Q9NVI1 (FANCI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fanconi anemia group I protein
Short name=Protein FACI

Gene names

Name:	FANCI
Synonyms:	KIAA1794

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1328 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for maintenance of chromosomal stability. Involved in the repair of DNA double-strand breaks by homologous recombination and in the repair of DNA cross-links. Participates in S phase and G2 phase checkpoint activation upon DNA damage. Promotes FANCD2 ubiquitination and recruitment to DNA repair sites. Ref.1 Ref.2 Ref.10
Subunit structure	Interacts directly with FANCD2. Interacts with MTMR15/FAN1. Ref.1 Ref.2 Ref.18
Subcellular location	Nucleus. 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. Ref.1 Ref.2 Ref.16
Domain	The C-terminal 30 residues are probably required for function in DNA repair.
Post-translational modification	Monoubiquitinated on Lys-523 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. Phosphorylated in response to DNA damage by ATM and/or ATR. Ref.1 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17
Involvement in disease	Defects in FANCI are a cause of Fanconi anemia complementation group I (FANCI) [MIM:609053]. A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. Ref.10
Sequence caution	The sequence AAH04277.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAA91770.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB55200.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Fanconi anemia
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Traceable author statement. Source: Reactome cell cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleoplasm Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay. Source: HPA
Molecular function	protein binding Inferred from physical interaction Ref.18. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FANCD2	Q9BXW9	2	EBI-1013291,EBI-359343

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 3 (identifier: Q9NVI1-3)

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.

Isoform 2 (identifier: Q9NVI1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     819-878: Missing.
     1117-1117: Missing.

Isoform 1 (identifier: Q9NVI1-1)

The sequence of this isoform differs from the canonical sequence as follows:
     819-878: Missing.

