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Q8NE71

- ABCF1_HUMAN

UniProt

Q8NE71 - ABCF1_HUMAN

Protein

ATP-binding cassette sub-family F member 1

Gene

ABCF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Isoform 2 is required for efficient Cap- and IRES-mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi336 – 3438ATP 1PROSITE-ProRule annotation
    Nucleotide bindingi658 – 6658ATP 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATPase activity Source: InterPro
    2. ATP binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. ribosome binding Source: UniProtKB
    6. translation activator activity Source: UniProtKB
    7. translation factor activity, nucleic acid binding Source: ProtInc

    GO - Biological processi

    1. inflammatory response Source: ProtInc
    2. positive regulation of translation Source: UniProtKB
    3. translation Source: ProtInc
    4. translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Activator

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-binding cassette sub-family F member 1
    Alternative name(s):
    ATP-binding cassette 50
    TNF-alpha-stimulated ABC protein
    Gene namesi
    Name:ABCF1
    Synonyms:ABC50
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:70. ABCF1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. membrane Source: UniProtKB
    3. nuclear envelope Source: UniProtKB
    4. nucleoplasm Source: UniProtKB
    5. polysomal ribosome Source: UniProtKB
    6. ribosome Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi109 – 1091S → A: Reduces phosphorylation. Inhibits strongly phosphorylation by CK2; when associated with S-140. Does not inhibit interaction with EIF2; when associated with S-140. Does not inhibit association with ribosomes; when associated with S-140. Reduces EIF2 interaction with ribosomes; when associated with S-140. Does not inhibit protein synthesis; when associated with A-140. 1 Publication
    Mutagenesisi140 – 1401S → A: Reduces phosphorylation. Inhibits strongly phosphorylation by CK2; when associated with S-109. Does not inhibits interaction with EIF2; when associated with S-109. Does not inhibit association with ribosomes; when associated with S-109. Reduces EIF2 interaction with ribosomes; when associated with S-109. Does not inhibit protein synthesis; when associated with A-109. 1 Publication
    Mutagenesisi342 – 3421K → M: Does not inhibit ribosome binding. Reduces ATP-binding. Inhibits ATP-binding and reduces protein synthesis; when associated with M-664. Shows an enhanced association with polyribosomes; when associated with M-664. Does not inhibit IRES-mediated protein synthesis; when associated with M-664. 1 Publication
    Mutagenesisi367 – 3671Q → E: Does not inhibit ribosome binding. 1 Publication
    Mutagenesisi454 – 4541G → D: Does not inhibit ribosome binding. 1 Publication
    Mutagenesisi477 – 4771E → Q: Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-768. 1 Publication
    Mutagenesisi506 – 5061H → L: Does not inhibit ribosome binding. 1 Publication
    Mutagenesisi664 – 6641K → M: Does not inhibit ribosome binding. Reduces ATP-binding. Inhibits ATP-binding and reduces protein synthesis; when associated with M-342. Shows a reduced association with polyribosomes; when associated with M-664. Does not inhibit IRES-mediated protein synthesis; when associated with M-664. 1 Publication
    Mutagenesisi695 – 6951Q → E: Does not inhibit ribosome binding. 1 Publication
    Mutagenesisi745 – 7451G → D: Does not inhibit ribosome binding. 1 Publication
    Mutagenesisi768 – 7681E → Q: Does not inhibit ribosome binding. Reduces protein synthesis; when associated with Q-477. 1 Publication
    Mutagenesisi797 – 7971H → L: Does not inhibit ribosome binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA24405.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 845845ATP-binding cassette sub-family F member 1PRO_0000093318Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei22 – 221Phosphoserine1 Publication
    Modified residuei24 – 241Phosphoserine1 Publication
    Modified residuei105 – 1051Phosphoserine2 Publications
    Modified residuei108 – 1081Phosphothreonine4 Publications
    Modified residuei109 – 1091Phosphoserine; by CK25 Publications
    Modified residuei140 – 1401Phosphoserine; by CK25 Publications
    Modified residuei166 – 1661Phosphoserine1 Publication
    Modified residuei228 – 2281Phosphoserine7 Publications
    Cross-linki573 – 573Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki582 – 582Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei595 – 5951Phosphoserine1 Publication

    Post-translational modificationi

    Isoform 2 is phosphorylated at phosphoserine and phosphothreonine. Isoform 2 phosphorylation on Ser-109 and Ser-140 by CK2; inhibits association of EIF2 with ribosomes.9 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8NE71.
    PaxDbiQ8NE71.
    PRIDEiQ8NE71.

