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Q9NZ56

- FMN2_HUMAN

UniProt

Q9NZ56 - FMN2_HUMAN

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Protein

Formin-2

Gene
FMN2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis By similarity. Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation.2 Publications

GO - Molecular functioni

  1. actin binding Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. cellular response to hypoxia Source: UniProtKB
  3. establishment of meiotic spindle localization Source: BHF-UCL
  4. formin-nucleated actin cable assembly Source: UniProtKB
  5. homologous chromosome movement towards spindle pole involved in homologous chromosome segregation Source: BHF-UCL
  6. intracellular signal transduction Source: InterPro
  7. intracellular transport Source: UniProtKB
  8. multicellular organismal development Source: UniProtKB-KW
  9. negative regulation of apoptotic process Source: UniProtKB
  10. negative regulation of protein catabolic process Source: UniProtKB
  11. oogenesis Source: BHF-UCL
  12. polar body extrusion after meiotic divisions Source: BHF-UCL
  13. protein transport Source: UniProtKB-KW
  14. vesicle-mediated transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

DNA damage, Protein transport, Stress response, Transport

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

SignaLinkiQ9NZ56.

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-2
Gene namesi
Name:FMN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14074. FMN2.

Subcellular locationi

Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Cytoplasmcytosol. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmcell cortex By similarity. Nucleusnucleolus
Note: Recruited to the membranes via its interaction with SPIRE1. Colocalizes with the actin cytoskeleton. Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion By similarity.2 Publications

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cytoplasmic vesicle membrane Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-SubCell
  4. cytosol Source: UniProtKB
  5. nucleolus Source: UniProtKB
  6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  7. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1715 – 17151K → A or E: Abolishes interaction with SPIRE1. 1 Publication
Mutagenesisi1717 – 17171K → A: Strongly reduces interaction with SPIRE1. 1 Publication
Mutagenesisi1721 – 17211K → A or E: Strongly reduces interaction with SPIRE1. 1 Publication

Organism-specific databases

PharmGKBiPA28185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17221722Formin-2PRO_0000194888Add
BLAST

Proteomic databases

MaxQBiQ9NZ56.
PaxDbiQ9NZ56.
PRIDEiQ9NZ56.

PTM databases

PhosphoSiteiQ9NZ56.

Expressioni

Tissue specificityi

Expressed almost exclusively in the developing and mature central nervous system.1 Publication

Inductioni

Up-regulated in response to cellular stress, hypoxia and DNA damage via NF-kappa-B.1 Publication

Gene expression databases

ArrayExpressiQ9NZ56.
BgeeiQ9NZ56.
CleanExiHS_FMN2.
GenevestigatoriQ9NZ56.

Organism-specific databases

HPAiHPA004937.

Interactioni

Subunit structurei

Interacts with SPIRE1. Binds actin. Interacts with CDKN1A.4 Publications

Protein-protein interaction databases

STRINGi9606.ENSP00000318884.

Structurei

Secondary structure

1
1722
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1706 – 17083
Helixi1714 – 17196

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YLEX-ray1.80B1694-1722[»]
3R7GX-ray2.20B1701-1722[»]
ProteinModelPortaliQ9NZ56.
SMRiQ9NZ56. Positions 1308-1699.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini758 – 1268511FH1Add
BLAST
Domaini1283 – 1698416FH2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1715 – 17228Important for interaction with SPIRE1

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili193 – 23139 Reviewed predictionAdd
BLAST
Coiled coili670 – 70637 Reviewed predictionAdd
BLAST
Coiled coili1567 – 159731 Reviewed predictionAdd
BLAST
Coiled coili1677 – 169923 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi200 – 22728Gln-richAdd
BLAST
Compositional biasi758 – 1268511Pro-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG264408.
HOGENOMiHOG000112618.
HOVERGENiHBG107923.
InParanoidiQ9NZ56.
KOiK02184.
OMAiEHRPKDA.
OrthoDBiEOG78M01H.
PhylomeDBiQ9NZ56.
TreeFamiTF326072.

