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Protein

YY1-associated factor 2

Gene

YAF2

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

Functioni

Binds to MYC and inhibits MYC-mediated transactivation. Also binds to MYCN and enhances MYCN-dependent transcriptional activation. Increases calpain 2-mediated proteolysis of YY1 in vitro. Component of the E2F6.com-1 complex, a repressive complex that methylates 'Lys-9' of histone H3, suggesting that it is involved in chromatin-remodeling.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri19 – 4830RanBP2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
YY1-associated factor 2
Gene namesi
Name:YAF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:17363. YAF2.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38236.

Polymorphism and mutation databases

BioMutaiYAF2.
DMDMi215274199.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180YY1-associated factor 2PRO_0000066113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei167 – 1671Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8IY57.
PaxDbiQ8IY57.
PRIDEiQ8IY57.

PTM databases

PhosphoSiteiQ8IY57.

Expressioni

Gene expression databases

BgeeiQ8IY57.
CleanExiHS_YAF2.
ExpressionAtlasiQ8IY57. baseline and differential.
GenevisibleiQ8IY57. HS.

Organism-specific databases

HPAiHPA026867.

Interactioni

Subunit structurei

Interacts with MYC, MYCN, RNF2/RING1B and YY1. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RING1Q065874EBI-2842031,EBI-752313
SETBP1Q9Y6X03EBI-2842031,EBI-2548259
XAGE1EQ9HD643EBI-2842031,EBI-2340004

Protein-protein interaction databases

BioGridi115441. 52 interactions.
DIPiDIP-44919N.
IntActiQ8IY57. 11 interactions.
MINTiMINT-1521451.

Structurei

Secondary structure

1
180
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 283Combined sources
Beta strandi40 – 423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9GNMR-A19-58[»]
ProteinModelPortaliQ8IY57.
SMRiQ8IY57. Positions 19-58, 101-133.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IY57.

Family & Domainsi

Sequence similaritiesi

Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri19 – 4830RanBP2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG268430.
GeneTreeiENSGT00390000013995.
HOGENOMiHOG000007553.
HOVERGENiHBG001768.
InParanoidiQ8IY57.
KOiK11468.
OMAiVNQQFAS.
OrthoDBiEOG7B8S61.
PhylomeDBiQ8IY57.
TreeFamiTF350501.

Family and domain databases

InterProiIPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IY57-1) [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
MGDKKSPTRP KRQPKPSSDE GYWDCSVCTF RNSAEAFKCM MCDVRKGTST
60 70 80 90 100
RKPRPVSQLV AQQVTQQFVP PTQSKKEKKD KVEKEKSEKE TTSKKNSHKK
110 120 130 140 150
TRPRLKNVDR SSAQHLEVTV GDLTVIITDF KEKTKSPPAS SAASADQHSQ
160 170 180
SGSSSDNTER GMSRSSSPRG EASSLNGESH
Length:180
Mass (Da):19,901
Last modified:November 25, 2008 - v3
Checksum:i199A56EE06BB4FBE
GO
Isoform 2 (identifier: Q8IY57-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     50-50: T → TRSTLFEVIVSASRTKEPLKFPISG

Note: No experimental confirmation available.
Show »
Length:204
Mass (Da):22,546
Checksum:i16C4D290C18BD880
GO
Isoform 3 (identifier: Q8IY57-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     8-49: Missing.

Note: No experimental confirmation available.
Show »
Length:138
Mass (Da):15,115
Checksum:i3E1E2E64F1003EC5
GO
Isoform 4 (identifier: Q8IY57-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     52-117: KPRPVSQLVA...VDRSSAQHLE → DSKEGGKLVS...QRSGPSLKEA
     118-180: Missing.

Note: No experimental confirmation available.
Show »
Length:117
Mass (Da):12,738
Checksum:i7A8B9E3A734AF65F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 142QP → HA in AAC51116 (PubMed:9016636).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei8 – 4942Missing in isoform 3. 1 PublicationVSP_043415Add
BLAST
Alternative sequencei50 – 501T → TRSTLFEVIVSASRTKEPLK FPISG in isoform 2. 1 PublicationVSP_055659
Alternative sequencei52 – 11766KPRPV…AQHLE → DSKEGGKLVSYSTASLGVRG TLRNRVGGGSSEEKKQAEYL APGRRRNIVHRGVGPGQRSG PSLKEA in isoform 4. 1 PublicationVSP_044598Add
BLAST
Alternative sequencei118 – 18063Missing in isoform 4. 1 PublicationVSP_044599Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72209 mRNA. Translation: AAC51116.1.
AK127531 mRNA. No translation available.
AK291355 mRNA. Translation: BAF84044.1.
AK294260 mRNA. Translation: BAG57554.1.
AC020629 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57839.1.
BC037777 mRNA. Translation: AAH37777.1.
CCDSiCCDS31775.1. [Q8IY57-1]
CCDS53778.1. [Q8IY57-3]
CCDS53779.1. [Q8IY57-5]
CCDS53780.1. [Q8IY57-4]
RefSeqiNP_001177906.1. NM_001190977.1. [Q8IY57-3]
NP_001177908.1. NM_001190979.1. [Q8IY57-5]
NP_001177909.1. NM_001190980.1. [Q8IY57-4]
NP_005739.2. NM_005748.4. [Q8IY57-1]
UniGeneiHs.649195.
Hs.708084.

Genome annotation databases

EnsembliENST00000327791; ENSP00000328004; ENSG00000015153. [Q8IY57-5]
ENST00000380790; ENSP00000370167; ENSG00000015153. [Q8IY57-3]
ENST00000534854; ENSP00000439256; ENSG00000015153.
ENST00000555248; ENSP00000451626; ENSG00000015153. [Q8IY57-4]
GeneIDi10138.
KEGGihsa:10138.
UCSCiuc001rmv.3. human. [Q8IY57-1]
uc010skp.2. human. [Q8IY57-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U72209 mRNA. Translation: AAC51116.1.
AK127531 mRNA. No translation available.
AK291355 mRNA. Translation: BAF84044.1.
AK294260 mRNA. Translation: BAG57554.1.
AC020629 Genomic DNA. No translation available.
CH471111 Genomic DNA. Translation: EAW57839.1.
BC037777 mRNA. Translation: AAH37777.1.
CCDSiCCDS31775.1. [Q8IY57-1]
CCDS53778.1. [Q8IY57-3]
CCDS53779.1. [Q8IY57-5]
CCDS53780.1. [Q8IY57-4]
RefSeqiNP_001177906.1. NM_001190977.1. [Q8IY57-3]
NP_001177908.1. NM_001190979.1. [Q8IY57-5]
NP_001177909.1. NM_001190980.1. [Q8IY57-4]
NP_005739.2. NM_005748.4. [Q8IY57-1]
UniGeneiHs.649195.
Hs.708084.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9GNMR-A19-58[»]
ProteinModelPortaliQ8IY57.
SMRiQ8IY57. Positions 19-58, 101-133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115441. 52 interactions.
DIPiDIP-44919N.
IntActiQ8IY57. 11 interactions.
MINTiMINT-1521451.

PTM databases

PhosphoSiteiQ8IY57.

Polymorphism and mutation databases

BioMutaiYAF2.
DMDMi215274199.

Proteomic databases

MaxQBiQ8IY57.
PaxDbiQ8IY57.
PRIDEiQ8IY57.

Protocols and materials databases

DNASUi10138.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327791; ENSP00000328004; ENSG00000015153. [Q8IY57-5]
ENST00000380790; ENSP00000370167; ENSG00000015153. [Q8IY57-3]
ENST00000534854; ENSP00000439256; ENSG00000015153.
ENST00000555248; ENSP00000451626; ENSG00000015153. [Q8IY57-4]
GeneIDi10138.
KEGGihsa:10138.
UCSCiuc001rmv.3. human. [Q8IY57-1]
uc010skp.2. human. [Q8IY57-3]

Organism-specific databases

CTDi10138.
GeneCardsiGC12M042550.
HGNCiHGNC:17363. YAF2.
HPAiHPA026867.
MIMi607534. gene.
neXtProtiNX_Q8IY57.
PharmGKBiPA38236.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG268430.
GeneTreeiENSGT00390000013995.
HOGENOMiHOG000007553.
HOVERGENiHBG001768.
InParanoidiQ8IY57.
KOiK11468.
OMAiVNQQFAS.
OrthoDBiEOG7B8S61.
PhylomeDBiQ8IY57.
TreeFamiTF350501.

Miscellaneous databases

ChiTaRSiYAF2. human.
EvolutionaryTraceiQ8IY57.
GeneWikiiYAF2.
GenomeRNAii10138.
NextBioi38355.
PROiQ8IY57.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IY57.
CleanExiHS_YAF2.
ExpressionAtlasiQ8IY57. baseline and differential.
GenevisibleiQ8IY57. HS.

Family and domain databases

InterProiIPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast two-hybrid cloning of a novel zinc finger protein that interacts with the multifunctional transcription factor YY1."
    Kalenik J.L., Chen D., Bradley M.E., Chen S.-J., Lee T.-C.
    Nucleic Acids Res. 25:843-849(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH YY1.
    Tissue: Skeletal muscle.
  2. "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; 3 AND 4).
    Tissue: Amygdala, Brain and Thalamus.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
    Tissue: Brain.
  6. "Functional interaction of Yaf2 with the central region of MycN."
    Bannasch D., Maedge B., Schwab M.
    Oncogene 20:5913-5919(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYCN.
  7. "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
    Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
    Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EUHMTASE1; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND BAT8.
  8. Cited for: FUNCTION, INTERACTION WITH MYC.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Solution structure of the ZF-RANBP domain of YY1-associated factor 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 17-58.

Entry informationi

Entry nameiYAF2_HUMAN
AccessioniPrimary (citable) accession number: Q8IY57
Secondary accession number(s): A8K5P0
, B4DFU3, G3V465, Q99710
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: November 25, 2008
Last modified: July 22, 2015
This is version 123 of the entry and version 3 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 12
    Human chromosome 12: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.