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Q8IYD8 (FANCM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fanconi anemia group M protein

Short name=Protein FACM
EC=3.6.4.13
Alternative name(s):
ATP-dependent RNA helicase FANCM
Fanconi anemia-associated polypeptide of 250 kDa
Short name=FAAP250
Protein Hef ortholog
Gene names
Name:FANCM
Synonyms:KIAA1596
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2048 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATPase required for FANCD2 ubiquitination, a key reaction in DNA repair. Binds to ssDNA but not to dsDNA. Recruited to forks stalled by DNA interstrand cross-links, and required for cellular resistance to such lesions. Ref.1 Ref.6 Ref.8 Ref.9

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Belongs to the multisubunit FA complex composed of APITD1, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9, FANCM, FAAP24 and STRA13/CENPX. The complex is not found in FA patients. Interacts with APITD1/CENPS, FAAP24 and EME1. Ref.1 Ref.7 Ref.8 Ref.9

Subcellular location

Nucleus Ref.1 Ref.8 Ref.9.

Post-translational modification

Phosphorylated; hyperphosphorylated in response to genotoxic stress. Ref.1

Involvement in disease

Fanconi anemia complementation group M (FANCM) [MIM:614087]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1

Sequence similarities

Belongs to the DEAD box helicase family. DEAH subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence BAB13422.1 differs from that shown. Reason: Intron retention.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IYD8-1)

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: Q8IYD8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     669-669: M → K
     670-2048: Missing.
Isoform 3 (identifier: Q8IYD8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     228-253: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20482048Fanconi anemia group M protein
PRO_0000055176

Regions

Domain98 – 266169Helicase ATP-binding
Domain452 – 627176Helicase C-terminal
Nucleotide binding111 – 1188ATP Probable
Region1727 – 2048322Interaction with FAAP24 and EME1
Motif214 – 2174DEAH box

Natural variations

Alternative sequence228 – 25326Missing in isoform 3.
VSP_054504
Alternative sequence6691M → K in isoform 2.
VSP_015989
Alternative sequence670 – 20481379Missing in isoform 2.
VSP_015990
Natural variant1751S → F.
Corresponds to variant rs10138997 [ dbSNP | Ensembl ].
VAR_023697
Natural variant2081I → M.
Corresponds to variant rs45547534 [ dbSNP | Ensembl ].
VAR_061827
Natural variant8781V → L. Ref.5
Corresponds to variant rs1367580 [ dbSNP | Ensembl ].
VAR_023698
Natural variant18121P → A. Ref.5
Corresponds to variant rs3736772 [ dbSNP | Ensembl ].
VAR_023699

Experimental info

Mutagenesis1161G → A: Reduces ATPase activity. Ref.6
Mutagenesis1171K → R: Abolishes ATPase activity. Ref.1
Sequence conflict681L → F in BAC04159. Ref.2
Sequence conflict14601I → V in BAB13422. Ref.5

Secondary structure

........................................................ 2048
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 25, 2005. Version 2.
Checksum: BDE0D6640B73C255

FASTA2,048232,191
        10         20         30         40         50         60 
MSGRQRTLFQ TWGSSISRSS GTPGCSSGTE RPQSPGSSKA PLPAAAEAQL ESDDDVLLVA 

        70         80         90        100        110        120 
AYEAERQLCL ENGGFCTSAG ALWIYPTNCP VRDYQLHISR AALFCNTLVC LPTGLGKTFI 

       130        140        150        160        170        180 
AAVVMYNFYR WFPSGKVVFM APTKPLVTQQ IEACYQVMGI PQSHMAEMTG STQASTRKEI 

       190        200        210        220        230        240 
WCSKRVLFLT PQVMVNDLSR GACPAAEIKC LVIDEAHKAL GNYAYCQVVR ELVKYTNHFR 

       250        260        270        280        290        300 
ILALSATPGS DIKAVQQVIT NLLIGQIELR SEDSPDILTY SHERKVEKLI VPLGEELAAI 

