsembliENST00000001146; ENSP00000001146; ENSG00000003137. [Q9NR63-1]
ENST00000546307; ENSP00000443304; ENSG00000003137. [Q9NR63-2]
GeneIDi56603.
KEGGihsa:56603.
UCSCiuc002sih.2. human. [Q9NR63-1]
uc010yra.1. human. [Q9NR63-3]
uc010yrb.2. human. [Q9NR63-2]

Polymorphism databases

DMDMi20137526.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF252297 mRNA. Translation: AAF76003.1 .
FJ467289 mRNA. Translation: ACR19332.1 .
AK294814 mRNA. Translation: BAH11892.1 .
AK294933 mRNA. Translation: BAH11930.1 .
AK295683 mRNA. Translation: BAH12154.1 . Different initiation.
AK313433 mRNA. Translation: BAG36224.1 .
AC007002 Genomic DNA. Translation: AAY14690.1 .
BC069443 mRNA. Translation: AAH69443.1 .
BC109205 mRNA. Translation: AAI09206.1 .
CCDSi CCDS1919.1. [Q9NR63-1 ]
CCDS62934.1. [Q9NR63-2 ]
RefSeqi NP_001264671.1. NM_001277742.1. [Q9NR63-2 ]
NP_063938.1. NM_019885.3. [Q9NR63-1 ]
UniGenei Hs.91546.

3D structure databases

ProteinModelPortali Q9NR63.
SMRi Q9NR63. Positions 32-493.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121153. 2 interactions.
STRINGi 9606.ENSP00000001146.

PTM databases

PhosphoSitei Q9NR63.

Polymorphism databases

DMDMi 20137526.

Proteomic databases

MaxQBi Q9NR63.
PaxDbi Q9NR63.
PRIDEi Q9NR63.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000001146 ; ENSP00000001146 ; ENSG00000003137 . [Q9NR63-1 ]
ENST00000546307 ; ENSP00000443304 ; ENSG00000003137 . [Q9NR63-2 ]
GeneIDi 56603.
KEGGi hsa:56603.
UCSCi uc002sih.2. human. [Q9NR63-1 ]
uc010yra.1. human. [Q9NR63-3 ]
uc010yrb.2. human. [Q9NR63-2 ]

Organism-specific databases

CTDi 56603.
GeneCardsi GC02M072356.
HGNCi HGNC:20581. CYP26B1.
HPAi HPA012567.
MIMi 605207. gene.
614416. phenotype.
neXtProti NX_Q9NR63.
Orphaneti 293925. Lethal occipital encephalocele-skeletal dysplasia syndrome.
PharmGKBi PA134879191.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2124.
GeneTreei ENSGT00660000095370.
HOGENOMi HOG000220829.
HOVERGENi HBG051099.
InParanoidi Q9NR63.
KOi K12664.
OMAi WSSQPEA.
OrthoDBi EOG7F24SP.
PhylomeDBi Q9NR63.
TreeFami TF105093.

Enzyme and pathway databases

Reactomei REACT_13450. Vitamins.

Miscellaneous databases

GeneWikii CYP26B1.
GenomeRNAii 56603.
NextBioi 62039.
PROi Q9NR63.
SOURCEi Search...

Gene expression databases

Bgeei Q9NR63.
CleanExi HS_CYP26B1.
ExpressionAtlasi Q9NR63. baseline and differential.
Genevestigatori Q9NR63.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00465. EP450IV.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the human cytochrome P450, P450RAI-2, which is predominantly expressed in the adult cerebellum and is responsible for all-trans-retinoic acid metabolism."
    White J.A., Ramshaw H., Taimi M., Stangle W., Zhang A., Everingham S., Creighton S., Tam S.-P., Jones G., Petkovich M.
    Proc. Natl. Acad. Sci. U.S.A. 97:6403-6408(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Retina.
  2. "A spliced version of the human cytochrome P450 26B1 has an alternative function in retinoic acid metabolism."
    Savenstrand H., Kumawat A., Karlsson M., Eriksson L.A., Sirsjo A., Strid A.
    Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT SER-264.
    Tissue: Vascular smooth muscle.
  3. "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] (ISOFORMS 1; 2 AND 3), VARIANT SER-264.
    Tissue: Brain, Cerebellum and Hippocampus.
  4. SeattleSNPs variation discovery resource
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-181; VAL-185; HIS-191; ASN-227; SER-264; LYS-380; GLY-420; CYS-473 AND ILE-479.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    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).
  7. "Craniosynostosis and multiple skeletal anomalies in humans and zebrafish result from a defect in the localized degradation of retinoic acid."
    Laue K., Pogoda H.M., Daniel P.B., van Haeringen A., Alanay Y., von Ameln S., Rachwalski M., Morgan T., Gray M.J., Breuning M.H., Sawyer G.M., Sutherland-Smith A.J., Nikkels P.G., Kubisch C., Bloch W., Wollnik B., Hammerschmidt M., Robertson S.P.
    Am. J. Hum. Genet. 89:595-606(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, VARIANTS RHFCA PRO-146 AND LEU-363.

Entry informationi

Entry nameiCP26B_HUMAN
AccessioniPrimary (citable) accession number: Q9NR63
Secondary accession number(s): B2R8M7
, B7Z2K6, B7Z2P4, B7Z3B8, E4W5W7, Q32MC0, Q53TW1, Q9NP41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 124 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 2
    Human chromosome 2: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3