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Protein

Fanconi anemia group D2 protein homolog

Gene

Fancd2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for maintenance of chromosomal stability. Promotes accurate and efficient pairing of homologs during meiosis. Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing. May participate in S phase and G2 phase checkpoint activation upon DNA damage. Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress (By similarity). Promotes BRCA2/FANCD1 loading onto damaged chromatin. May also be involved in B-cell immunoglobulin isotype switching.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • brain morphogenesis Source: MGI
  • cellular response to DNA damage stimulus Source: MGI
  • cellular response to oxidative stress Source: MGI
  • DNA repair Source: UniProtKB-KW
  • gamete generation Source: MGI
  • neuronal stem cell population maintenance Source: MGI
  • regulation of CD40 signaling pathway Source: MGI
  • regulation of inflammatory response Source: MGI
  • regulation of regulatory T cell differentiation Source: MGI
  • regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • response to gamma radiation Source: MGI
  • synapsis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiR-MMU-6783310. Fanconi Anemia Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Fanconi anemia group D2 protein homolog
Short name:
Protein FACD2
Gene namesi
Name:Fancd2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:2448480. Fancd2.

Subcellular locationi

  • Nucleus By similarity

  • Note: Concentrates in nuclear foci during S phase and upon genotoxic stress.By similarity

GO - Cellular componenti

  • condensed chromosome Source: MGI
  • cytoplasm Source: MGI
  • nucleolus Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice display delayed pre- and postnatal development, defects in germ-cell development, and increase incidence of microphthalmia and tumors of epithelial cell origin.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14501450Fanconi anemia group D2 protein homologPRO_0000087169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei220 – 2201PhosphoserineBy similarity
Cross-linki559 – 559Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei714 – 7141PhosphoserineBy similarity
Modified residuei1255 – 12551PhosphoserineBy similarity
Modified residuei1404 – 14041PhosphoserineBy similarity
Modified residuei1412 – 14121PhosphoserineBy similarity
Modified residuei1426 – 14261PhosphothreonineBy similarity
Modified residuei1434 – 14341PhosphoserineBy similarity

Post-translational modificationi

Monoubiquitinated on Lys-559 during S phase and upon genotoxic stress by FANCL in complex with E2 ligases UBE2T or UBE2W. Deubiquitinated by USP1 as cells enter G2/M, or once DNA repair is completed. Monoubiquitination requires the joint intervention of the FANC core complex, including FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL and FANCM, and proteins involved in cell cycle checkpoints and DNA repair, including RPA1, ATR, CHEK1 and BRCA1. Ubiquitination is required for binding to chromatin, interaction with BRCA1, BRCA2 and MTMR15/FAN1, DNA repair, and normal cell cycle progression (By similarity).By similarity
Phosphorylated on several sites including Ser-220 and Ser-1399 in response to genotoxic stress.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ80V62.
MaxQBiQ80V62.
PaxDbiQ80V62.
PeptideAtlasiQ80V62.
PRIDEiQ80V62.

PTM databases

iPTMnetiQ80V62.
PhosphoSiteiQ80V62.

Expressioni

Gene expression databases

BgeeiQ80V62.
CleanExiMM_FANCD2.
ExpressionAtlasiQ80V62. baseline and differential.
GenevisibleiQ80V62. MM.

Interactioni

Subunit structurei

Interacts directly with FANCE and FANCI. Interacts with USP1 and MEN1. The ubiquitinated form specifically interacts with BRCA1 and BLM. Both the nonubiquitinated and the monoubiquitinated forms interact with BRCA2; this interaction is mediated by phosphorylated FANCG and the complex also includes XCCR3 (By similarity). The ubiquitinated form specifically interacts with MTMR15/FAN1 (via UBZ-type zinc finger), leading to recruit MTMR15/FAN1 to sites of DNA damage. Interacts with DCLRE1B/Apollo (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
H2afxP276612EBI-7268304,EBI-495621

GO - Molecular functioni

Protein-protein interaction databases

BioGridi229254. 7 interactions.
IntActiQ80V62. 1 interaction.
MINTiMINT-4507601.
STRINGi10090.ENSMUSP00000045667.

