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P22392

- NDKB_HUMAN

UniProt

P22392 - NDKB_HUMAN

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Protein

Nucleoside diphosphate kinase B

Gene

NME2

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

Functioni

Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752). Exhibits histidine protein kinase activity.3 Publications

Catalytic activityi

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

Cofactori

Magnesium.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121ATP
Binding sitei60 – 601ATP
Binding sitei88 – 881ATP
Binding sitei94 – 941ATP
Binding sitei105 – 1051ATP
Binding sitei115 – 1151ATP
Active sitei118 – 1181Pros-phosphohistidine intermediate1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. nucleoside diphosphate kinase activity Source: UniProtKB
  5. protein histidine kinase activity Source: UniProtKB-EC
  6. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: HGNC
  2. CTP biosynthetic process Source: InterPro
  3. GTP biosynthetic process Source: InterPro
  4. integrin-mediated signaling pathway Source: UniProtKB
  5. negative regulation of apoptotic process Source: HGNC
  6. nucleobase-containing small molecule interconversion Source: Reactome
  7. nucleobase-containing small molecule metabolic process Source: Reactome
  8. nucleoside triphosphate biosynthetic process Source: UniProtKB
  9. positive regulation of epithelial cell proliferation Source: HGNC
  10. positive regulation of keratinocyte differentiation Source: HGNC
  11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  12. regulation of epidermis development Source: HGNC
  13. regulation of transcription, DNA-templated Source: UniProtKB
  14. small molecule metabolic process Source: Reactome
  15. transcription, DNA-templated Source: UniProtKB-KW
  16. UTP biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Activator, Kinase, Transferase

Keywords - Biological processi

Nucleotide metabolism, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS04463-MONOMER.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
SignaLinkiP22392.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoside diphosphate kinase B (EC:2.7.4.6)
Short name:
NDK B
Short name:
NDP kinase B
Alternative name(s):
C-myc purine-binding transcription factor PUF
Histidine protein kinase NDKB (EC:2.7.13.3)
nm23-H2
Gene namesi
Name:NME2
Synonyms:NM23B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:7850. NME2.

Subcellular locationi

Cytoplasm. Nucleus. Cell projectionlamellipodium. Cell projectionruffle
Note: Isoform 2 is mainly cytoplasmic and isoform 1 and isoform 2 are excluded from the nucleolus. Colocalizes with ITGB1 and ITGB1BP1 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen but not on vitronectin or laminin substrates.

GO - Cellular componenti

  1. cell periphery Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. lamellipodium Source: HGNC
  6. nucleus Source: UniProt
  7. ruffle Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162398077.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 152151Nucleoside diphosphate kinase BPRO_0000137117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei128 – 1281N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP22392.
PRIDEiP22392.

2D gel databases

DOSAC-COBS-2DPAGEP22392.
OGPiP22392.
UCD-2DPAGEP22392.

PTM databases

PhosphoSiteiP22392.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiP22392.
ExpressionAtlasiP22392. baseline.
GenevestigatoriP22392.

Organism-specific databases

HPAiCAB002169.
CAB040571.
HPA008467.
HPA041113.

Interactioni

Subunit structurei

Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with CAPN8 (By similarity). Interacts with AKAP13. Interacts ITGB1BP1 (via C-terminal domain region).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB1BP1O14713-17EBI-713693,EBI-2127367
NME1P155312EBI-713693,EBI-741141

Protein-protein interaction databases

BioGridi110895. 44 interactions.
576341. 8 interactions.
IntActiP22392. 18 interactions.
MINTiMINT-1429922.
STRINGi9606.ENSP00000376886.

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 116
Helixi13 – 175
Helixi21 – 3111
Beta strandi34 – 418
Helixi45 – 517
Helixi53 – 553
Helixi61 – 688
Beta strandi73 – 808
Helixi83 – 919
Helixi96 – 983
Helixi104 – 1085
Helixi112 – 1143
Beta strandi117 – 1193
Helixi123 – 13311
Helixi136 – 1383
Helixi147 – 1504

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NSKX-ray2.80L/N/O/R/T/U1-152[»]
1NUEX-ray2.00A/B/C/D/E/F2-152[»]
3BBBX-ray1.30A/B/C/D/E/F2-152[»]
3BBCX-ray1.70A/B/C/D/E/F2-152[»]
3BBFX-ray1.70A/B/C/D/E/F2-152[»]
ProteinModelPortaliP22392.
SMRiP22392. Positions 2-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22392.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 6665Interaction with AKAP13Add
BLAST

Sequence similaritiesi

Belongs to the NDK family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119146.
HOGENOMiHOG000224564.
HOVERGENiHBG000423.
InParanoidiP22392.
KOiK00940.
OrthoDBiEOG7GJ6FG.
PhylomeDBiP22392.
TreeFamiTF106373.