Isoform 4 (identifier: Q9NVI1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     253-1328: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1328	1328	Fanconi anemia group I protein		PRO_0000248376
Amino acid modifications
	Modified residue	215	1	Phosphotyrosine Ref.8
	Modified residue	407	1	Phosphoserine Ref.9 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17
	Modified residue	556	1	Phosphoserine By similarity
	Modified residue	730	1	Phosphoserine Ref.1 Ref.11
	Modified residue	952	1	Phosphothreonine Ref.1 Ref.11
	Modified residue	1121	1	Phosphoserine Ref.1 Ref.11
	Cross-link	523		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.1 Ref.2
Natural variations
	Alternative sequence	253 – 1328	1076	Missing in isoform 4.		VSP_035606
	Alternative sequence	819 – 878	60	Missing in isoform 1 and isoform 2.		VSP_026069
	Alternative sequence	1117	1	Missing in isoform 2.		VSP_020257
	Natural variant	55	1	P → L in FA; could be a polymorphism; no effect on ubiquitination and DNA repair. Ref.1 Ref.10		VAR_032689
	Natural variant	86	1	A → V. Ref.4 Corresponds to variant rs17803620 [ dbSNP | Ensembl ].		VAR_032690
	Natural variant	686	1	Q → K. Corresponds to variant rs28378332 [ dbSNP | Ensembl ].		VAR_027278
	Natural variant	742	1	C → S. Ref.5 Ref.6 Corresponds to variant rs2283432 [ dbSNP | Ensembl ].		VAR_027279
	Natural variant	858	1	H → Y in FA. Ref.2		VAR_032691
	Natural variant	1285	1	R → Q in FA/FANCI; abolishes function in DNA repair. Ref.1 Ref.10		VAR_032692
Experimental info
	Sequence conflict	528	1	N → S in BAB47423. Ref.6
	Sequence conflict	604	1	M → T in BAA91770. Ref.5
	Sequence conflict	877	1	I → L in BAB47423. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [UniParc]. Last modified November 4, 2008. Version 4. Checksum: 07E80FD2F0BCCB32	FASTA	1,328	149,324
	10 20 30 40 50 60 MDQKILSLAA EKTADKLQEF LQTLREGDLT NLLQNQAVKG KVAGALLRAI FKGSPCSEEA 70 80 90 100 110 120 GTLRRRKIYT CCIQLVESGD LQKEIASEII GLLMLEAHHF PGPLLVELAN EFISAVREGS 130 140 150 160 170 180 LVNGKSLELL PIILTALATK KENLAYGKGV LSGEECKKQL INTLCSGRWD QQYVIQLTSM 190 200 210 220 230 240 FKDVPLTAEE VEFVVEKALS MFSKMNLQEI PPLVYQLLVL SSKGSRKSVL EGIIAFFSAL 250 260 270 280 290 300 DKQHNEEQSG DELLDVVTVP SGELRHVEGT IILHIVFAIK LDYELGRELV KHLKVGQQGD 310 320 330 340 350 360 SNNNLSPFSI ALLLSVTRIQ RFQDQVLDLL KTSVVKSFKD LQLLQGSKFL QNLVPHRSYV 370 380 390 400 410 420 STMILEVVKN SVHSWDHVTQ GLVELGFILM DSYGPKKVLD GKTIETSPSL SRMPNQHACK 430 440 450 460 470 480 LGANILLETF KIHEMIRQEI LEQVLNRVVT RASSPISHFL DLLSNIVMYA PLVLQSCSSK 490 500 510 520 530 540 VTEAFDYLSF LPLQTVQRLL KAVQPLLKVS MSMRDCLILV LRKAMFANQL DARKSAVAGF 550 560 570 580 590 600 LLLLKNFKVL GSLSSSQCSQ SLSVSQVHVD VHSHYNSVAN ETFCLEIMDS LRRCLSQQAD 610 620 630 640 650 660 VRLMLYEGFY DVLRRNSQLA NSVMQTLLSQ LKQFYEPKPD LLPPLKLEAC ILTQGDKISL 670 680 690 700 710 720 QEPLDYLLCC IQHCLAWYKN TVIPLQQGEE EEEEEEAFYE DLDDILESIT NRMIKSELED 730 740 750 760 770 780 FELDKSADFS QSTSIGIKNN ICAFLVMGVC EVLIEYNFSI SSFSKNRFED ILSLFMCYKK 790 800 810 820 830 840 LSDILNEKAG KAKTKMANKT SDSLLSMKFV SSLLTALFRD SIQSHQESLS VLRSSNEFMR 850 860 870 880 890 900 YAVNVALQKV QQLKETGHVS GPDGQNPEKI FQNLCDITRV LLWRYTSIPT SVEESGKKEK 910 920 930 940 950 960 GKSISLLCLE GLQKIFSAVQ QFYQPKIQQF LRALDVTDKE GEEREDADVS VTQRTAFQIR 970 980 990 1000 1010 1020 QFQRSLLNLL SSQEEDFNSK EALLLVTVLT SLSKLLEPSS PQFVQMLSWT SKICKENSRE 1030 1040 1050 1060 1070 1080 DALFCKSLMN LLFSLHVSYK SPVILLRDLS QDIHGHLGDI DQDVEVEKTN HFAIVNLRTA 1090 1100 1110 1120 1130 1140 APTVCLLVLS QAEKVLEEVD WLITKLKGQV SQETLSEEAS SQATLPNQPV EKAIIMQLGT 1150 1160 1170 1180 1190 1200 LLTFFHELVQ TALPSGSCVD TLLKDLCKMY TTLTALVRYY LQVCQSSGGI PKNMEKLVKL 1210 1220 1230 1240 1250 1260 SGSHLTPLCY SFISYVQNKS KSLNYTGEKK EKPAAVATAM ARVLRETKPI PNLIFAIEQY 1270 1280 1290 1300 1310 1320 EKFLIHLSKK SKVNLMQHMK LSTSRDFKIK GNILDMVLRE DGEDENEEGT ASEHGGQNKE PAKKKRKK