Family and domain databases

InterProiIPR000591. DEP_dom.
IPR015425. FH2_Formin.
IPR009408. Formin_homology_1.
[Graphical view]
PfamiPF06346. Drf_FH1. 4 hits.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
PROSITEiPS51444. FH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NZ56-1 [UniParc]FASTAAdd to Basket

« Hide

MGNQDGKLKR SAGDALHEGG GGAEDALGPR DVEATKKGSG GKKALGKHGK     50
GGGGGGGGGE SGKKKSKSDS RASVFSNLRI RKNLSKGKGA GGSREDVLDS 100
QALQTGELDS AHSLLTKTPD LSLSADEAGL SDTECADPFE VTGPGGPGPA 150
EARVGGRPIA EDVETAAGAQ DGQRTSSGSD TDIYSFHSAT EQEDLLSDIQ 200
QAIRLQQQQQ QQLQLQLQQQ QQQQQLQGAE EPAAPPTAVS PQPGAFLGLD 250
RFLLGPSGGA GEAPGSPDTE QALSALSDLP ESLAAEPREP QQPPSPGGLP 300
VSEAPSLPAA QPAAKDSPSS TAFPFPEAGP GEEAAGAPVR GAGDTDEEGE 350
EDAFEDAPRG SPGEEWAPEV GEDAPQRLGE EPEEEAQGPD APAAASLPGS 400
PAPSQRCFKP YPLITPCYIK TTTRQLSSPN HSPSQSPNQS PRIKRRPEPS 450
LSRGSRTALA SVAAPAKKHR ADGGLAAGLS RSADWTEELG ARTPRVGGSA 500
HLLERGVASD SGGGVSPALA AKASGAPAAA DGFQNVFTGR TLLEKLFSQQ 550
ENGPPEEAEK FCSRIIAMGL LLPFSDCFRE PCNQNAQTNA ASFDQDQLYT 600
WAAVSQPTHS LDYSEGQFPR RVPSMGPPSK PPDEEHRLED AETESQSAVS 650
ETPQKRSDAV QKEVVDMKSE GQATVIQQLE QTIEDLRTKI AELERQYPAL 700
DTEVASGHQG LENGVTASGD VCLEALRLEE KEVRHHRILE AKSIQTSPTE 750
EGGVLTLPPV DGLPGRPPCP PGAESGPQTK FCSEISLIVS PRRISVQLDS 800
HQPTQSISQP PPPPSLLWSA GQGQPGSQPP HSISTEFQTS HEHSVSSAFK 850
NSCNIPSPPP LPCTESSSSM PGLGMVPPPP PPLPGMTVPT LPSTAIPQPP 900
PLQGTEMLPP PPPPLPGAGI PPPPPLPGAG ILPLPPLPGA GIPPPPPLPG 950
AAIPPPPPLP GAGIPLPPPL PGAGIPPPPP LPGAGIPPPP PLPGAGIPPP 1000
PPLPGAGIPP PPPLPGAGIP PPPPLPGAGI PPPPPLPGAG IPPPPPLPGA 1050
GIPPPPPLPG AGIPPPPPLP GAGIPPPPPL PGAGIPPPPP LPGAGIPPPP 1100
PLPGVGIPPP PPLPGAGIPP PPPLPGAGIP PPPPLPGAGI PPPPPLPRVG 1150
IPPPPPLPGA GIPPPPPLPG AGIPPPPPLP GVGIPPPPPL PGVGIPPPPP 1200
LPGAGIPPPP PLPGMGIPPA PAPPLPPPGT GIPPPPLLPV SGPPLLPQVG 1250
SSTLPTPQVC GFLPPPLPSG LFGLGMNQDK GSRKQPIEPC RPMKPLYWTR 1300
IQLHSKRDSS TSLIWEKIEE PSIDCHEFEE LFSKTAVKER KKPISDTISK 1350
TKAKQVVKLL SNKRSQAVGI LMSSLHLDMK DIQHAVVNLD NSVVDLETLQ 1400
ALYENRAQSD ELEKIEKHGR SSKDKENAKS LDKPEQFLYE LSLIPNFSER 1450
VFCILFQSTF SESICSIRRK LELLQKLCET LKNGPGVMQV LGLVLAFGNY 1500
MNGGNKTRGQ ADGFGLDILP KLKDVKSSDN SRSLLSYIVS YYLRNFDEDA 1550
GKEQCLFPLP EPQDLFQASQ MKFEDFQKDL RKLKKDLKAC EVEAGKVYQV 1600
SSKEHMQPFK ENMEQFIIQA KIDQEAEENS LTETHKCFLE TTAYFFMKPK 1650
LGEKEVSPNA FFSIWHEFSS DFKDFWKKEN KLLLQERVKE AEEVCRQKKG 1700
KSLYKIKPRH DSGIKAKISM KT 1722
Length:1,722
Mass (Da):180,106
Last modified:January 15, 2008 - v4
Checksum:i26525AC7868A949C
GO

