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Q9UG63

- ABCF2_HUMAN

UniProt

Q9UG63 - ABCF2_HUMAN

Protein

ATP-binding cassette sub-family F member 2

Gene

ABCF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (24 Jan 2001)
      Previous versions | rss
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    Functioni

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi118 – 1258ATP 1PROSITE-ProRule annotation
    Nucleotide bindingi430 – 4378ATP 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATPase activity Source: InterPro
    2. ATP binding Source: ProtInc
    3. transporter activity Source: ProtInc

    GO - Biological processi

    1. transport Source: ProtInc

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-binding cassette sub-family F member 2
    Alternative name(s):
    Iron-inhibited ABC transporter 2
    Gene namesi
    Name:ABCF2
    ORF Names:HUSSY-18
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:71. ABCF2.

    Subcellular locationi

    GO - Cellular componenti

    1. ATP-binding cassette (ABC) transporter complex Source: ProtInc
    2. membrane Source: UniProtKB
    3. mitochondrial envelope Source: ProtInc

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24406.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 623623ATP-binding cassette sub-family F member 2PRO_0000093323Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei304 – 3041N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UG63.
    PaxDbiQ9UG63.
    PRIDEiQ9UG63.

    PTM databases

    PhosphoSiteiQ9UG63.

    Miscellaneous databases

    PMAP-CutDBQ9UG63.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UG63.
    BgeeiQ9UG63.
    CleanExiHS_ABCF2.
    GenevestigatoriQ9UG63.

    Organism-specific databases

    HPAiCAB020682.
    HPA020091.
    HPA021815.
    HPA030388.

    Interactioni

    Protein-protein interaction databases

    BioGridi115372. 11 interactions.
    IntActiQ9UG63. 3 interactions.
    MINTiMINT-3079728.
    STRINGi9606.ENSP00000222388.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UG63.
    SMRiQ9UG63. Positions 98-609.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini86 – 325240ABC transporter 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini396 – 613218ABC transporter 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 ABC transporter domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0488.
    HOGENOMiHOG000271637.
    HOVERGENiHBG050440.
    InParanoidiQ9UG63.
    KOiK06185.
    OrthoDBiEOG7RJPQW.
    PhylomeDBiQ9UG63.
    TreeFamiTF105208.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR003439. ABC_transporter-like.
    IPR017871. ABC_transporter_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00005. ABC_tran. 2 hits.
    [Graphical view]
    SMARTiSM00382. AAA. 2 hits.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00211. ABC_TRANSPORTER_1. 1 hit.
    PS50893. ABC_TRANSPORTER_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UG63-1) [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

    MPSDLAKKKA AKKKEAAKAR QRPRKGHEEN GDVVTEPQVA EKNEANGRET    50
    TEVDLLTKEL EDFEMKKAAA RAVTGVLASH PNSTDVHIIN LSLTFHGQEL 100
    LSDTKLELNS GRRYGLIGLN GIGKSMLLSA IGKREVPIPE HIDIYHLTRE 150
    MPPSDKTPLH CVMEVDTERA MLEKEAERLA HEDAECEKLM ELYERLEELD 200
    ADKAEMRASR ILHGLGFTPA MQRKKLKDFS GGWRMRVALA RALFIRPFML 250
    LLDEPTNHLD LDACVWLEEE LKTFKRILVL VSHSQDFLNG VCTNIIHMHN 300
    KKLKYYTGNY DQYVKTRLEL EENQMKRFHW EQDQIAHMKN YIARFGHGSA 350
    KLARQAQSKE KTLQKMMASG LTERVVSDKT LSFYFPPCGK IPPPVIMVQN 400
    VSFKYTKDGP CIYNNLEFGI DLDTRVALVG PNGAGKSTLL KLLTGELLPT 450
    DGMIRKHSHV KIGRYHQHLQ EQLDLDLSPL EYMMKCYPEI KEKEEMRKII 500
    GRYGLTGKQQ VSPIRNLSDG QKCRVCLAWL AWQNPHMLFL DEPTNHLDIE 550
    TIDALADAIN EFEGGMMLVS HDFRLIQQVA QEIWVCEKQT ITKWPGDILA 600
    YKEHLKSKLV DEEPQLTKRT HNV 623
    Length:623
    Mass (Da):71,290
    Last modified:January 24, 2001 - v2
    Checksum:i702A968BCF8061AE
    GO
    Isoform 2 (identifier: Q9UG63-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         623-623: V → VCTLTLASLPRP

    Show »
    Length:634
    Mass (Da):72,444
    Checksum:iFCB0633F0D9BA0DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391V → A in AAG13902. (PubMed:10944468)Curated
    Sequence conflicti39 – 391V → A in AAG13903. (PubMed:10944468)Curated
    Sequence conflicti74 – 741T → A in CAA06290. (PubMed:11124703)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei623 – 6231V → VCTLTLASLPRP in isoform 2. 1 PublicationVSP_054715

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF261091 mRNA. Translation: AAG13902.1.
    AF261092 mRNA. Translation: AAG13903.1.
    BT007451 mRNA. Translation: AAP36119.1.
    AL050291 mRNA. Translation: CAB43392.1.
    AC021097 Genomic DNA. Translation: AAS00378.1.
    AC021097 Genomic DNA. Translation: AAS00379.1.
    CH471173 Genomic DNA. Translation: EAW54014.1.
    CH471173 Genomic DNA. Translation: EAW54016.1.
    CH471173 Genomic DNA. Translation: EAW54017.1.
    BC001661 mRNA. Translation: AAH01661.1.
    AJ005016 mRNA. Translation: CAA06290.1.
    CCDSiCCDS5922.1. [Q9UG63-2]
    CCDS5923.1. [Q9UG63-1]
    PIRiT08810.
    RefSeqiNP_005683.2. NM_005692.4. [Q9UG63-2]
    NP_009120.1. NM_007189.2. [Q9UG63-1]
    XP_005249988.1. XM_005249931.2. [Q9UG63-2]
    XP_006715887.1. XM_006715824.1. [Q9UG63-2]
    UniGeneiHs.654958.

    Genome annotation databases

    EnsembliENST00000222388; ENSP00000222388; ENSG00000033050. [Q9UG63-2]
    ENST00000287844; ENSP00000287844; ENSG00000033050. [Q9UG63-1]
    GeneIDi10061.
    KEGGihsa:10061.
    UCSCiuc003wjo.1. human.
    uc003wjp.3. human. [Q9UG63-1]

    Polymorphism databases

    DMDMi12643306.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    ABCMdb

    Database for mutations in ABC proteins

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF261091 mRNA. Translation: AAG13902.1 .
    AF261092 mRNA. Translation: AAG13903.1 .
    BT007451 mRNA. Translation: AAP36119.1 .
    AL050291 mRNA. Translation: CAB43392.1 .
    AC021097 Genomic DNA. Translation: AAS00378.1 .
    AC021097 Genomic DNA. Translation: AAS00379.1 .
    CH471173 Genomic DNA. Translation: EAW54014.1 .
    CH471173 Genomic DNA. Translation: EAW54016.1 .
    CH471173 Genomic DNA. Translation: EAW54017.1 .
    BC001661 mRNA. Translation: AAH01661.1 .
    AJ005016 mRNA. Translation: CAA06290.1 .
    CCDSi CCDS5922.1. [Q9UG63-2 ]
    CCDS5923.1. [Q9UG63-1 ]
    PIRi T08810.
    RefSeqi NP_005683.2. NM_005692.4. [Q9UG63-2 ]
    NP_009120.1. NM_007189.2. [Q9UG63-1 ]
    XP_005249988.1. XM_005249931.2. [Q9UG63-2 ]
    XP_006715887.1. XM_006715824.1. [Q9UG63-2 ]
    UniGenei Hs.654958.

    3D structure databases

    ProteinModelPortali Q9UG63.
    SMRi Q9UG63. Positions 98-609.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115372. 11 interactions.
    IntActi Q9UG63. 3 interactions.
    MINTi MINT-3079728.
    STRINGi 9606.ENSP00000222388.

    PTM databases

    PhosphoSitei Q9UG63.

    Polymorphism databases

    DMDMi 12643306.

    Proteomic databases

    MaxQBi Q9UG63.
    PaxDbi Q9UG63.
    PRIDEi Q9UG63.

    Protocols and materials databases

    DNASUi 10061.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222388 ; ENSP00000222388 ; ENSG00000033050 . [Q9UG63-2 ]
    ENST00000287844 ; ENSP00000287844 ; ENSG00000033050 . [Q9UG63-1 ]
    GeneIDi 10061.
    KEGGi hsa:10061.
    UCSCi uc003wjo.1. human.
    uc003wjp.3. human. [Q9UG63-1 ]

    Organism-specific databases

    CTDi 10061.
    GeneCardsi GC07M150904.
    HGNCi HGNC:71. ABCF2.
    HPAi CAB020682.
    HPA020091.
    HPA021815.
    HPA030388.
    MIMi 612510. gene.
    neXtProti NX_Q9UG63.
    PharmGKBi PA24406.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0488.
    HOGENOMi HOG000271637.
    HOVERGENi HBG050440.
    InParanoidi Q9UG63.
    KOi K06185.
    OrthoDBi EOG7RJPQW.
    PhylomeDBi Q9UG63.
    TreeFami TF105208.

    Miscellaneous databases

    ChiTaRSi ABCF2. human.
    GeneWikii ABCF2.
    GenomeRNAii 10061.
    NextBioi 38023.
    PMAP-CutDB Q9UG63.
    PROi Q9UG63.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UG63.
    Bgeei Q9UG63.
    CleanExi HS_ABCF2.
    Genevestigatori Q9UG63.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR003439. ABC_transporter-like.
    IPR017871. ABC_transporter_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00005. ABC_tran. 2 hits.
    [Graphical view ]
    SMARTi SM00382. AAA. 2 hits.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS00211. ABC_TRANSPORTER_1. 1 hit.
    PS50893. ABC_TRANSPORTER_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs."
      Ye Z., Connor J.R.
      Biochem. Biophys. Res. Commun. 275:223-227(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Uterus.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1).
      Tissue: Colon.
    7. "Characterization of 16 novel human genes showing high similarity to yeast sequences."
      Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G.
      Yeast 18:69-80(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-623.
      Tissue: Lung.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiABCF2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UG63
    Secondary accession number(s): O60864
    , Q75MJ0, Q75MJ1, Q96TE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Caution

    Lacks transmembrane domains and is probably not involved in transport.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3