       310        320        330        340        350        360 
QKTYIQILES FARSLIQRNV LMRRDIPNLT KYQIILARDQ FRKNPSPNIV GIQQGIIEGE 

       370        380        390        400        410        420 
FAICISLYHG YELLQQMGMR SLYFFLCGIM DGTKGMTRSK NELGRNEDFM KLYNHLECMF 

       430        440        450        460        470        480 
ARTRSTSANG ISAIQQGDKN KKFVYSHPKL KKLEEVVIEH FKSWNAENTT EKKRDETRVM 

       490        500        510        520        530        540 
IFSSFRDSVQ EIAEMLSQHQ PIIRVMTFVG HASGKSTKGF TQKEQLEVVK QFRDGGYNTL 

       550        560        570        580        590        600 
VSTCVGEEGL DIGEVDLIIC FDSQKSPIRL VQRMGRTGRK RQGRIVIILS EGREERIYNQ 

       610        620        630        640        650        660 
SQSNKRSIYK AISSNRQVLH FYQRSPRMVP DGINPKLHKM FITHGVYEPE KPSRNLQRKS 

       670        680        690        700        710        720 
SIFSYRDGMR QSSLKKDWFL SEEEFKLWNR LYRLRDSDEI KEITLPQVQF SSLQNEENKP 

       730        740        750        760        770        780 
AQESTTGIHQ LSLSEWRLWQ DHPLPTHQVD HSDRCRHFIG LMQMIEGMRH EEGECSYELE 

       790        800        810        820        830        840 
VESYLQMEDV TSTFIAPRNE SNNLASDTFI THKKSSFIKN INQGSSSSVI ESDEECAEIV 

       850        860        870        880        890        900 
KQTHIKPTKI VSLKKKVSKE IKKDQLKKEN NHGIIDSVDN DRNSTVENIF QEDLPNDKRT 

       910        920        930        940        950        960 
SDTDEIAATC TINENVIKEP CVLLTECQFT NKSTSSLAGN VLDSGYNSFN DEKSVSSNLF 

       970        980        990       1000       1010       1020 
LPFEEELYIV RTDDQFYNCH SLTKEVLANV ERFLSYSPPP LSGLSDLEYE IAKGTALENL 

      1030       1040       1050       1060       1070       1080 
LFLPCAEHLR SDKCTCLLSH SAVNSQQNLE LNSLKCINYP SEKSCLYDIP NDNISDEPSL 

      1090       1100       1110       1120       1130       1140 
CDCDVHKHNQ NENLVPNNRV QIHRSPAQNL VGENNHDVDN SDLPVLSTDQ DESLLLFEDV 

      1150       1160       1170       1180       1190       1200 
NTEFDDVSLS PLNSKSESLP VSDKTAISET PLVSQFLISD ELLLDNNSEL QDQITRDANS 

      1210       1220       1230       1240       1250       1260 
FKSRDQRGVQ EEKVKNHEDI FDCSRDLFSV TFDLGFCSPD SDDEILEHTS DSNRPLDDLY 

      1270       1280       1290       1300       1310       1320 
GRYLEIKEIS DANYVSNQAL IPRDHSKNFT SGTVIIPSNE DMQNPNYVHL PLSAAKNEEL 

      1330       1340       1350       1360       1370       1380 
LSPGYSQFSL PVQKKVMSTP LSKSNTLNSF SKIRKEILKT PDSSKEKVNL QRFKEALNST 

      1390       1400       1410       1420       1430       1440 
FDYSEFSLEK SKSSGPMYLH KSCHSVEDGQ LLTSNESEDD EIFRRKVKRA KGNVLNSPED 

      1450       1460       1470       1480       1490       1500 
QKNSEVDSPL HAVKKRRFPI NRSELSSSDE SENFPKPCSQ LEDFKVCNGN ARRGIKVPKR 

      1510       1520       1530       1540       1550       1560 
QSHLKHVARK FLDDEAELSE EDAEYVSSDE NDESENEQDS SLLDFLNDET QLSQAINDSE 