Sequence cautioni

The sequence AAF72884.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1148 – 11481R → G.1 Publication
Corresponds to variant rs12732924 [ dbSNP | Ensembl ].
VAR_059290
Natural varianti1291 – 12911R → G.
Corresponds to variant rs12732924 [ dbSNP | Ensembl ].
VAR_049094
Natural varianti1468 – 14681R → H.1 Publication
Corresponds to variant rs3795677 [ dbSNP | Ensembl ].
VAR_033932

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti644 – 6441E → EDDGE in BAD92390. 1 Publication
Sequence conflicti768 – 7681P → T in BAD92390. 1 Publication
Sequence conflicti1426 – 14272EN → TR in AAF72885. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL359918
, AL513342, AL590490, AL646016 Genomic DNA. Translation: CAQ10135.1.
AL513342
, AL359918, AL590490, AL646016 Genomic DNA. Translation: CAQ10526.1.
AL590490
, AL359918, AL513342, AL646016 Genomic DNA. Translation: CAQ10976.1.
AL646016
, AL359918, AL513342, AL590490 Genomic DNA. Translation: CAQ08405.1.
AB209153 mRNA. Translation: BAD92390.1.
AF218941 mRNA. Translation: AAF72884.1. Sequence problems.
AF218942 mRNA. Translation: AAF72885.1.
CCDSiCCDS31069.2.
RefSeqiNP_064450.3. NM_020066.4.
UniGeneiHs.24889.

Genome annotation databases

EnsembliENST00000319653; ENSP00000318884; ENSG00000155816.
GeneIDi56776.
KEGGihsa:56776.
UCSCiuc010pyd.2. human.

Polymorphism databases

DMDMi166215083.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL359918
, AL513342 , AL590490 , AL646016 Genomic DNA. Translation: CAQ10135.1 .
AL513342
, AL359918 , AL590490 , AL646016 Genomic DNA. Translation: CAQ10526.1 .
AL590490
, AL359918 , AL513342 , AL646016 Genomic DNA. Translation: CAQ10976.1 .
AL646016
, AL359918 , AL513342 , AL590490 Genomic DNA. Translation: CAQ08405.1 .
AB209153 mRNA. Translation: BAD92390.1 .
AF218941 mRNA. Translation: AAF72884.1 . Sequence problems.
AF218942 mRNA. Translation: AAF72885.1 .
CCDSi CCDS31069.2.
RefSeqi NP_064450.3. NM_020066.4.
UniGenei Hs.24889.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YLE X-ray 1.80 B 1694-1722 [» ]
3R7G X-ray 2.20 B 1701-1722 [» ]
ProteinModelPortali Q9NZ56.
SMRi Q9NZ56. Positions 1308-1699.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000318884.

PTM databases

PhosphoSitei Q9NZ56.

Polymorphism databases

DMDMi 166215083.