    PTM databases

    PhosphoSiteiQ8NE71.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Inductioni

    By TNF in cultured synoviocytes.

    Gene expression databases

    ArrayExpressiQ8NE71.
    BgeeiQ8NE71.
    CleanExiHS_ABCF1.
    GenevestigatoriQ8NE71.

    Organism-specific databases

    HPAiHPA017578.

    Interactioni

    Subunit structurei

    Isoform 2 interacts (via N-terminus) with EIF2S1; the interaction is independent of its phosphorylated status. Isoform 2 associates (via both ABC transporter domains) with the ribosomes.1 Publication

    Protein-protein interaction databases

    BioGridi106541. 47 interactions.
    IntActiQ8NE71. 6 interactions.
    MINTiMINT-1392646.
    STRINGi9606.ENSP00000412553.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NE71.
    SMRiQ8NE71. Positions 301-834.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini304 – 548245ABC transporter 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini625 – 840216ABC transporter 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi141 – 243103Glu-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 ABC transporter domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0488.
    HOGENOMiHOG000271637.
    HOVERGENiHBG050440.
    InParanoidiQ8NE71.
    KOiK06184.
    OMAiFNELVIP.
    PhylomeDBiQ8NE71.
    TreeFamiTF105207.

    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. 3 hits.
    PROSITEiPS00211. ABC_TRANSPORTER_1. 2 hits.
    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: Q8NE71-1) [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

    MPKAPKQQPP EPEWIGDGES TSPSDKVVKK GKKDKKIKKT FFEELAVEDK    50
    QAGEEEKVLK EKEQQQQQQQ QQQKKKRDTR KGRRKKDVDD DGEEKELMER 100
    LKKLSVPTSD EEDEVPAPKP RGGKKTKGGN VFAALIQDQS EEEEEEEKHP 150
    PKPAKPEKNR INKAVSEEQQ PALKGKKGKE EKSKGKAKPQ NKFAALDNEE 200
    EDKEEEIIKE KEPPKQGKEK AKKAEQGSEE EGEGEEEEEE GGESKADDPY 250
    AHLSKKEKKK LKKQMEYERQ VASLKAANAA ENDFSVSQAE MSSRQAMLEN 300
    ASDIKLEKFS ISAHGKELFV NADLYIVAGR RYGLVGPNGK GKTTLLKHIA 350
    NRALSIPPNI DVLLCEQEVV ADETPAVQAV LRADTKRLKL LEEERRLQGQ 400
    LEQGDDTAAE RLEKVYEELR ATGAAAAEAK ARRILAGLGF DPEMQNRPTQ 450
    KFSGGWRMRV SLARALFMEP TLLMLDEPTN HLDLNAVIWL NNYLQGWRKT 500
    LLIVSHDQGF LDDVCTDIIH LDAQRLHYYR GNYMTFKKMY QQKQKELLKQ 550
    YEKQEKKLKE LKAGGKSTKQ AEKQTKEALT RKQQKCRRKN QDEESQEAPE 600
    LLKRPKEYTV RFTFPDPPPL SPPVLGLHGV TFGYQGQKPL FKNLDFGIDM 650
    DSRICIVGPN GVGKSTLLLL LTGKLTPTHG EMRKNHRLKI GFFNQQYAEQ 700
    LRMEETPTEY LQRGFNLPYQ DARKCLGRFG LESHAHTIQI CKLSGGQKAR 750
    VVFAELACRE PDVLILDEPT NNLDIESIDA LGEAINEYKG AVIVVSHDAR 800
    LITETNCQLW VVEEQSVSQI DGDFEDYKRE VLEALGEVMV SRPRE 845
    Length:845
    Mass (Da):95,926
    Last modified:December 7, 2004 - v2
    Checksum:i5C5AA662DF4C99E4
    GO
    Isoform 2 (identifier: Q8NE71-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         226-263: Missing.