      1570       1580       1590       1600       1610       1620 
MRAIYMKSLR SPMMNNKYKM IHKTHKNINI FSQIPEQDET YLEDSFCVDE EESCKGQSSE 

      1630       1640       1650       1660       1670       1680 
EEVCVDFNLI TDDCFANSKK YKTRRAVMLK EMMEQNCAHS KKKLSRIILP DDSSEEENNV 

      1690       1700       1710       1720       1730       1740 
NDKRESNIAV NPSTVKKNKQ QDHCLNSVPS GSSAQSKVRS TPRVNPLAKQ SKQTSLNLKD 

      1750       1760       1770       1780       1790       1800 
TISEVSDFKP QNHNEVQSTT PPFTTVDSQK DCRKFPVPQK DGSALEDSST SGASCSKSRP 

      1810       1820       1830       1840       1850       1860 
HLAGTHTSLR LPQEGKGTCI LVGGHEITSG LEVISSLRAI HGLQVEVCPL NGCDYIVSNR 

      1870       1880       1890       1900       1910       1920 
MVVERRSQSE MLNSVNKNKF IEQIQHLQSM FERICVIVEK DREKTGDTSR MFRRTKSYDS 

      1930       1940       1950       1960       1970       1980 
LLTTLIGAGI RILFSSCQEE TADLLKELSL VEQRKNVGIH VPTVVNSNKS EALQFYLSIP 

      1990       2000       2010       2020       2030       2040 
NISYITALNM CHQFSSVKRM ANSSLQEISM YAQVTHQKAE EIYRYIHYVF DIQMLPNDLN 


QDRLKSDI 

« Hide

Isoform 2 [UniParc].

Checksum: A10DBC94FFA28C0B
Show »

FASTA66975,579
Isoform 3 [UniParc].

Checksum: F31611E4697FA196
Show »

FASTA2,022229,281

References

« Hide 'large scale' references
[1]"A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M."
Meetei A.R., Medhurst A.L., Ling C., Xue Y., Singh T.R., Bier P., Steltenpool J., Stone S., Dokal I., Mathew C.G., Hoatlin M., Joenje H., de Winter J.P., Wang W.
Nat. Genet. 37:958-963(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; FANCE; FANCF; FANCG AND FANCL, SUBCELLULAR LOCATION, INVOLVEMENT IN FANCM, PHOSPHORYLATION, FUNCTION, MUTAGENESIS OF LYS-117.
[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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Testis.
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Brain and Testis.
[5]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 794-2048 (ISOFORM 1), VARIANTS LEU-878 AND ALA-1812.
Tissue: Brain.
[6]"The vertebrate Hef ortholog is a component of the Fanconi anemia tumor-suppressor pathway."
Mosedale G., Niedzwiedz W., Alpi A., Perrina F., Pereira-Leal J.B., Johnson M., Langevin F., Pace P., Patel K.J.
Nat. Struct. Mol. Biol. 12:763-771(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, MUTAGENESIS OF GLY-116, IDENTIFICATION AS PART OF THE FA COMPLEX, FUNCTION.
[7]"Identification of FAAP24, a Fanconi anemia core complex protein that interacts with FANCM."
Ciccia A., Ling C., Coulthard R., Yan Z., Xue Y., Meetei A.R., Laghmani el H., Joenje H., McDonald N., de Winter J.P., Wang W., West S.C.
Mol. Cell 25:331-343(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EME1 AND FAAP24.
[8]"A histone-fold complex and FANCM form a conserved DNA-remodeling complex to maintain genome stability."
Yan Z., Delannoy M., Ling C., Daee D., Osman F., Muniandy P.A., Shen X., Oostra A.B., Du H., Steltenpool J., Lin T., Schuster B., Decaillet C., Stasiak A., Stasiak A.Z., Stone S., Hoatlin M.E., Schindler D. expand/collapse author list , Woodcock C.L., Joenje H., Sen R., de Winter J.P., Li L., Seidman M.M., Whitby M.C., Myung K., Constantinousend A., Wang W.
Mol. Cell 37:865-878(2010)
Cited for: IDENTIFICATION IN THE FA CORE COMPLEX, INTERACTION WITH APITD1, SUBCELLULAR LOCATION, FUNCTION.
[9]"MHF1-MHF2, a histone-fold-containing protein complex, participates in the Fanconi anemia pathway via FANCM."
Singh T.R., Saro D., Ali A.M., Zheng X.-F., Du C., Killen M.W., Sachpatzidis A., Wahengbam K., Pierce A.J., Xiong Y., Sung P., Meetei A.R.
Mol. Cell 37:879-886(2010)
Cited for: IDENTIFICATION IN THE FA CORE COMPLEX, INTERACTION WITH APITD1, SUBCELLULAR LOCATION, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ140356 mRNA. Translation: AAZ53290.1.
AK093422 mRNA. Translation: BAC04159.1.
AL121809 Genomic DNA. No translation available.
BC036056 mRNA. Translation: AAH36056.1.
BC140776 mRNA. Translation: AAI40777.1.
BC144511 mRNA. Translation: AAI44512.1.
AB046816 mRNA. Translation: BAB13422.1. Sequence problems.
CCDSCCDS32070.1. [Q8IYD8-1]
RefSeqNP_065988.1. NM_020937.2. [Q8IYD8-1]
XP_005267986.1. XM_005267929.1. [Q8IYD8-3]
UniGeneHs.509229.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BXOX-ray2.15A1798-2048[»]
4DAYX-ray3.30C1218-1251[»]
4DRBX-ray2.63C/F/I661-800[»]
4E45X-ray2.00E/J/O667-800[»]
4M6WX-ray2.90A1813-2031[»]
ProteinModelPortalQ8IYD8.
SMRQ8IYD8. Positions 92-602, 675-790, 1818-2035.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121722. 28 interactions.
DIPDIP-43972N.
IntActQ8IYD8. 6 interactions.
MINTMINT-4789123.
STRING9606.ENSP00000267430.

