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Q8K368

- FANCI_MOUSE

UniProt

Q8K368 - FANCI_MOUSE

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Protein

Fanconi anemia group I protein homolog

Gene

Fanci

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Plays an essential role in the repair of DNA double-strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites. Required for maintenance of chromosomal stability. Specifically binds branched DNA: binds both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). Participates in S phase and G2 phase checkpoint activation upon DNA damage.

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. DNA repair Source: UniProtKB-KW
  3. positive regulation of protein ubiquitination Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_232842. Fanconi Anemia pathway.
REACT_260435. Regulation of the Fanconi anemia pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Fanconi anemia group I protein homolog
Short name:
Protein FACI
Gene namesi
Name:Fanci
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:2384790. Fanci.

Subcellular locationi

Nucleus By similarity
Note: Observed in spots localized in pairs on the sister chromatids of mitotic chromosome arms and not centromeres, one on each chromatids. These foci coincide with common fragile sites. They are frequently interlinked through BLM-associated ultra-fine DNA bridges (By similarity).By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13301330Fanconi anemia group I protein homologPRO_0000289977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki522 – 522Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei555 – 5551Phosphoserine1 Publication
Modified residuei558 – 5581Phosphothreonine1 Publication
Modified residuei729 – 7291PhosphoserineBy similarity
Modified residuei948 – 9481PhosphothreonineBy similarity
Modified residuei1122 – 11221PhosphoserineBy similarity

Post-translational modificationi

Monoubiquitinated by FANCL on Lys-522 during S phase and upon genotoxic stress. Deubiquitinated by USP1 as cells enter G2/M, or once DNA repair is completed. Monoubiquitination requires the FANCA-FANCB-FANCC-FANCE-FANCF-FANCG-FANCM complex. Ubiquitination is required for binding to chromatin, DNA repair, and normal cell cycle progression. Monoubiquitination is stimulated by DNA-binding (By similarity).By similarity
Phosphorylated in response to DNA damage by ATM and/or ATR.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8K368.
PaxDbiQ8K368.
PRIDEiQ8K368.

PTM databases

PhosphoSiteiQ8K368.

Expressioni

Gene expression databases

BgeeiQ8K368.
CleanExiMM_FANCI.
ExpressionAtlasiQ8K368. baseline and differential.
GenevestigatoriQ8K368.

Interactioni

Subunit structurei

Interacts with FANCD2; the interaction is direct. Interacts with FANCL. Interacts with MTMR15/FAN1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi229017. 2 interactions.
STRINGi10090.ENSMUSP00000044931.