Structurei

Secondary structure

1
1450
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 528Combined sources
Beta strandi65 – 684Combined sources
Helixi72 – 8312Combined sources
Helixi87 – 10115Combined sources
Helixi105 – 1117Combined sources
Beta strandi112 – 1143Combined sources
Helixi133 – 1397Combined sources
Turni141 – 1433Combined sources
Helixi144 – 15916Combined sources
Helixi170 – 1756Combined sources
Helixi176 – 1783Combined sources
Helixi187 – 20014Combined sources
Turni203 – 2053Combined sources
Helixi206 – 2116Combined sources
Helixi213 – 2164Combined sources
Helixi219 – 2213Combined sources
Helixi222 – 23514Combined sources
Helixi240 – 24910Combined sources
Helixi254 – 26613Combined sources
Helixi275 – 28511Combined sources
Helixi292 – 30413Combined sources
Helixi336 – 35419Combined sources
Helixi356 – 36813Combined sources
Helixi369 – 3713Combined sources
Helixi378 – 38912Combined sources
Helixi391 – 40515Combined sources
Turni406 – 4083Combined sources
Helixi412 – 42615Combined sources
Helixi430 – 44112Combined sources
Beta strandi443 – 4453Combined sources
Helixi446 – 46116Combined sources
Helixi465 – 48117Combined sources
Helixi484 – 50017Combined sources
Helixi502 – 5076Combined sources
Helixi509 – 5135Combined sources
Helixi514 – 5218Combined sources
Helixi524 – 54118Combined sources
Helixi548 – 56114Combined sources
Helixi566 – 58217Combined sources
Helixi603 – 61917Combined sources
Beta strandi620 – 6223Combined sources
Helixi623 – 63917Combined sources
Helixi644 – 66219Combined sources
Beta strandi679 – 6813Combined sources
Beta strandi685 – 6873Combined sources
Beta strandi689 – 6924Combined sources
Helixi697 – 70610Combined sources
Helixi727 – 74216Combined sources
Turni747 – 7493Combined sources
Helixi750 – 7523Combined sources
Beta strandi757 – 7593Combined sources
Beta strandi765 – 7684Combined sources
Helixi774 – 79724Combined sources
Helixi803 – 82725Combined sources
Helixi916 – 9194Combined sources
Turni920 – 9223Combined sources
Helixi928 – 9358Combined sources
Helixi960 – 97819Combined sources
Turni1001 – 10044Combined sources
Helixi1007 – 103428Combined sources
Helixi1050 – 107122Combined sources
Turni1074 – 10774Combined sources
Helixi1082 – 10909Combined sources
Helixi1105 – 111713Combined sources
Helixi1118 – 11225Combined sources
Helixi1126 – 114015Combined sources
Helixi1149 – 116012Combined sources
Helixi1174 – 119017Combined sources
Helixi1194 – 120310Combined sources
Turni1204 – 12063Combined sources
Helixi1207 – 12104Combined sources
Helixi1226 – 124419Combined sources
Helixi1254 – 128027Combined sources
Turni1281 – 12833Combined sources
Helixi1287 – 130519Combined sources
Helixi1307 – 13148Combined sources
Turni1315 – 13173Combined sources
Helixi1319 – 134022Combined sources
Helixi1344 – 13463Combined sources
Helixi1349 – 13524Combined sources
Helixi1355 – 137319Combined sources
Helixi1379 – 13879Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S4WX-ray3.41B33-1415[»]
ProteinModelPortaliQ80V62.
SMRiQ80V62. Positions 43-845.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 289289Interaction with FANCEBy similarityAdd
BLAST
Regioni246 – 357112Interaction with BRCA2By similarityAdd
BLAST

Phylogenomic databases

eggNOGiKOG4712. Eukaryota.
ENOG410XT6B. LUCA.
GeneTreeiENSGT00390000016970.
HOGENOMiHOG000060189.
HOVERGENiHBG060904.
InParanoidiQ80V62.
KOiK10891.
OMAiSHIQDDM.
OrthoDBiEOG7QZGB3.
PhylomeDBiQ80V62.
TreeFamiTF101106.