	Isoform 2 [UniParc]. Checksum: AD13BB6692A0D812	FASTA	1,267	142,440
	10 20 30 40 50 60 MDQKILSLAA EKTADKLQEF LQTLREGDLT NLLQNQAVKG KVAGALLRAI FKGSPCSEEA 70 80 90 100 110 120 GTLRRRKIYT CCIQLVESGD LQKEIASEII GLLMLEAHHF PGPLLVELAN EFISAVREGS 130 140 150 160 170 180 LVNGKSLELL PIILTALATK KENLAYGKGV LSGEECKKQL INTLCSGRWD QQYVIQLTSM 190 200 210 220 230 240 FKDVPLTAEE VEFVVEKALS MFSKMNLQEI PPLVYQLLVL SSKGSRKSVL EGIIAFFSAL 250 260 270 280 290 300 DKQHNEEQSG DELLDVVTVP SGELRHVEGT IILHIVFAIK LDYELGRELV KHLKVGQQGD 310 320 330 340 350 360 SNNNLSPFSI ALLLSVTRIQ RFQDQVLDLL KTSVVKSFKD LQLLQGSKFL QNLVPHRSYV 370 380 390 400 410 420 STMILEVVKN SVHSWDHVTQ GLVELGFILM DSYGPKKVLD GKTIETSPSL SRMPNQHACK 430 440 450 460 470 480 LGANILLETF KIHEMIRQEI LEQVLNRVVT RASSPISHFL DLLSNIVMYA PLVLQSCSSK 490 500 510 520 530 540 VTEAFDYLSF LPLQTVQRLL KAVQPLLKVS MSMRDCLILV LRKAMFANQL DARKSAVAGF 550 560 570 580 590 600 LLLLKNFKVL GSLSSSQCSQ SLSVSQVHVD VHSHYNSVAN ETFCLEIMDS LRRCLSQQAD 610 620 630 640 650 660 VRLMLYEGFY DVLRRNSQLA NSVMQTLLSQ LKQFYEPKPD LLPPLKLEAC ILTQGDKISL 670 680 690 700 710 720 QEPLDYLLCC IQHCLAWYKN TVIPLQQGEE EEEEEEAFYE DLDDILESIT NRMIKSELED 730 740 750 760 770 780 FELDKSADFS QSTSIGIKNN ICAFLVMGVC EVLIEYNFSI SSFSKNRFED ILSLFMCYKK 790 800 810 820 830 840 LSDILNEKAG KAKTKMANKT SDSLLSMKFV SSLLTALFRV LLWRYTSIPT SVEESGKKEK 850 860 870 880 890 900 GKSISLLCLE GLQKIFSAVQ QFYQPKIQQF LRALDVTDKE GEEREDADVS VTQRTAFQIR 910 920 930 940 950 960 QFQRSLLNLL SSQEEDFNSK EALLLVTVLT SLSKLLEPSS PQFVQMLSWT SKICKENSRE 970 980 990 1000 1010 1020 DALFCKSLMN LLFSLHVSYK SPVILLRDLS QDIHGHLGDI DQDVEVEKTN HFAIVNLRTA 1030 1040 1050 1060 1070 1080 APTVCLLVLS QAEKVLEEVD WLITKLKGQV SQETLSEASS QATLPNQPVE KAIIMQLGTL 1090 1100 1110 1120 1130 1140 LTFFHELVQT ALPSGSCVDT LLKDLCKMYT TLTALVRYYL QVCQSSGGIP KNMEKLVKLS 1150 1160 1170 1180 1190 1200 GSHLTPLCYS FISYVQNKSK SLNYTGEKKE KPAAVATAMA RVLRETKPIP NLIFAIEQYE 1210 1220 1230 1240 1250 1260 KFLIHLSKKS KVNLMQHMKL STSRDFKIKG NILDMVLRED GEDENEEGTA SEHGGQNKEP AKKKRKK
	Isoform 1 [UniParc]. Checksum: 7D3A1A04E97FE80C	FASTA	1,268	142,569
	10 20 30 40 50 60 MDQKILSLAA EKTADKLQEF LQTLREGDLT NLLQNQAVKG KVAGALLRAI FKGSPCSEEA 70 80 90 100 110 120 GTLRRRKIYT CCIQLVESGD LQKEIASEII GLLMLEAHHF PGPLLVELAN EFISAVREGS 130 140 150 160 170 180 LVNGKSLELL PIILTALATK KENLAYGKGV LSGEECKKQL INTLCSGRWD QQYVIQLTSM 190 200 210 220 230 240 FKDVPLTAEE VEFVVEKALS MFSKMNLQEI PPLVYQLLVL SSKGSRKSVL EGIIAFFSAL 250 260 270 280 290 300 DKQHNEEQSG DELLDVVTVP SGELRHVEGT IILHIVFAIK LDYELGRELV KHLKVGQQGD 310 320 330 340 350 360 SNNNLSPFSI ALLLSVTRIQ RFQDQVLDLL KTSVVKSFKD LQLLQGSKFL QNLVPHRSYV 370 380 390 400 410 420 STMILEVVKN SVHSWDHVTQ GLVELGFILM DSYGPKKVLD GKTIETSPSL SRMPNQHACK 430 440 450 460 470 480 LGANILLETF KIHEMIRQEI LEQVLNRVVT RASSPISHFL DLLSNIVMYA PLVLQSCSSK 490 500 510 520 530 540 VTEAFDYLSF LPLQTVQRLL KAVQPLLKVS MSMRDCLILV LRKAMFANQL DARKSAVAGF 550 560 570 580 590 600 LLLLKNFKVL GSLSSSQCSQ SLSVSQVHVD VHSHYNSVAN ETFCLEIMDS LRRCLSQQAD 610 620 630 640 650 660 VRLMLYEGFY DVLRRNSQLA NSVMQTLLSQ LKQFYEPKPD LLPPLKLEAC ILTQGDKISL 670 680 690 700 710 720 QEPLDYLLCC IQHCLAWYKN TVIPLQQGEE EEEEEEAFYE DLDDILESIT NRMIKSELED 730 740 750 760 770 780 FELDKSADFS QSTSIGIKNN ICAFLVMGVC EVLIEYNFSI SSFSKNRFED ILSLFMCYKK 790 800 810 820 830 840 LSDILNEKAG KAKTKMANKT SDSLLSMKFV SSLLTALFRV LLWRYTSIPT SVEESGKKEK 850 860 870 880 890 900 GKSISLLCLE GLQKIFSAVQ QFYQPKIQQF LRALDVTDKE GEEREDADVS VTQRTAFQIR 910 920 930 940 950 960 QFQRSLLNLL SSQEEDFNSK EALLLVTVLT SLSKLLEPSS PQFVQMLSWT SKICKENSRE 970 980 990 1000 1010 1020 DALFCKSLMN LLFSLHVSYK SPVILLRDLS QDIHGHLGDI DQDVEVEKTN HFAIVNLRTA 1030 1040 1050 1060 1070 1080 APTVCLLVLS QAEKVLEEVD WLITKLKGQV SQETLSEEAS SQATLPNQPV EKAIIMQLGT 1090 1100 1110 1120 1130 1140 LLTFFHELVQ TALPSGSCVD TLLKDLCKMY TTLTALVRYY LQVCQSSGGI PKNMEKLVKL 1150 1160 1170 1180 1190 1200 SGSHLTPLCY SFISYVQNKS KSLNYTGEKK EKPAAVATAM ARVLRETKPI PNLIFAIEQY 1210 1220 1230 1240 1250 1260 EKFLIHLSKK SKVNLMQHMK LSTSRDFKIK GNILDMVLRE DGEDENEEGT ASEHGGQNKE PAKKKRKK
	Isoform 4 [UniParc]. Checksum: 8C0E5CC711546A8B	FASTA	252	27,824
	10 20 30 40 50 60 MDQKILSLAA EKTADKLQEF LQTLREGDLT NLLQNQAVKG KVAGALLRAI FKGSPCSEEA 70 80 90 100 110 120 GTLRRRKIYT CCIQLVESGD LQKEIASEII GLLMLEAHHF PGPLLVELAN EFISAVREGS 130 140 150 160 170 180 LVNGKSLELL PIILTALATK KENLAYGKGV LSGEECKKQL INTLCSGRWD QQYVIQLTSM 190 200 210 220 230 240 FKDVPLTAEE VEFVVEKALS MFSKMNLQEI PPLVYQLLVL SSKGSRKSVL EGIIAFFSAL 250 DKQHNEEQSG DE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 17412408] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, UBIQUITINATION AT LYS-523, PHOSPHORYLATION AT SER-730; THR-952 AND SER-1121, SUBCELLULAR LOCATION, INTERACTION WITH FANCD2, VARIANTS FA LEU-55 AND GLN-1285, CHARACTERIZATION OF VARIANTS FA LEU-55 AND GLN-1285.
[2]	"FANCI is a second monoubiquitinated member of the Fanconi anemia pathway." Sims A.E., Spiteri E., Sims R.J. III, Arita A.G., Lach F.P., Landers T., Wurm M., Freund M., Neveling K., Hanenberg H., Auerbach A.D., Huang T.T. Nat. Struct. Mol. Biol. 14:564-567(2007) [PubMed: 17460694] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, UBIQUITINATION AT LYS-523, SUBCELLULAR LOCATION, INTERACTION WITH FANCD2, VARIANT FA TYR-858.
[3]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed: 16572171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), VARIANT VAL-86. Tissue: Brain and Skin.
[5]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 175-1324 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 342-1328 (ISOFORM 1), VARIANT SER-742. Tissue: Teratocarcinoma.
[6]	"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. DNA Res. 8:85-95(2001) [PubMed: 11347906] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 527-1328 (ISOFORM 3), VARIANT SER-742. Tissue: Brain.
[7]	Bienvenut W.V. Submitted (JUN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 438-447; 781-788; 809-819; 885-897; 965-994 AND 1079-1094, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[8]	"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling." Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z. EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-215, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Identification of the Fanconi anemia complementation group I gene, FANCI." Dorsman J.C., Levitus M., Rockx D., Rooimans M.A., Oostra A.B., Haitjema A., Bakker S.T., Steltenpool J., Schuler D., Mohan S., Schindler D., Arwert F., Pals G., Mathew C.G., Waisfisz Q., de Winter J.P., Joenje H. Cell. Oncol. 29:211-218(2007) [PubMed: 17452773] [Abstract] Cited for: FUNCTION, VARIANT FANCI GLN-1285, VARIANT LEU-55.
[11]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730; THR-952 AND SER-1121, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Replication stress induces sister-chromatid bridging at fragile site loci in mitosis." Chan K.L., Palmai-Pallag T., Ying S., Hickson I.D. Nat. Cell Biol. 11:753-760(2009) [PubMed: 19465922] [Abstract] Cited for: SUBCELLULAR LOCATION.
[17]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to DNA damage by monoubiquitinated FANCD2." MacKay C., Declais A.C., Lundin C., Agostinho A., Deans A.J., MacArtney T.J., Hofmann K., Gartner A., West S.C., Helleday T., Lilley D.M., Rouse J. Cell 142:65-76(2010) [PubMed: 20603015] [Abstract] Cited for: INTERACTION WITH MTMR15.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Fanconi Anemia Mutation Database

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	EF469766 mRNA. Translation: ABP88002.1. EF567077 mRNA. Translation: ABQ63084.1. AC124068 Genomic DNA. No translation available. BC004277 mRNA. Translation: AAH04277.1. Different initiation. BC140769 mRNA. Translation: AAI40770.1. AK001581 mRNA. Translation: BAA91770.1. Different initiation. AK027564 mRNA. Translation: BAB55200.1. Different initiation. AB058697 mRNA. Translation: BAB47423.1.
IPI	IPI00019447. IPI00306518. IPI00784704. IPI00884225.
RefSeq	NP_001106849.1. NM_001113378.1. NP_060663.2. NM_018193.2.
UniGene	Hs.513126.
3D structure databases
ProteinModelPortal	Q9NVI1.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29381N.
IntAct	Q9NVI1. 6 interactions.
MINT	MINT-1138578.
STRING	Q9NVI1.
PTM databases
PhosphoSite	Q9NVI1.
Polymorphism databases
DMDM	212276518.
Proteomic databases
PRIDE	Q9NVI1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000310775; ENSP00000310842; ENSG00000140525.
GeneID	55215.
KEGG	hsa:55215.
UCSC	uc002bnm.1. human. uc002bnp.1. human.
Organism-specific databases
CTD	55215.
GeneCards	GC15P089787.
H-InvDB	HIX0012562.
HGNC	HGNC:25568. FANCI.
HPA	HPA039972.
MIM	227650. phenotype. 609053. phenotype. 611360. gene.
neXtProt	NX_Q9NVI1.
Orphanet	84. Fanconi anemia.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05441.
GeneTree	ENSGT00390000005855.
HOVERGEN	HBG106622.
InParanoid	Q9NVI1.
OMA	EEVDWLI.
PhylomeDB	Q9NVI1.
Enzyme and pathway databases
Reactome	REACT_216. DNA Repair.
Gene expression databases
ArrayExpress	Q9NVI1.
Bgee	Q9NVI1.
CleanEx	HS_FANCI.
Genevestigator	Q9NVI1.
GermOnline	ENSG00000140525. Homo sapiens.
Family and domain databases
KO	K10895.
ProtoNet	Search...
Other
NextBio	59172.
SOURCE	Search...

Entry information

Entry name

FANCI_HUMAN

Accession

Primary (citable) accession number: Q9NVI1
Secondary accession number(s): A4ZVE4 , A5YMH4, A6NJZ0, Q96JN1, Q96ST0, Q9BT96

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	November 4, 2008
Last modified:	January 25, 2012
This is version 80 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.