Structurei

Secondary structure

1
1330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1110Combined sources
Helixi15 – 2410Combined sources
Helixi29 – 3810Combined sources
Helixi40 – 445Combined sources
Helixi46 – 516Combined sources
Beta strandi56 – 583Combined sources
Helixi59 – 7820Combined sources
Helixi83 – 9614Combined sources
Helixi97 – 993Combined sources
Helixi102 – 11716Combined sources
Turni125 – 1284Combined sources
Helixi129 – 13810Combined sources
Beta strandi145 – 1484Combined sources
Helixi153 – 16614Combined sources
Turni171 – 1733Combined sources
Helixi174 – 1807Combined sources
Helixi181 – 1833Combined sources
Helixi188 – 20215Combined sources
Helixi207 – 2093Combined sources
Helixi210 – 22112Combined sources
Helixi226 – 24823Combined sources
Helixi261 – 28121Combined sources
Helixi283 – 29311Combined sources
Helixi299 – 3046Combined sources
Helixi307 – 31610Combined sources
Helixi320 – 3223Combined sources
Helixi323 – 34422Combined sources
Helixi348 – 3536Combined sources
Helixi360 – 37011Combined sources
Turni371 – 3744Combined sources
Helixi377 – 39317Combined sources
Turni397 – 3993Combined sources
Helixi413 – 43220Combined sources
Helixi434 – 4363Combined sources
Helixi437 – 45014Combined sources
Helixi457 – 46913Combined sources
Helixi471 – 4744Combined sources
Helixi478 – 4814Combined sources
Helixi482 – 4865Combined sources
Turni487 – 4893Combined sources
Helixi492 – 50615Combined sources
Helixi510 – 52314Combined sources
Helixi529 – 54517Combined sources
Helixi546 – 5494Combined sources
Helixi555 – 5595Combined sources
Turni560 – 5623Combined sources
Beta strandi566 – 5705Combined sources
Beta strandi572 – 5743Combined sources
Helixi582 – 59110Combined sources
Helixi592 – 5954Combined sources
Helixi598 – 61417Combined sources
Helixi616 – 6183Combined sources
Helixi619 – 63315Combined sources
Beta strandi641 – 6444Combined sources
Helixi647 – 6493Combined sources
Beta strandi650 – 6534Combined sources
Beta strandi656 – 6594Combined sources
Helixi663 – 67917Combined sources
Helixi693 – 71220Combined sources
Turni718 – 7214Combined sources
Helixi733 – 75927Combined sources
Helixi764 – 78320Combined sources
Helixi806 – 81611Combined sources
Beta strandi821 – 8233Combined sources
Helixi825 – 8328Combined sources
Helixi836 – 85419Combined sources
Helixi866 – 88419Combined sources
Helixi903 – 92018Combined sources
Helixi923 – 9253Combined sources
Helixi926 – 9327Combined sources
Turni940 – 9445Combined sources
Helixi946 – 96722Combined sources
Helixi976 – 98813Combined sources
Helixi998 – 101114Combined sources
Helixi1018 – 103215Combined sources
Turni1033 – 10353Combined sources
Helixi1039 – 105315Combined sources
Beta strandi1056 – 10583Combined sources
Helixi1073 – 10764Combined sources
Turni1077 – 10793Combined sources
Helixi1080 – 110324Combined sources
Helixi1128 – 115124Combined sources
Turni1156 – 11583Combined sources
Helixi1159 – 118426Combined sources
Turni1185 – 11884Combined sources
Helixi1193 – 11997Combined sources
Helixi1202 – 12054Combined sources
Helixi1207 – 122115Combined sources
Helixi1249 – 126921Combined sources
Beta strandi1270 – 12723Combined sources
Helixi1274 – 12785Combined sources
Beta strandi1281 – 12844Combined sources
Helixi1292 – 12976Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S4WX-ray3.41A1-1302[»]
3S4ZX-ray7.80A/B/C1-1302[»]
3S51X-ray3.30A/B/C/D1-1302[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The C-terminal 30 residues are probably required for function in DNA repair.By similarity

Phylogenomic databases

eggNOGiNOG324185.
GeneTreeiENSGT00390000005855.
HOGENOMiHOG000112497.
HOVERGENiHBG106622.
InParanoidiQ8K368.
KOiK10895.
OMAiSQEEDFN.
PhylomeDBiQ8K368.
TreeFamiTF323694.