Family and domain databases

InterProiIPR029448. FANCD2.
[Graphical view]
PfamiPF14631. FancD2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80V62-1) [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
MISKRRRLDS EDKENLTEDA SKTMPLSKLA KKSHNSHEVE ENGSVFVKLL
60 70 80 90 100
KASGLTLKTG ENQNQLGVDQ VIFQRKLFQA LRKHPAYPKV IEEFVNGLES
110 120 130 140 150
YTEDSESLRN CLLSCERLQD EEASMGTFYS KSLIKLLLGI DILQPAIIKM
160 170 180 190 200
LFEKVPQFLF ESENRDGINM ARLIINQLKW LDRIVDGKDL TAQMMQLISV
210 220 230 240 250
APVNLQHDFI TSLPEILGDS QHANVGKELG ELLVQNTSLT VPILDVFSSL
260 270 280 290 300
RLDPNFLSKI RQLVMGKLSS VRLEDFPVIV KFLLHSVTDT TSLEVIAELR
310 320 330 340 350
ENLNVQQFIL PSRIQASQSK LKSKGLASSS GNQENSDKDC IVLVFDVIKS
360 370 380 390 400
AIRYEKTISE AWFKAIERIE SAAEHKALDV VMLLIIYSTS TQTKKGVEKL
410 420 430 440 450
LRNKIQSDCI QEQLLDSAFS THYLVLKDIC PSILLLAQTL FHSQDQRIIL
460 470 480 490 500
FGSLLYKYAF KFFDTYCQQE VVGALVTHVC SGTEAEVDTA LDVLLELIVL
510 520 530 540 550
NASAMRLNAA FVKGILDYLE NMSPQQIRKI FCILSTLAFS QQPGTSNHIQ
560 570 580 590 600
DDMHLVIRKQ LSSTVFKYKL IGIIGAVTMA GIMAEDRSVP SNSSQRSANV
610 620 630 640 650
SSEQRTQVTS LLQLVHSCTE HSPWASSLYY DEFANLIQER KLAPKTLEWV
660 670 680 690 700
GQTIFNDFQD AFVVDFCAAP EGDFPFPVKA LYGLEEYSTQ DGIVINLLPL
710 720 730 740 750
FYQECAKDAS RATSQESSQR SMSSLCLASH FRLLRLCVAR QHDGNLDEID
760 770 780 790 800
GLLDCPLFLP DLEPGEKLES MSAKDRSLMC SLTFLTFNWF REVVNAFCQQ
810 820 830 840 850
TSPEMKGKVL SRLKDLVELQ GILEKYLAVI PDYVPPFASV DLDTLDMMPR
860 870 880 890 900
SSSAVAAKNR NKGKTGGKKQ KADSNKASCS DTLLTEDTSE CDMAPSGRSH
910 920 930 940 950
VDKESTGKEG KTFVSLQNYR AFFRELDIEV FSILHSGLVT KFILDTEMHT
960 970 980 990 1000
EATEVVQLGP AELLFLLEDL SQKLENMLTA PFAKRICCFK NKGRQNIGFS
1010 1020 1030 1040 1050
HLHQRSVQDI VHCVVQLLTP MCNHLENIHN FFQCLGAEHL SADDKARATA
1060 1070 1080 1090 1100
QEQHTMACCY QKLLQVLHAL FAWKGFTHQS KHRLLHSALE VLSNRLKQME
1110 1120 1130 1140 1150
QDQPLEELVS QSFSYLQNFH HSVPSFQCGL YLLRLLMALL EKSAVPNQKK
1160 1170 1180 1190 1200
EKLASLAKQL LCRAWPHGEK EKNPTFNDHL HDVLYIYLEH TDNVLKAIEE
1210 1220 1230 1240 1250
ITGVGVPELV SAPKDAASST FPTLTRHTFV IFFRVMMAEL EKTVKGLQAG
1260 1270 1280 1290 1300
TAADSQQVHE EKLLYWNMAV RDFSILLNLM KVFDSYPVLH VCLKYGRRFV
1310 1320 1330 1340 1350
EAFLKQCMPL LDFSFRKHRE DVLSLLQTLQ LNTRLLHHLC GHSKIRQDTR
1360 1370 1380 1390 1400
LTKHVPLLKK SLELLVCRVK AMLVLNNCRE AFWLGTLKNR DLQGEEIISQ
1410 1420 1430 1440 1450
DPSSSESNAE DSEDGVTSHV SRNRATEDGE DEASDEQKDQ DSDESDDSSS
Length:1,450
Mass (Da):163,618
Last modified:June 7, 2005 - v2
Checksum:iB1B9AE5B580AC2E9
GO
Isoform 2 (identifier: Q80V62-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     124-129: SMGTFY → RCGEEA
     130-1450: Missing.

Show »
Length:129
Mass (Da):14,683
Checksum:iFFF76AC76AC4DA8D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei124 – 1296SMGTFY → RCGEEA in isoform 2. 1 PublicationVSP_013889
Alternative sequencei130 – 14501321Missing in isoform 2. 1 PublicationVSP_013890Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019136 mRNA. Translation: BAB31563.1.
CK634273 mRNA. No translation available.
CN460982 mRNA. No translation available.
BC042619 mRNA. Translation: AAH42619.1.
CCDSiCCDS20426.1. [Q80V62-1]
RefSeqiNP_001028416.2. NM_001033244.3. [Q80V62-1]
UniGeneiMm.160061.

Genome annotation databases

EnsembliENSMUST00000036340; ENSMUSP00000045667; ENSMUSG00000034023. [Q80V62-1]
GeneIDi211651.
KEGGimmu:211651.
UCSCiuc009dgw.2. mouse. [Q80V62-2]
uc009dgx.2. mouse. [Q80V62-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019136 mRNA. Translation: BAB31563.1.
CK634273 mRNA. No translation available.
CN460982 mRNA. No translation available.
BC042619 mRNA. Translation: AAH42619.1.
CCDSiCCDS20426.1. [Q80V62-1]
RefSeqiNP_001028416.2. NM_001033244.3. [Q80V62-1]
UniGeneiMm.160061.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S4WX-ray3.41B33-1415[»]
ProteinModelPortaliQ80V62.
SMRiQ80V62. Positions 43-845.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229254. 7 interactions.
IntActiQ80V62. 1 interaction.
MINTiMINT-4507601.
STRINGi10090.ENSMUSP00000045667.

PTM databases

iPTMnetiQ80V62.
PhosphoSiteiQ80V62.

Proteomic databases

EPDiQ80V62.
MaxQBiQ80V62.
PaxDbiQ80V62.
PeptideAtlasiQ80V62.
PRIDEiQ80V62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036340; ENSMUSP00000045667; ENSMUSG00000034023. [Q80V62-1]
GeneIDi211651.
KEGGimmu:211651.
UCSCiuc009dgw.2. mouse. [Q80V62-2]
uc009dgx.2. mouse. [Q80V62-1]

Organism-specific databases

CTDi2177.
MGIiMGI:2448480. Fancd2.

Phylogenomic databases

eggNOGiKOG4712. Eukaryota.
ENOG410XT6B. LUCA.
GeneTreeiENSGT00390000016970.
HOGENOMiHOG000060189.
HOVERGENiHBG060904.
InParanoidiQ80V62.
KOiK10891.
OMAiSHIQDDM.
OrthoDBiEOG7QZGB3.
PhylomeDBiQ80V62.
TreeFamiTF101106.

Enzyme and pathway databases

ReactomeiR-MMU-6783310. Fanconi Anemia Pathway.

Miscellaneous databases

PROiQ80V62.
SOURCEiSearch...

Gene expression databases

BgeeiQ80V62.
CleanExiMM_FANCD2.
ExpressionAtlasiQ80V62. baseline and differential.
GenevisibleiQ80V62. MM.

Family and domain databases

InterProiIPR029448. FANCD2.
[Graphical view]
PfamiPF14631. FancD2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
  2. The MGC Project Team
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-422 (ISOFORM 1).
  3. "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] OF 341-1450 (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Epithelial cancer in Fanconi anemia complementation group D2 (Fancd2) knockout mice."
    Houghtaling S., Timmers C., Noll M., Finegold M.J., Jones S.N., Meyn M.S., Grompe M.
    Genes Dev. 17:2021-2035(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiFACD2_MOUSE
AccessioniPrimary (citable) accession number: Q80V62
Secondary accession number(s): Q9CWC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: July 6, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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 one 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.