Family and domain databases

Gene3Di3.30.70.141. 1 hit.
HAMAPiMF_00451. NDP_kinase.
InterProiIPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view]
PfamiPF00334. NDK. 1 hit.
[Graphical view]
PRINTSiPR01243. NUCDPKINASE.
SMARTiSM00562. NDK. 1 hit.
[Graphical view]
SUPFAMiSSF54919. SSF54919. 1 hit.
PROSITEiPS00469. NDP_KINASES. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P22392-1) [UniParc]FASTAAdd to Basket

Also known as: NM23-H2

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
MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ
60 70 80 90 100
HYIDLKDRPF FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK
110 120 130 140 150
PGTIRGDFCI QVGRNIIHGS DSVKSAEKEI SLWFKPEELV DYKSCAHDWV

YE
Length:152
Mass (Da):17,298
Last modified:August 1, 1991 - v1
Checksum:i1A5C3F84D7AD272C
GO
Isoform 3 (identifier: P22392-2) [UniParc]FASTAAdd to Basket

Also known as: NM23-LV

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MANCERTFIA...DFCIQVGRTM

Note: Based on a naturally occurring readthrough transcript which produces an NME1-NME2 fusion protein. Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity).By similarity

Show »
Length:267
Mass (Da):30,137
Checksum:i3AB02272AF24AAC3
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MANCERTFIAIKPDGVQRGL VGEIIKRFEQKGFRLVGLKF MQASEDLLKEHYVDLKDRPF FAGLVKYMHSGPVVAMVWEG LNVVKTGRVMLGETNPADSK PGTIRGDFCIQVGRTM in isoform 3. 2 PublicationsVSP_036708

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58965 mRNA. Translation: CAB37870.1.
M36981 mRNA. Translation: AAA36369.1.
L16785 mRNA. Translation: AAA60228.1.
DQ109675 mRNA. Translation: AAZ82097.1.
AC005839 Genomic DNA. No translation available.
BC002476 mRNA. Translation: AAH02476.1.
BC133029 mRNA. Translation: AAI33030.1.
BC133031 mRNA. Translation: AAI33032.1.
U29200 Genomic DNA. Translation: AAA86745.1.
CCDSiCCDS11580.1. [P22392-1]
PIRiA49798.
RefSeqiNP_001018146.1. NM_001018136.2. [P22392-2]
NP_001018147.1. NM_001018137.2. [P22392-1]
NP_001018148.1. NM_001018138.1. [P22392-1]
NP_001018149.1. NM_001018139.2. [P22392-1]
NP_002503.1. NM_002512.3. [P22392-1]
UniGeneiHs.463456.

Genome annotation databases

EnsembliENST00000393193; ENSP00000376889; ENSG00000011052. [P22392-2]
GeneIDi4831.
654364.
KEGGihsa:4831.
hsa:654364.
UCSCiuc002itj.3. human. [P22392-2]
uc002itl.3. human. [P22392-1]

Polymorphism databases

DMDMi127983.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X58965 mRNA. Translation: CAB37870.1 .
M36981 mRNA. Translation: AAA36369.1 .
L16785 mRNA. Translation: AAA60228.1 .
DQ109675 mRNA. Translation: AAZ82097.1 .
AC005839 Genomic DNA. No translation available.
BC002476 mRNA. Translation: AAH02476.1 .
BC133029 mRNA. Translation: AAI33030.1 .
BC133031 mRNA. Translation: AAI33032.1 .
U29200 Genomic DNA. Translation: AAA86745.1 .
CCDSi CCDS11580.1. [P22392-1 ]
PIRi A49798.
RefSeqi NP_001018146.1. NM_001018136.2. [P22392-2 ]
NP_001018147.1. NM_001018137.2. [P22392-1 ]
NP_001018148.1. NM_001018138.1. [P22392-1 ]
NP_001018149.1. NM_001018139.2. [P22392-1 ]
NP_002503.1. NM_002512.3. [P22392-1 ]
UniGenei Hs.463456.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NSK X-ray 2.80 L/N/O/R/T/U 1-152 [» ]
1NUE X-ray 2.00 A/B/C/D/E/F 2-152 [» ]
3BBB X-ray 1.30 A/B/C/D/E/F 2-152 [» ]
3BBC X-ray 1.70 A/B/C/D/E/F 2-152 [» ]
3BBF X-ray 1.70 A/B/C/D/E/F 2-152 [» ]
ProteinModelPortali P22392.
SMRi P22392. Positions 2-152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110895. 44 interactions.
576341. 8 interactions.
IntActi P22392. 18 interactions.
MINTi MINT-1429922.
STRINGi 9606.ENSP00000376886.

Chemistry

ChEMBLi CHEMBL2160.
DrugBanki DB00718. Adefovir Dipivoxil.
DB00709. Lamivudine.
DB00300. Tenofovir.

PTM databases

PhosphoSitei P22392.

Polymorphism databases

DMDMi 127983.

2D gel databases

DOSAC-COBS-2DPAGE P22392.
OGPi P22392.
UCD-2DPAGE P22392.

Proteomic databases

MaxQBi P22392.
PRIDEi P22392.

Protocols and materials databases

DNASUi 4831.
654364.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000393193 ; ENSP00000376889 ; ENSG00000011052 . [P22392-2 ]
GeneIDi 4831.
654364.
KEGGi hsa:4831.
hsa:654364.
UCSCi uc002itj.3. human. [P22392-2 ]
uc002itl.3. human. [P22392-1 ]

Organism-specific databases

CTDi 4831.
654364.
GeneCardsi GC17P049230.
GC17P049242.
HGNCi HGNC:7850. NME2.
HPAi CAB002169.
CAB040571.
HPA008467.
HPA041113.
MIMi 156491. gene.
neXtProti NX_P22392.
PharmGKBi PA162398077.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00760000119146.
HOGENOMi HOG000224564.
HOVERGENi HBG000423.
InParanoidi P22392.
KOi K00940.
OrthoDBi EOG7GJ6FG.
PhylomeDBi P22392.
TreeFami TF106373.

Enzyme and pathway databases

BioCyci MetaCyc:HS04463-MONOMER.
Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
SignaLinki P22392.

Miscellaneous databases

ChiTaRSi NME2. human.
EvolutionaryTracei P22392.
GeneWikii NME1-NME2.
NME2.
NextBioi 18612.
PROi P22392.
SOURCEi Search...

Gene expression databases

Bgeei P22392.
ExpressionAtlasi P22392. baseline.
Genevestigatori P22392.

Family and domain databases

Gene3Di 3.30.70.141. 1 hit.
HAMAPi MF_00451. NDP_kinase.
InterProi IPR001564. Nucleoside_diP_kinase.
IPR023005. Nucleoside_diP_kinase_AS.
[Graphical view ]
Pfami PF00334. NDK. 1 hit.
[Graphical view ]
PRINTSi PR01243. NUCDPKINASE.
SMARTi SM00562. NDK. 1 hit.
[Graphical view ]
SUPFAMi SSF54919. SSF54919. 1 hit.
PROSITEi PS00469. NDP_KINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a second human nm23 gene, nm23-H2."
    Stahl J.A., Leone A., Rosengard A.M., Porter L., Liotta L.A., Steeg P.S., King C.R.
    Cancer Res. 51:445-449(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme."
    Gilles A.-M., Presecan E., Vonica A., Lascu I.
    J. Biol. Chem. 266:8784-8789(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (ISOFORM 1), SUBUNIT, ACTIVE SITE.
  3. "Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis."
    Postel E.H., Berberich S.J., Flint S.J., Ferrone C.A.
    Science 261:478-480(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV."
    Valentijn L.J., Koster J., Versteeg R.
    Genomics 87:483-489(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Neuroblastoma.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [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] (ISOFORMS 1 AND 3).
    Tissue: Eye.
  7. "Characterization of the human nm23-H2 promoter region and localization of the microsatellite D17S396."
    Seifert M., Seib T., Engel M., Dooley S., Welter C.
    Biochem. Biophys. Res. Commun. 215:910-914(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
  8. "Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement."
    Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C., Block M.R., Albiges-Rizo C.
    J. Biol. Chem. 277:20895-20902(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITGB1BP1, SUBCELLULAR LOCATION.
  9. "Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2."
    Iwashita S., Fujii M., Mukai H., Ono Y., Miyamoto M.
    Biochem. Biophys. Res. Commun. 320:1063-1068(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AKAP13.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Reversible histidine phosphorylation in mammalian cells: a teeter-totter formed by nucleoside diphosphate kinase and protein histidine phosphatase 1."
    Wieland T., Hippe H.J., Ludwig K., Zhou X.B., Korth M., Klumpp S.
    Methods Enzymol. 471:379-402(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS HISTIDINE PROTEIN KINASE.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The crystal structure of a human nucleoside diphosphate kinase, NM23-H2."
    Webb P.A., Perisic O., Mendola C.E., Backer J.M., Williams R.L.
    J. Mol. Biol. 251:574-587(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  15. "X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2-A resolution."
    Morera S., Lacombe M.-L., Xu Y., Lebras G., Janin J.
    Structure 3:1307-1314(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).

Entry informationi

Entry nameiNDKB_HUMAN
AccessioniPrimary (citable) accession number: P22392
Secondary accession number(s): A8MWA3, Q1WM23, Q6LCT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 29, 2014
This is version 178 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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