Family and domain databases

InterProiIPR026171. FANCI.
IPR029310. FANCI_HD1.
IPR029312. FANCI_HD2.
IPR029308. FANCI_S1.
IPR029305. FANCI_S1-cap.
IPR029315. FANCI_S2.
IPR029313. FANCI_S3.
IPR029314. FANCI_S4.
[Graphical view]
PANTHERiPTHR21818:SF0. PTHR21818:SF0. 1 hit.
PfamiPF14679. FANCI_HD1. 1 hit.
PF14680. FANCI_HD2. 1 hit.
PF14675. FANCI_S1. 1 hit.
PF14674. FANCI_S1-cap. 1 hit.
PF14676. FANCI_S2. 1 hit.
PF14677. FANCI_S3. 1 hit.
PF14678. FANCI_S4. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8K368-1) [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
MDLKILSLAT DKTTDKLQEF LQTLKDDDLA SLLQNQAVKG RAVGTLLRAV
60 70 80 90 100
LKGSPCSEED GALRRYKIYS CCIQLVESGD LQQDVASEII GLLMLEVHHF
110 120 130 140 150
PGPLLVDLAS DFVGAVREDR LVNGKSLELL PIILTALATK KEVLACGKGD
160 170 180 190 200
LNGEEYKRQL IDTLCSVRWP QRYMIQLTSV FKDVCLTPEE MNLVVAKVLT
210 220 230 240 250
MFSKLNLQEI PPLVYQLLVL SSKGSRRSVL DGIIAFFREL DKQHREEQSS
260 270 280 290 300
DELSELITAP ADELYHVEGT VILHIVFAIK LDCELGRELL KHLKAGQQGD
310 320 330 340 350
PSKCLCPFSI ALLLSLTRIQ RFEEQVFDLL KTSVVKSFKD LQLLQGSKFL
360 370 380 390 400
QTLVPQRTCV STMILEVVRN SVHSWDHVTQ GLIEFGFILM DSYGPKKILD
410 420 430 440 450
GKAVEIGTSL SKMTNQHACK LGANILLETF KIHEMIRQEI LEQVLNRVVT
460 470 480 490 500
RTSSPINHFL DLFSDIIMYA PLILQNCSKV TETFDYLTFL PLQTVQGLLK
510 520 530 540 550
AVQPLLKISM SMRDSLILVL RKAMFASQLD ARKSAVAGFL LLLKNFKVLG
560 570 580 590 600
SLPSSQCTQS IGVTQVRVDV HSRYSAVANE TFCLEIIDSL KRSLGQQADI
610 620 630 640 650
RLMLYDGFYD VLRRNSQLAS SIMQTLFSQL KQFYEPEPDL LPPLKLGACV
660 670 680 690 700
LTQGSQIFLQ EPLDHLLSCI QHCLAWYKSR VVPLQQGDEG EEEEEELYSE
710 720 730 740 750
LDDMLESITV RMIKSELEDF ELDKSADFSQ NTNVGIKNNI CACLIMGVCE
760 770 780 790 800
VLMEYNFSIS NFSKSKFEEI LSLFTCYKKF SDILSEKAGK GKAKMTSKVS
810 820 830 840 850
DSLLSLKFVS DLLTALFRDS IQSHEESLSV LRSSGEFMHY AVNVTLQKIQ
860 870 880 890 900
QLIRTGHVSG PDGQNPDKIF QNLCDITRVL LWRYTSIPTS VEESGKKEKG
910 920 930 940 950
KSISLLCLEG LQKTFSVVLQ FYQPKVQQFL QALDVMGTEE EEAGVTVTQR
960 970 980 990 1000
ASFQIRQFQR SLLNLLSSEE DDFNSKEALL LIAVLSTLSR LLEPTSPQFV
1010 1020 1030 1040 1050
QMLSWTSKIC KEYSQEDASF CKSLMNLFFS LHVLYKSPVT LLRDLSQDIH
1060 1070 1080 1090 1100
GQLGDIDQDV EIEKTDHFAV VNLRTAAPTV CLLVLSQAEK VLEEVDWLIA
1110 1120 1130 1140 1150
KIKGSANQET LSDKVTPEDA SSQAVPPTLL IEKAIVMQLG TLVTFFHELV
1160 1170 1180 1190 1200
QTALPSGSCV DTLLKGLSKI YSTLTAFVKY YLQVCQSSRG IPNTVEKLVK
1210 1220 1230 1240 1250
LSGSHLTPVC YSFISYVQNK SSDAPKCSEK EKAAVSTTMA KVLRETKPIP
1260 1270 1280 1290 1300
NLVFAIEQYE KFLIQLSKKS KVNLMQHMKL STSRDFKIKG SVLDMVLRED
1310 1320 1330
EEDENEEGTA SAHTQQDREP AKKRRKKCLS
Length:1,330
Mass (Da):149,326
Last modified:June 12, 2007 - v2
Checksum:i68A0580B54E20CBB
GO
Isoform 2 (identifier: Q8K368-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     371-394: SVHSWDHVTQGLIEFGFILMDSYG → RLVFRYHHVCTFNSSELFKSHGNF
     395-1330: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Show »
Length:394
Mass (Da):44,333
Checksum:i71530D576E81F23B
GO
Isoform 4 (identifier: Q8K368-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     879-1330: Missing.

Note: No experimental confirmation available.

Show »
Length:878
Mass (Da):98,663
Checksum:iBC9A79AED797F624
GO

Sequence cautioni

The sequence BAC39475.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti540 – 5401L → W in BAC39475. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei371 – 39424SVHSW…MDSYG → RLVFRYHHVCTFNSSELFKS HGNF in isoform 2. 1 PublicationVSP_026072Add
BLAST
Alternative sequencei395 – 1330936Missing in isoform 2. 1 PublicationVSP_026073Add
BLAST
Alternative sequencei879 – 1330452Missing in isoform 4. 1 PublicationVSP_026074Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC110909 Genomic DNA. No translation available.
BC027836 mRNA. No translation available.
AK085572 mRNA. Translation: BAC39475.1. Different initiation.
CCDSiCCDS39991.1. [Q8K368-1]
RefSeqiNP_666058.2. NM_145946.2. [Q8K368-1]
UniGeneiMm.349493.

Genome annotation databases

EnsembliENSMUST00000036865; ENSMUSP00000044931; ENSMUSG00000039187. [Q8K368-1]
ENSMUST00000132091; ENSMUSP00000122113; ENSMUSG00000039187. [Q8K368-2]
GeneIDi208836.
KEGGimmu:208836.
UCSCiuc009hyh.1. mouse. [Q8K368-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC110909 Genomic DNA. No translation available.
BC027836 mRNA. No translation available.
AK085572 mRNA. Translation: BAC39475.1 . Different initiation.
CCDSi CCDS39991.1. [Q8K368-1 ]
RefSeqi NP_666058.2. NM_145946.2. [Q8K368-1 ]
UniGenei Mm.349493.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3S4W X-ray 3.41 A 1-1302 [» ]
3S4Z X-ray 7.80 A/B/C 1-1302 [» ]
3S51 X-ray 3.30 A/B/C/D 1-1302 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 229017. 2 interactions.
STRINGi 10090.ENSMUSP00000044931.

PTM databases

PhosphoSitei Q8K368.

Proteomic databases

MaxQBi Q8K368.
PaxDbi Q8K368.
PRIDEi Q8K368.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000036865 ; ENSMUSP00000044931 ; ENSMUSG00000039187 . [Q8K368-1 ]
ENSMUST00000132091 ; ENSMUSP00000122113 ; ENSMUSG00000039187 . [Q8K368-2 ]
GeneIDi 208836.
KEGGi mmu:208836.
UCSCi uc009hyh.1. mouse. [Q8K368-1 ]

Organism-specific databases

CTDi 55215.
MGIi MGI:2384790. Fanci.

Phylogenomic databases

eggNOGi NOG324185.
GeneTreei ENSGT00390000005855.
HOGENOMi HOG000112497.
HOVERGENi HBG106622.
InParanoidi Q8K368.
KOi K10895.
OMAi SQEEDFN.
PhylomeDBi Q8K368.
TreeFami TF323694.

Enzyme and pathway databases

Reactomei REACT_232842. Fanconi Anemia pathway.
REACT_260435. Regulation of the Fanconi anemia pathway.

Miscellaneous databases

NextBioi 372429.
PROi Q8K368.
SOURCEi Search...

Gene expression databases

Bgeei Q8K368.
CleanExi MM_FANCI.
ExpressionAtlasi Q8K368. baseline and differential.
Genevestigatori Q8K368.

Family and domain databases

InterProi IPR026171. FANCI.
IPR029310. FANCI_HD1.
IPR029312. FANCI_HD2.
IPR029308. FANCI_S1.
IPR029305. FANCI_S1-cap.
IPR029315. FANCI_S2.
IPR029313. FANCI_S3.
IPR029314. FANCI_S4.
[Graphical view ]
PANTHERi PTHR21818:SF0. PTHR21818:SF0. 1 hit.
Pfami PF14679. FANCI_HD1. 1 hit.
PF14680. FANCI_HD2. 1 hit.
PF14675. FANCI_S1. 1 hit.
PF14674. FANCI_S1-cap. 1 hit.
PF14676. FANCI_S2. 1 hit.
PF14677. FANCI_S3. 1 hit.
PF14678. FANCI_S4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "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).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "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] OF 27-1330 (ISOFORM 4).
    Strain: C57BL/6J.
    Tissue: Kidney.
  4. "Identification of the FANCI protein, a monoubiquitinated FANCD2 paralog required for DNA repair."
    Smogorzewska A., Matsuoka S., Vinciguerra P., McDonald E.R. III, Hurov K.E., Luo J., Ballif B.A., Gygi S.P., Hofmann K., D'Andrea A.D., Elledge S.J.
    Cell 129:289-301(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-555 AND THR-558.
  5. Cited for: IDENTIFICATION.

Entry informationi

Entry nameiFANCI_MOUSE
AccessioniPrimary (citable) accession number: Q8K368
Secondary accession number(s): Q8BUE9, Q8R3G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: June 12, 2007
Last modified: November 26, 2014
This is version 79 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

External Data

Dasty 3