PTM databases

PhosphoSiteQ8IYD8.

Polymorphism databases

DMDM78099254.

Proteomic databases

MaxQBQ8IYD8.
PaxDbQ8IYD8.
PRIDEQ8IYD8.

Protocols and materials databases

DNASU57697.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267430; ENSP00000267430; ENSG00000187790. [Q8IYD8-1]
ENST00000542564; ENSP00000442493; ENSG00000187790.
ENST00000556036; ENSP00000450596; ENSG00000187790. [Q8IYD8-2]
GeneID57697.
KEGGhsa:57697.
UCSCuc001wwc.2. human. [Q8IYD8-2]
uc001wwd.4. human. [Q8IYD8-1]

Organism-specific databases

CTD57697.
GeneCardsGC14P045605.
GeneReviewsFANCM.
HGNCHGNC:23168. FANCM.
HPAHPA055144.
MIM609644. gene.
614087. phenotype.
neXtProtNX_Q8IYD8.
Orphanet84. Fanconi anemia.
PharmGKBPA134943156.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1948.
HOGENOMHOG000112498.
HOVERGENHBG081520.
InParanoidQ8IYD8.
KOK10896.
OMASIYKAIS.
OrthoDBEOG7B8S3M.
PhylomeDBQ8IYD8.
TreeFamTF324610.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ8IYD8.
BgeeQ8IYD8.
CleanExHS_FANCM.
GenevestigatorQ8IYD8.

Family and domain databases

Gene3D3.40.50.10130. 1 hit.
3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR020819. DNA_repair_nuc_XPF/helicase.
IPR006166. ERCC4_domain.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR011335. Restrct_endonuc-II-like.
IPR010994. RuvA_2-like.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF02732. ERCC4. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00891. ERCC4. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF47781. SSF47781. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF52980. SSF52980. 1 hit.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi57697.
NextBio35468386.
PROQ8IYD8.
SOURCESearch...

Entry information

Entry nameFANCM_HUMAN
AccessionPrimary (citable) accession number: Q8IYD8
Secondary accession number(s): B2RTQ9 expand/collapse secondary AC list , Q3YFH9, Q8N9X6, Q9HCH6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: July 9, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM