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O60238

- BNI3L_HUMAN

UniProt

O60238 - BNI3L_HUMAN

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Protein

BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like

Gene

BNIP3L

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

Functioni

Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates to mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor.2 Publications

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. lamin binding Source: UniProtKB
  3. protein heterodimerization activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. defense response to virus Source: UniProtKB
  2. mitochondrial outer membrane permeabilization Source: RefGenome
  3. mitochondrial protein catabolic process Source: UniProtKB
  4. negative regulation of apoptotic process Source: UniProtKB
  5. positive regulation of apoptotic process Source: UniProtKB
  6. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Host-virus interaction

Protein family/group databases

TCDBi1.A.20.1.2. the bcl2/adenovirus e1b-interacting protein 3 (bnip3) family.

Names & Taxonomyi

Protein namesi
Recommended name:
BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
Alternative name(s):
Adenovirus E1B19K-binding protein B5
BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A
NIP3-like protein X
Short name:
NIP3L
Gene namesi
Name:BNIP3L
Synonyms:BNIP3A, BNIP3H, NIX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:1085. BNIP3L.

Subcellular locationi

Nucleus envelope. Endoplasmic reticulum. Mitochondrion outer membrane. Membrane Curated; Single-pass membrane protein Curated
Note: Colocalizes with SPATA18 at the mitochondrion outer membrane.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei188 – 20821HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. endoplasmic reticulum Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. intrinsic component of membrane Source: UniProtKB
  5. mitochondrial outer membrane Source: UniProtKB
  6. mitochondrion Source: UniProtKB
  7. nuclear envelope Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25395.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-likePRO_0000064957Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621PhosphoserineBy similarity
Modified residuei117 – 1171PhosphoserineBy similarity
Modified residuei118 – 1181PhosphoserineBy similarity
Modified residuei120 – 1201Phosphoserine1 Publication

Post-translational modificationi

Undergoes progressive proteolysis to an 11 kDa C-terminal fragment, which is blocked by the proteasome inhibitor lactacystin.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO60238.
PaxDbiO60238.
PRIDEiO60238.

PTM databases

PhosphoSiteiO60238.

Expressioni

Gene expression databases

BgeeiO60238.
CleanExiHS_BNIP3L.
ExpressionAtlasiO60238. baseline and differential.
GenevestigatoriO60238.

Organism-specific databases

HPAiCAB025371.
HPA015652.

Interactioni

Subunit structurei

Self-associates. Interacts with BNIP3 and STEAP3. Interacts with human adenovirus-2 E1B 19 kDa protein. Interacts (via BH3 domain) with SPATA18 (via coiled-coil domains).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself8EBI-849893,EBI-849893
ATP13A2Q9NQ112EBI-849893,EBI-6308763
BADQ929342EBI-849893,EBI-700771
BCL2P104152EBI-849893,EBI-77694
BNIP3Q129839EBI-849893,EBI-749464
E1BP032477EBI-849893,EBI-849856From a different organism.

Protein-protein interaction databases

BioGridi107133. 27 interactions.
DIPiDIP-35187N.
IntActiO60238. 28 interactions.
MINTiMINT-1429960.
STRINGi9606.ENSP00000370003.

Structurei

3D structure databases

ProteinModelPortaliO60238.
SMRiO60238. Positions 178-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi126 – 14823BH3Add
BLAST

Sequence similaritiesi

Belongs to the NIP3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG83470.
GeneTreeiENSGT00390000013415.
HOVERGENiHBG050707.
InParanoidiO60238.
KOiK15465.
OMAiMVGGLEH.
OrthoDBiEOG74N5J4.
PhylomeDBiO60238.
TreeFamiTF315424.

Family and domain databases

InterProiIPR010548. BNIP3.
[Graphical view]
PfamiPF06553. BNIP3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60238-1) [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
MSSHLVEPPP PLHNNNNNCE ENEQSLPPPA GLNSSWVELP MNSSNGNDNG
60 70 80 90 100
NGKNGGLEHV PSSSSIHNGD MEKILLDAQH ESGQSSSRGS SHCDSPSPQE
110 120 130 140 150
DGQIMFDVEM HTSRDHSSQS EEEVVEGEKE VEALKKSADW VSDWSSRPEN
160 170 180 190 200
IPPKEFHFRH PKRSVSLSMR KSGAMKKGGI FSAEFLKVFI PSLFLSHVLA
210
LGLGIYIGKR LSTPSASTY
Length:219
Mass (Da):23,930
Last modified:August 1, 1998 - v1
Checksum:i19372E897BC63609
GO
Isoform 2 (identifier: O60238-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: Missing.

Note: No experimental confirmation available.

Show »
Length:179
Mass (Da):19,559
Checksum:i3C5A4AA97F65D467
GO

Sequence cautioni

The sequence CAI46217.1 differs from that shown. Reason: Erroneous termination at position 122. Translated as Glu.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071D → E in AAN04051. (PubMed:10381623)Curated
Sequence conflicti150 – 1501N → S in CAI46217. (PubMed:17974005)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4040Missing in isoform 2. 1 PublicationVSP_056248Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004788 mRNA. Translation: BAA28692.1.
AF079221 mRNA. Translation: AAC27723.1.
AF067396 mRNA. Translation: AAD03589.1.
AF536326 mRNA. Translation: AAN04051.1.
AF452712 mRNA. Translation: AAL50978.1.
AF255051 Genomic DNA. Translation: AAF70290.1.
AK315870 mRNA. Translation: BAF98761.1.
AK316315 mRNA. Translation: BAH14686.1.
BT019501 mRNA. Translation: AAV38308.1.
AL132665 mRNA. Translation: CAI46217.1. Sequence problems.
AC011726 Genomic DNA. No translation available.
AC015743 Genomic DNA. No translation available.
AC022911 Genomic DNA. No translation available.
BC001559 mRNA. Translation: AAH01559.1.
BC009603 mRNA. Translation: AAH09603.1.
CCDSiCCDS6050.1. [O60238-1]
PIRiT34523.
RefSeqiNP_004322.1. NM_004331.2. [O60238-1]
XP_005273674.1. XM_005273617.1. [O60238-2]
UniGeneiHs.131226.

Genome annotation databases

EnsembliENST00000380629; ENSP00000370003; ENSG00000104765. [O60238-1]
ENST00000518611; ENSP00000429851; ENSG00000104765. [O60238-2]
ENST00000520409; ENSP00000428597; ENSG00000104765. [O60238-2]
ENST00000523515; ENSP00000429698; ENSG00000104765. [O60238-2]
GeneIDi665.
KEGGihsa:665.
UCSCiuc003xex.1. human. [O60238-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB004788 mRNA. Translation: BAA28692.1 .
AF079221 mRNA. Translation: AAC27723.1 .
AF067396 mRNA. Translation: AAD03589.1 .
AF536326 mRNA. Translation: AAN04051.1 .
AF452712 mRNA. Translation: AAL50978.1 .
AF255051 Genomic DNA. Translation: AAF70290.1 .
AK315870 mRNA. Translation: BAF98761.1 .
AK316315 mRNA. Translation: BAH14686.1 .
BT019501 mRNA. Translation: AAV38308.1 .
AL132665 mRNA. Translation: CAI46217.1 . Sequence problems.
AC011726 Genomic DNA. No translation available.
AC015743 Genomic DNA. No translation available.
AC022911 Genomic DNA. No translation available.
BC001559 mRNA. Translation: AAH01559.1 .
BC009603 mRNA. Translation: AAH09603.1 .
CCDSi CCDS6050.1. [O60238-1 ]
PIRi T34523.
RefSeqi NP_004322.1. NM_004331.2. [O60238-1 ]
XP_005273674.1. XM_005273617.1. [O60238-2 ]
UniGenei Hs.131226.

3D structure databases

ProteinModelPortali O60238.
SMRi O60238. Positions 178-212.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107133. 27 interactions.
DIPi DIP-35187N.
IntActi O60238. 28 interactions.
MINTi MINT-1429960.
STRINGi 9606.ENSP00000370003.

Protein family/group databases

TCDBi 1.A.20.1.2. the bcl2/adenovirus e1b-interacting protein 3 (bnip3) family.

PTM databases

PhosphoSitei O60238.

Proteomic databases

MaxQBi O60238.
PaxDbi O60238.
PRIDEi O60238.

Protocols and materials databases

DNASUi 665.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380629 ; ENSP00000370003 ; ENSG00000104765 . [O60238-1 ]
ENST00000518611 ; ENSP00000429851 ; ENSG00000104765 . [O60238-2 ]
ENST00000520409 ; ENSP00000428597 ; ENSG00000104765 . [O60238-2 ]
ENST00000523515 ; ENSP00000429698 ; ENSG00000104765 . [O60238-2 ]
GeneIDi 665.
KEGGi hsa:665.
UCSCi uc003xex.1. human. [O60238-1 ]

Organism-specific databases

CTDi 665.
GeneCardsi GC08P026240.
HGNCi HGNC:1085. BNIP3L.
HPAi CAB025371.
HPA015652.
MIMi 605368. gene.
neXtProti NX_O60238.
PharmGKBi PA25395.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG83470.
GeneTreei ENSGT00390000013415.
HOVERGENi HBG050707.
InParanoidi O60238.
KOi K15465.
OMAi MVGGLEH.
OrthoDBi EOG74N5J4.
PhylomeDBi O60238.
TreeFami TF315424.

Miscellaneous databases

ChiTaRSi BNIP3L. human.
GeneWikii BNIP3L.
GenomeRNAii 665.
NextBioi 2712.
PROi O60238.
SOURCEi Search...

Gene expression databases

Bgeei O60238.
CleanExi HS_BNIP3L.
ExpressionAtlasi O60238. baseline and differential.
Genevestigatori O60238.

Family and domain databases

InterProi IPR010548. BNIP3.
[Graphical view ]
Pfami PF06553. BNIP3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, mapping, and functional analysis of a novel human cDNA (BNIP3L) encoding a protein homologous to human NIP3."
    Matsushima M., Fujiwara T., Takahashi E., Minaguchi T., Eguchi Y., Tsujimoto Y., Suzumori K., Nakamura Y.
    Genes Chromosomes Cancer 21:230-235(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "BNIP3a, a human homolog of pro-apoptotic protein BNIP3, promotes apoptosis and interacts with viral and cellular anti-apoptosis proteins."
    Yasuda M., Han J.-W., Dionne C.A., Boyd J.M., Chinnadurai G.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins."
    Chen G., Cizeau J., Vande Velde C., Park J.H., Bozek G., Bolton J., Shi L., Dubik D., Greenberg A.
    J. Biol. Chem. 274:7-10(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal liver.
  4. "A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region."
    Ohi N., Tokunaga A., Tsunoda H., Nakano K., Haraguchi K., Oda K., Motoyama N., Nakajima T.
    Cell Death Differ. 6:314-325(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, SELF-ASSOCIATION, INTERACTION WITH BNIP3 AND HUMAN ADENOVIRUS-2 E1B 19 KDA PROTEIN.
  5. "The proapoptotic factor Nix is coexpressed with Bcl-xL during terminal erythroid differentiation."
    Aerbajinai W., Giattina M., Lee Y.T., Raffeld M., Miller J.L.
    Blood 102:712-717(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  6. "A catalog of genes in the human dermal papilla cells as identified by expressed sequence tags."
    Farooq M., Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Sohn M.Y., Hwang S.Y., Chung H.J., Im S.U., Jung E.J., Kim J.C.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Hair follicle dermal papilla.
  7. "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 2).
    Tissue: Brain.
  8. "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] (ISOFORM 1).
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  10. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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).
    Tissue: Bone marrow and Cervix.
  12. Cited for: INTERACTION WITH STEAP3.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Mieap, a p53-inducible protein, controls mitochondrial quality by repairing or eliminating unhealthy mitochondria."
    Kitamura N., Nakamura Y., Miyamoto Y., Miyamoto T., Kabu K., Yoshida M., Futamura M., Ichinose S., Arakawa H.
    PLoS ONE 6:E16060-E16060(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SPATA18, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiBNI3L_HUMAN
AccessioniPrimary (citable) accession number: O60238
Secondary accession number(s): B0AZS9, Q5JW63, Q8NF87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: November 26, 2014
This is version 134 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 8
    Human chromosome 8: 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