Proteomic databases

MaxQBi Q9NZ56.
PaxDbi Q9NZ56.
PRIDEi Q9NZ56.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319653 ; ENSP00000318884 ; ENSG00000155816 .
GeneIDi 56776.
KEGGi hsa:56776.
UCSCi uc010pyd.2. human.

Organism-specific databases

CTDi 56776.
GeneCardsi GC01P240177.
H-InvDB HIX0021237.
HGNCi HGNC:14074. FMN2.
HPAi HPA004937.
MIMi 606373. gene.
neXtProti NX_Q9NZ56.
PharmGKBi PA28185.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG264408.
HOGENOMi HOG000112618.
HOVERGENi HBG107923.
InParanoidi Q9NZ56.
KOi K02184.
OMAi EHRPKDA.
OrthoDBi EOG78M01H.
PhylomeDBi Q9NZ56.
TreeFami TF326072.

Enzyme and pathway databases

SignaLinki Q9NZ56.

Miscellaneous databases

GenomeRNAii 56776.
NextBioi 62219.
PROi Q9NZ56.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NZ56.
Bgeei Q9NZ56.
CleanExi HS_FMN2.
Genevestigatori Q9NZ56.

Family and domain databases

InterProi IPR000591. DEP_dom.
IPR015425. FH2_Formin.
IPR009408. Formin_homology_1.
[Graphical view ]
Pfami PF06346. Drf_FH1. 4 hits.
PF02181. FH2. 1 hit.
[Graphical view ]
SMARTi SM00498. FH2. 1 hit.
[Graphical view ]
PROSITEi PS51444. FH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1722, VARIANTS GLY-1148 AND HIS-1468.
    Tissue: Brain.
  3. "Formin-2, a novel formin homology protein of the cappuccino subfamily, is highly expressed in the developing and adult central nervous system."
    Leader B., Leder P.
    Mech. Dev. 93:221-231(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 396-727 AND 1426-1722, TISSUE SPECIFICITY.
    Tissue: Brain.
  4. "Effects of genistein on beta-catenin signaling and subcellular distribution of actin-binding proteins in human umbilical CD105-positive stromal cells."
    Shieh D.B., Li R.Y., Liao J.M., Chen G.D., Liou Y.M.
    J. Cell. Physiol. 223:423-434(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACTIN, SUBCELLULAR LOCATION.
  5. "Differential role of actin-binding proteins in controlling the adipogenic differentiation of human CD105-positive Wharton's Jelly cells."
    Peng K.W., Liou Y.M.
    Biochim. Biophys. Acta 1820:469-481(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Identification and functional characterization of FMN2, a regulator of the cyclin-dependent kinase inhibitor p21."
    Yamada K., Ono M., Perkins N.D., Rocha S., Lamond A.I.
    Mol. Cell 49:922-933(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDKN1A, SUBCELLULAR LOCATION, INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Molecular basis of actin nucleation factor cooperativity: crystal structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)*formin-2 formin SPIR interaction motif (FSI) complex."
    Zeth K., Pechlivanis M., Samol A., Pleiser S., Vonrhein C., Kerkhoff E.
    J. Biol. Chem. 286:30732-30739(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1694-1722 IN COMPLEX WITH SPIRE1, INTERACTION WITH SPIRE1.
  8. "Structure and function of the interacting domains of Spire and Fmn-family formins."
    Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W., Quinlan M.E., Eck M.J.
    Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1701-1722 IN COMPLEX WITH SPIRE1, INTERACTION WITH SPIRE1, MUTAGENESIS OF LYS-1715; LYS-1717 AND LYS-1721.

Entry informationi

Entry nameiFMN2_HUMAN
AccessioniPrimary (citable) accession number: Q9NZ56
Secondary accession number(s): B0QZA7
, Q59GF6, Q5VU37, Q9NZ55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 15, 2008
Last modified: July 9, 2014
This is version 114 of the entry and version 4 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 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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