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O75436

- VP26A_HUMAN

UniProt

O75436 - VP26A_HUMAN

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Protein
Vacuolar protein sorting-associated protein 26A
Gene
VPS26A, VPS26
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Essential component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Also required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA).2 Publications

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. protein transporter activity Source: UniProtKB

GO - Biological processi

  1. retrograde transport, endosome to Golgi Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein sorting-associated protein 26A
Alternative name(s):
Vesicle protein sorting 26A
Short name:
hVPS26
Gene namesi
Name:VPS26A
Synonyms:VPS26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:12711. VPS26A.

Subcellular locationi

Cytoplasm. Endosome membrane; Peripheral membrane protein 3 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. endosome Source: UniProtKB
  3. endosome membrane Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProt
  5. intracellular membrane-bounded organelle Source: HPA
  6. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi235 – 2362IM → DD: Abolishes interaction with VPS35 and endosomal subcellular location. 1 Publication

Organism-specific databases

PharmGKBiPA37326.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 327327Vacuolar protein sorting-associated protein 26A
PRO_0000073007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei315 – 3151Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75436.
PaxDbiO75436.
PeptideAtlasiO75436.
PRIDEiO75436.

PTM databases

PhosphoSiteiO75436.

Expressioni

Inductioni

Down-regulated in Alzheimer disease. No polymorphism or variant is however associated with Alzheimer disease for VPS26A.2 Publications

Gene expression databases

ArrayExpressiO75436.
BgeeiO75436.
CleanExiHS_VPS26A.
GenevestigatoriO75436.

Organism-specific databases

HPAiCAB011602.
HPA044581.

Interactioni

Subunit structurei

Component of the retromer complex composed of VPS26 (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts directly with VPS35. Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with ECM29.5 Publications

Protein-protein interaction databases

BioGridi114930. 58 interactions.
DIPiDIP-29075N.
IntActiO75436. 2 interactions.
MINTiMINT-5000831.
STRINGi9606.ENSP00000263559.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 115
Beta strandi12 – 187
Helixi21 – 233
Beta strandi26 – 305
Beta strandi36 – 427
Beta strandi48 – 6013
Beta strandi63 – 664
Beta strandi68 – 7811
Beta strandi85 – 9612
Beta strandi98 – 1014
Beta strandi105 – 1117
Beta strandi124 – 13613
Beta strandi139 – 1413
Beta strandi143 – 1519
Beta strandi164 – 1707
Turni171 – 1733
Beta strandi174 – 1818
Beta strandi183 – 1864
Beta strandi190 – 20011
Beta strandi204 – 21815
Helixi220 – 2223
Beta strandi224 – 23411
Beta strandi246 – 2527
Turni253 – 2553
Beta strandi261 – 2655
Beta strandi268 – 28013
Beta strandi285 – 29511

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FAUX-ray2.10A1-327[»]
ProteinModelPortaliO75436.
SMRiO75436. Positions 6-299.

Miscellaneous databases

EvolutionaryTraceiO75436.

Family & Domainsi

Sequence similaritiesi

Belongs to the VPS26 family.

Phylogenomic databases

eggNOGiNOG256244.
HOGENOMiHOG000191799.
HOVERGENiHBG082914.
InParanoidiO75436.
OMAiPVCEIDV.
OrthoDBiEOG7NW699.
PhylomeDBiO75436.
TreeFamiTF300907.

Family and domain databases

InterProiIPR028934. Vps26-related.
[Graphical view]
PfamiPF03643. Vps26. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75436-1) [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

MSFLGGFFGP ICEIDIVLND GETRKMAEMK TEDGKVEKHY LFYDGESVSG    50
KVNLAFKQPG KRLEHQGIRI EFVGQIELFN DKSNTHEFVN LVKELALPGE 100
LTQSRSYDFE FMQVEKPYES YIGANVRLRY FLKVTIVRRL TDLVKEYDLI 150
VHQLATYPDV NNSIKMEVGI EDCLHIEFEY NKSKYHLKDV IVGKIYFLLV 200
RIKIQHMELQ LIKKEITGIG PSTTTETETI AKYEIMDGAP VKGESIPIRL 250
FLAGYDPTPT MRDVNKKFSV RYFLNLVLVD EEDRRYFKQQ EIILWRKAPE 300
KLRKQRTNFH QRFESPESQA SAEQPEM 327
Length:327
Mass (Da):38,170
Last modified:November 25, 2002 - v2
Checksum:iBD3B2EAA6CFCBFA9
GO
Isoform 2 (identifier: O75436-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     243-327: GESIPIRLFL...SQASAEQPEM → GDNFMEKSS

Note: No experimental confirmation available.

Show »
Length:251
Mass (Da):28,938
Checksum:i1140DC4C2D80D257
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei243 – 32785GESIP…EQPEM → GDNFMEKSS in isoform 2.
VSP_044910Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751Q → R in BAB14351. 1 Publication
Sequence conflicti242 – 2421K → Q in BQ048905. 1 Publication
Sequence conflicti285 – 2862RY → SS in AAF89954. 1 Publication
Sequence conflicti285 – 2862RY → SS in AAC39912. 1 Publication
Isoform 2 (identifier: O75436-2)
Sequence conflicti243 – 2431G → R in BQ048905. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF175266 mRNA. Translation: AAF89954.1.
AF054179 mRNA. Translation: AAC39912.1.
AK022992 mRNA. Translation: BAB14351.1.
AK315496 mRNA. Translation: BAG37880.1.
AL596223, AL442635 Genomic DNA. Translation: CAH71501.1.
AL442635, AL596223 Genomic DNA. Translation: CAH71779.1.
CH471083 Genomic DNA. Translation: EAW54313.1.
BC022505 mRNA. Translation: AAH22505.1.
BQ048905 mRNA. No translation available.
CCDSiCCDS41536.1. [O75436-2]
CCDS7286.1. [O75436-1]
RefSeqiNP_001030337.1. NM_001035260.1. [O75436-2]
NP_004887.2. NM_004896.3. [O75436-1]
UniGeneiHs.499925.

Genome annotation databases

EnsembliENST00000263559; ENSP00000263559; ENSG00000122958. [O75436-1]
ENST00000373382; ENSP00000362480; ENSG00000122958. [O75436-1]
ENST00000395098; ENSP00000378532; ENSG00000122958. [O75436-2]
GeneIDi9559.
KEGGihsa:9559.
UCSCiuc001jpb.3. human. [O75436-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF175266 mRNA. Translation: AAF89954.1 .
AF054179 mRNA. Translation: AAC39912.1 .
AK022992 mRNA. Translation: BAB14351.1 .
AK315496 mRNA. Translation: BAG37880.1 .
AL596223 , AL442635 Genomic DNA. Translation: CAH71501.1 .
AL442635 , AL596223 Genomic DNA. Translation: CAH71779.1 .
CH471083 Genomic DNA. Translation: EAW54313.1 .
BC022505 mRNA. Translation: AAH22505.1 .
BQ048905 mRNA. No translation available.
CCDSi CCDS41536.1. [O75436-2 ]
CCDS7286.1. [O75436-1 ]
RefSeqi NP_001030337.1. NM_001035260.1. [O75436-2 ]
NP_004887.2. NM_004896.3. [O75436-1 ]
UniGenei Hs.499925.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FAU X-ray 2.10 A 1-327 [» ]
ProteinModelPortali O75436.
SMRi O75436. Positions 6-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114930. 58 interactions.
DIPi DIP-29075N.
IntActi O75436. 2 interactions.
MINTi MINT-5000831.
STRINGi 9606.ENSP00000263559.

PTM databases

PhosphoSitei O75436.

Proteomic databases

MaxQBi O75436.
PaxDbi O75436.
PeptideAtlasi O75436.
PRIDEi O75436.

Protocols and materials databases

DNASUi 9559.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263559 ; ENSP00000263559 ; ENSG00000122958 . [O75436-1 ]
ENST00000373382 ; ENSP00000362480 ; ENSG00000122958 . [O75436-1 ]
ENST00000395098 ; ENSP00000378532 ; ENSG00000122958 . [O75436-2 ]
GeneIDi 9559.
KEGGi hsa:9559.
UCSCi uc001jpb.3. human. [O75436-1 ]

Organism-specific databases

CTDi 9559.
GeneCardsi GC10P070885.
HGNCi HGNC:12711. VPS26A.
HPAi CAB011602.
HPA044581.
MIMi 605506. gene.
neXtProti NX_O75436.
PharmGKBi PA37326.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG256244.
HOGENOMi HOG000191799.
HOVERGENi HBG082914.
InParanoidi O75436.
OMAi PVCEIDV.
OrthoDBi EOG7NW699.
PhylomeDBi O75436.
TreeFami TF300907.

Enzyme and pathway databases

Reactomei REACT_163710. WNT ligand biogenesis and trafficking.

Miscellaneous databases

ChiTaRSi VPS26A. human.
EvolutionaryTracei O75436.
GeneWikii VPS26A.
GenomeRNAii 9559.
NextBioi 35853.
PROi O75436.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75436.
Bgeei O75436.
CleanExi HS_VPS26A.
Genevestigatori O75436.

Family and domain databases

InterProi IPR028934. Vps26-related.
[Graphical view ]
Pfami PF03643. Vps26. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes."
    Renfrew Haft C., de la Luz Sierra M., Bafford R., Lesniak M.A., Barr V.A., Taylor S.I.
    Mol. Biol. Cell 11:4105-4116(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH VPS29; VPS35; SNX1 AND SNX2.
    Tissue: Colon.
  2. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
    Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
    Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  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] (ISOFORM 1).
    Tissue: Tongue.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-249 (ISOFORM 2).
    Tissue: Brain and Embryonic testis carcinoma.
  7. "Exportin 7 defines a novel general nuclear export pathway."
    Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.
    EMBO J. 23:3227-3236(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS29; VPS35 AND SFN.
  8. "The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor."
    Verges M., Luton F., Gruber C., Tiemann F., Reinders L.G., Huang L., Burlingame A.L., Haft C.R., Mostov K.E.
    Nat. Cell Biol. 6:763-769(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Model-guided microarray implicates the retromer complex in Alzheimer's disease."
    Small S.A., Kent K., Pierce A., Leung C., Kang M.S., Okada H., Honig L., Vonsattel J.-P., Kim T.-W.
    Ann. Neurol. 58:909-919(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VPS35.
  11. "An essential role for SNX1 in lysosomal sorting of protease-activated receptor-1: evidence for retromer-, Hrs-, and Tsg101-independent functions of sorting nexins."
    Gullapalli A., Wolfe B.L., Griffin C.T., Magnuson T., Trejo J.
    Mol. Biol. Cell 17:1228-1238(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "No association of vacuolar protein sorting 26 polymorphisms with Alzheimer's disease."
    Riemenschneider M., Schoepfer-Wendels A., Friedrich P., Konta L., Laws S.M., Mueller J.C., Kurz A., Forstl H.
    Neurobiol. Aging 28:883-884(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
    Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
    J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.
  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-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain."
    Shi H., Rojas R., Bonifacino J.S., Hurley J.H.
    Nat. Struct. Mol. Biol. 13:540-548(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBCELLULAR LOCATION, INTERACTION WITH VPS35, MUTAGENESIS OF 236-ILE-MET-237.

Entry informationi

Entry nameiVP26A_HUMAN
AccessioniPrimary (citable) accession number: O75436
Secondary accession number(s): A8MZ56
, B2RDD3, Q8TBH4, Q9H982
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 25, 2002
Last modified: September 3, 2014
This is version 126 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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