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Q9BQS8 (FYCO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
FYVE and coiled-coil domain-containing protein 1
Alternative name(s):
Zinc finger FYVE domain-containing protein 7
Gene names
Name:FYCO1
Synonyms:ZFYVE7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May mediate microtubule plus end-directed vesicle transport. Ref.9

Subunit structure

Can form homodimers. Interacts (via C-terminus) with MAP1LC3B. Interacts with RAB7A; the interaction with RAB7A induces FYCO1 recruitment to late endosomal/lysosomal compartments. Interacts with MAP1LC3B By similarity. Ref.9 Ref.14

Subcellular location

Cytoplasmic vesicleautophagosome. Endosome. Lysosome. Note: Localizes to the external but not to the internal membrane of autophagosomes, and upon autophagosome/late endosome/lysosome fusion, it stays on the external surface of autolysosomes. Ref.9 Ref.10

Tissue specificity

Expressed in heart and skeletal muscle. Ref.1

Involvement in disease

Cataract 18 (CTRCT18) [MIM:610019]: An opacification of the crystalline lens of the eye becoming evident at birth or in infancy. It frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function.
Note: The disease is caused by mutations affecting the gene represented in this entry. Pathogenic mutations in FYCO1 can affect intracellular transport of autophagocytic vesicles from the perinuclear area to the periphery, leading to an accumulation of large numbers of vesicles and hence loss of lens transparency (Ref.10). Ref.10

Sequence similarities

Contains 1 FYVE-type zinc finger.

Contains 1 GOLD domain.

Contains 1 RUN domain.

Sequence caution

The sequence AAH07218.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB14559.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB84991.1 differs from that shown. Reason: Frameshift at position 1402.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BQS8-1)

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: Q9BQS8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     376-380: QQKAD → LHVGD
     381-1478: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9BQS8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     376-380: QQKAD → HLSE
     381-1478: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9BQS8-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1315-1315: Q → QASVGASKGLGNLLCESSACR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 14781477FYVE and coiled-coil domain-containing protein 1
PRO_0000245837

Regions

Domain36 – 169134RUN
Domain1337 – 1466130GOLD
Zinc finger1173 – 123159FYVE-type
Coiled coil4 – 3330 Potential
Coiled coil225 – 28056 Potential
Coiled coil394 – 555162 Potential
Coiled coil596 – 1151556 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.12 Ref.13
Modified residue3811Phosphothreonine By similarity
Modified residue8781Phosphoserine Ref.7

Natural variations

Alternative sequence376 – 3805QQKAD → LHVGD in isoform 2.
VSP_019795
Alternative sequence376 – 3805QQKAD → HLSE in isoform 3.
VSP_019796
Alternative sequence381 – 14781098Missing in isoform 2 and isoform 3.
VSP_019797
Alternative sequence13151Q → QASVGASKGLGNLLCESSAC R in isoform 4.
VSP_054477
Natural variant2501R → Q. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs4683158 [ dbSNP | Ensembl ].
VAR_027006
Natural variant2821R → H.
Corresponds to variant rs9875356 [ dbSNP | Ensembl ].
VAR_027007
Natural variant3211G → A. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs3733100 [ dbSNP | Ensembl ].
VAR_027008
Natural variant3811T → M.
Corresponds to variant rs3733101 [ dbSNP | Ensembl ].
VAR_027009
Natural variant4471R → C.
Corresponds to variant rs33910087 [ dbSNP | Ensembl ].
VAR_056882
Natural variant6791A → V. Ref.2
Corresponds to variant rs3796375 [ dbSNP | Ensembl ].
VAR_027010
Natural variant9941E → K.
Corresponds to variant rs34801630 [ dbSNP | Ensembl ].
VAR_056883
Natural variant10011N → D.
Corresponds to variant rs13059238 [ dbSNP | Ensembl ].
VAR_027011
Natural variant13761L → P in CTRCT18. Ref.10
VAR_065974

Experimental info

Sequence conflict1551Y → C in CAD91151. Ref.2
Sequence conflict3591D → G in CAD91151. Ref.2
Sequence conflict3651L → S in BAB14559. Ref.5
Sequence conflict3811T → S in CAC33883. Ref.1
Sequence conflict9161T → I in CAD89924. Ref.2
Sequence conflict9641K → E in CAD89924. Ref.2
Sequence conflict13821A → P in CAC33883. Ref.1
Sequence conflict13851G → A in CAC33883. Ref.1

Sequences

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

Last modified February 8, 2011. Version 3.
Checksum: 11AB671A9F2B3D21

FASTA1,478166,983
        10         20         30         40         50         60 
MASTNAESQL QRIIRDLQDA VTELSKEFQE AGEPITDDST SLHKFSYKLE YLLQFDQKEK 

        70         80         90        100        110        120 
ATLLGNKKDY WDYFCACLAK VKGANDGIRF VKSISELRTS LGKGRAFIRY SLVHQRLADT 

       130        140        150        160        170        180 
LQQCFMNTKV TSDWYYARSP FLQPKLSSDI VGQLYELTEV QFDLASRGFD LDAAWPTFAR 

       190        200        210        220        230        240 
RTLTTGSSAY LWKPPSRSSS MSSLVSSYLQ TQEMVSNFDL NSPLNNEALE GFDEMRLELD 

       250        260        270        280        290        300 
QLEVREKQLR ERMQQLDREN QELRAAVSQQ GEQLQTERER GRTAAEDNVR LTCLVAELQK 

       310        320        330        340        350        360 
QWEVTQATQN TVKELQTCLQ GLELGAAEKE EDYHTALRRL ESMLQPLAQE LEATRDSLDK 

       370        380        390        400        410        420 
KNQHLASFPG WLAMAQQKAD TASDTKGRQE PIPSDAAQEM QELGEKLQAL ERERTKVEEV 

       430        440        450        460        470        480 
NRQQSAQLEQ LVKELQLKED ARASLERLVK EMAPLQEELS GKGQEADQLW RRLQELLAHT 

       490        500        510        520        530        540 
SSWEEELAEL RREKKQQQEE KELLEQEVRS LTRQLQFLET QLAQVSQHVS DLEEQKKQLI 

       550        560        570        580        590        600 
QDKDHLSQQV GMLERLAGPP GPELPVAGEK NEALVPVNSS LQEAWGKPEE EQRGLQEAQL 

       610        620        630        640        650        660 
DDTKVQEGSQ EEELRQANRE LEKELQNVVG RNQLLEGKLQ ALQADYQALQ QRESAIQGSL 

       670        680        690        700        710        720 
ASLEAEQASI RHLGDQMEAS LLAVRKAKEA MKAQMAEKEA ILQSKEGECQ QLREEVEQCQ 

       730        740        750        760        770        780 
QLAEARHREL RALESQCQQQ TQLIEVLTAE KGQQGVGPPT DNEARELAAQ LALSQAQLEV 

       790        800        810        820        830        840 
HQGEVQRLQA QVVDLQAKMR AALDDQDKVQ SQLSMAEAVL REHKTLVQQL KEQNEALNRA 

       850        860        870        880        890        900 
HVQELLQCSE REGALQEERA DEAQQREEEL RALQEELSQA KCSSEEAQLE HAELQEQLHR 

       910        920        930        940        950        960 
ANTDTAELGI QVCALTVEKE RVEEALACAV QELQDAKEAA SREREGLERQ VAGLQQEKES 

       970        980        990       1000       1010       1020 
LQEKLKAAKA AAGSLPGLQA QLAQAEQRAQ SLQEAAHQEL NTLKFQLSAE IMDYQSRLKN 

      1030       1040       1050       1060       1070       1080 
AGEECKSLRG QLEEQGRQLQ AAEEAVEKLK ATQADMGEKL SCTSNHLAEC QAAMLRKDKE 

      1090       1100       1110       1120       1130       1140 
GAALREDLER TQKELEKATT KIQEYYNKLC QEVTNRERND QKMLADLDDL NRTKKYLEER 

      1150       1160       1170       1180       1190       1200 
LIELLRDKDA LWQKSDALEF QQKLSAEERW LGDTEANHCL DCKREFSWMV RRHHCRICGR 

      1210       1220       1230       1240       1250       1260 
IFCYYCCNNY VLSKHGGKKE RCCRACFQKL SEGPGSPDSS GSGTSQGEPS PALSPASPGP 

      1270       1280       1290       1300       1310       1320 
QATGGQGANT DYRPPDDAVF DIITDEELCQ IQESGSSLPE TPTETDSLDP NAAEQDTTST 

      1330       1340       1350       1360       1370       1380 
SLTPEDTEDM PVGQDSEICL LKSGELMIKV PLTVDEIASF GEGSRELFVR SSTYSLIPIT 

      1390       1400       1410       1420       1430       1440 
VAEAGLTISW VFSSDPKSIS FSVVFQEAED TPLDQCKVLI PTTRCNSHKE NIQGQLKVRT 

      1450       1460       1470 
PGIYMLIFDN TFSRFVSKKV FYHLTVDRPV IYDGSDFL 

« Hide

Isoform 2 [UniParc].

Checksum: 141833AF14C25727
Show »

FASTA38043,482
Isoform 3 [UniParc].

Checksum: 4B54D9D20257275F
Show »

FASTA37943,427
Isoform 4 [UniParc].

Checksum: BF5ABFEDF2712834
Show »

FASTA1,498168,888

References

« Hide 'large scale' references
[1]"The transcriptional map of the common eliminated region 1 (C3CER1) in 3p21.3."
Kiss H., Yang Y., Kiss C., Andersson K., Klein G., Imreh S., Dumanski J.P.
Eur. J. Hum. Genet. 10:52-61(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS GLN-250 AND ALA-321.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLN-250; ALA-321 AND VAL-679.
Tissue: Skeletal muscle.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [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 1 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-1478 (ISOFORM 2), VARIANTS GLN-250 AND ALA-321.
Tissue: Heart, Lung 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. 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] OF 56-1478 (ISOFORM 3), VARIANTS GLN-250 AND ALA-321.
Tissue: Ovary.
[6]"The nucleotide sequence of a long cDNA clone isolated from human spleen."
Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1213-1478 (ISOFORM 1).
Tissue: Spleen.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[8]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport."
Pankiv S., Alemu E.A., Brech A., Bruun J.A., Lamark T., Overvatn A., Bjorkoy G., Johansen T.
J. Cell Biol. 188:253-269(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH MAP1LC3B AND RAB7A.
[10]"Mutations in FYCO1 cause autosomal-recessive congenital cataracts."
Chen J., Ma Z., Jiao X., Fariss R., Kantorow W.L., Kantorow M., Pras E., Frydman M., Pras E., Riazuddin S., Riazuddin S.A., Hejtmancik J.F.
Am. J. Hum. Genet. 88:827-838(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, VARIANT CTRCT18 PRO-1376.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Autophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellites."
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B., Zhong Q.
Nature 502:254-257(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAP1LC3B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ292348 mRNA. Translation: CAC33883.1.
AL833308 mRNA. Translation: CAD89924.1.
AL832358 mRNA. Translation: CAD91151.1.
AC099782 Genomic DNA. No translation available.
BC007218 mRNA. Translation: AAH07218.1. Different initiation.
BC101468 mRNA. Translation: AAI01469.1.
BC101470 mRNA. Translation: AAI01471.1.
BC143368 mRNA. Translation: AAI43369.1.
AK023397 mRNA. Translation: BAB14559.1. Different initiation.
AK074165 mRNA. Translation: BAB84991.1. Frameshift.
CCDSCCDS2734.1. [Q9BQS8-1]
RefSeqNP_078789.2. NM_024513.3. [Q9BQS8-1]
XP_006713396.1. XM_006713333.1. [Q9BQS8-1]
XP_006713397.1. XM_006713334.1. [Q9BQS8-1]
XP_006713398.1. XM_006713335.1. [Q9BQS8-1]
UniGeneHs.200227.
Hs.739775.

3D structure databases

ProteinModelPortalQ9BQS8.
SMRQ9BQS8. Positions 32-173, 1137-1230, 1385-1469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122669. 23 interactions.
DIPDIP-60600N.
IntActQ9BQS8. 27 interactions.
MINTMINT-8385159.
STRING9606.ENSP00000296137.

PTM databases

PhosphoSiteQ9BQS8.

Polymorphism databases

DMDM322510128.

Proteomic databases

MaxQBQ9BQS8.
PaxDbQ9BQS8.
PRIDEQ9BQS8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296137; ENSP00000296137; ENSG00000163820. [Q9BQS8-1]
ENST00000535325; ENSP00000441178; ENSG00000163820.
GeneID79443.
KEGGhsa:79443.
UCSCuc003cpb.5. human. [Q9BQS8-1]

Organism-specific databases

CTD79443.
GeneCardsGC03M045934.
H-InvDBHIX0003244.
HGNCHGNC:14673. FYCO1.
HPAHPA035526.
MIM607182. gene.
610019. phenotype.
neXtProtNX_Q9BQS8.
Orphanet98991. Nuclear cataract.
PharmGKBPA28453.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262828.
HOVERGENHBG063805.
InParanoidQ9BQS8.
OrthoDBEOG7Z0JVJ.
PhylomeDBQ9BQS8.
TreeFamTF341788.

Gene expression databases

ArrayExpressQ9BQS8.
BgeeQ9BQS8.
CleanExHS_FYCO1.
GenevestigatorQ9BQS8.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR009038. GOLD.
IPR004012. Run.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF01363. FYVE. 1 hit.
PF02759. RUN. 1 hit.
[Graphical view]
SMARTSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMSSF101576. SSF101576. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEPS50866. GOLD. 1 hit.
PS50826. RUN. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFYCO1. human.
GenomeRNAi79443.
NextBio35481191.
PROQ9BQS8.
SOURCESearch...

Entry information

Entry nameFYCO1_HUMAN
AccessionPrimary (citable) accession number: Q9BQS8
Secondary accession number(s): B7ZKT7 expand/collapse secondary AC list , Q3MJE6, Q86T41, Q86TB1, Q8TEF9, Q96IV5, Q9H8P9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: February 8, 2011
Last modified: July 9, 2014
This is version 106 of the entry and version 3 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

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 3

Human chromosome 3: entries, gene names and cross-references to MIM