    Show »
    Length:807
    Mass (Da):91,680
    Checksum:i1B6547EABEE7FC75
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti166 – 1661S → P in AAH34488. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti198 – 1981N → D.
    Corresponds to variant rs6902544 [ dbSNP | Ensembl ].
    VAR_048136

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei226 – 26338Missing in isoform 2. 1 PublicationVSP_012078Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027302 mRNA. Translation: AAC70891.1.
    BA000025 Genomic DNA. Translation: BAB63325.1.
    AB088096 Genomic DNA. Translation: BAC54928.1.
    AL662800 Genomic DNA. Translation: CAI18158.1.
    AL662800 Genomic DNA. Translation: CAI18159.1.
    AL662825 Genomic DNA. Translation: CAI17836.1.
    AL662825 Genomic DNA. Translation: CAI17837.1.
    BX000357 Genomic DNA. Translation: CAI18562.1.
    BX000357 Genomic DNA. Translation: CAI18563.1.
    BX119957, BX248518 Genomic DNA. Translation: CAM25907.1.
    BX248518, BX119957 Genomic DNA. Translation: CAM26017.1.
    CR753328, CR388372 Genomic DNA. Translation: CAQ07804.1.
    CR388372, CR753328 Genomic DNA. Translation: CAQ07873.1.
    BX927220 Genomic DNA. Translation: CAQ09058.1.
    CR759778, CR847863 Genomic DNA. Translation: CAQ09401.1.
    CR847863, CR759778 Genomic DNA. Translation: CAQ10059.1.
    BC034488 mRNA. Translation: AAH34488.1.
    BC112923 mRNA. Translation: AAI12924.1.
    AL832430 mRNA. Translation: CAH10648.1.
    CCDSiCCDS34380.1. [Q8NE71-1]
    CCDS34381.1. [Q8NE71-2]
    RefSeqiNP_001020262.1. NM_001025091.1. [Q8NE71-1]
    NP_001081.1. NM_001090.2. [Q8NE71-2]
    UniGeneiHs.655285.

    Genome annotation databases

    EnsembliENST00000326195; ENSP00000313603; ENSG00000204574. [Q8NE71-1]
    ENST00000376545; ENSP00000365728; ENSG00000204574. [Q8NE71-2]
    ENST00000383587; ENSP00000373081; ENSG00000206490. [Q8NE71-2]
    ENST00000383588; ENSP00000373082; ENSG00000206490. [Q8NE71-1]
    ENST00000412443; ENSP00000404726; ENSG00000236342. [Q8NE71-2]
    ENST00000419893; ENSP00000389065; ENSG00000232169. [Q8NE71-1]
    ENST00000420257; ENSP00000391102; ENSG00000225989. [Q8NE71-2]
    ENST00000421042; ENSP00000393143; ENSG00000231129. [Q8NE71-2]
    ENST00000423247; ENSP00000411327; ENSG00000225989. [Q8NE71-1]
    ENST00000426219; ENSP00000414373; ENSG00000231129. [Q8NE71-1]
    ENST00000448939; ENSP00000403526; ENSG00000232169. [Q8NE71-2]
    ENST00000452530; ENSP00000389472; ENSG00000236149. [Q8NE71-2]
    ENST00000457078; ENSP00000412553; ENSG00000236342. [Q8NE71-1]
    ENST00000457111; ENSP00000413319; ENSG00000236149. [Q8NE71-1]
    GeneIDi23.
    KEGGihsa:23.
    UCSCiuc003nqk.2. human. [Q8NE71-1]

    Polymorphism databases

    DMDMi56417894.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    ABCMdb

    Database for mutations in ABC proteins

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027302 mRNA. Translation: AAC70891.1 .
    BA000025 Genomic DNA. Translation: BAB63325.1 .
    AB088096 Genomic DNA. Translation: BAC54928.1 .
    AL662800 Genomic DNA. Translation: CAI18158.1 .
    AL662800 Genomic DNA. Translation: CAI18159.1 .
    AL662825 Genomic DNA. Translation: CAI17836.1 .
    AL662825 Genomic DNA. Translation: CAI17837.1 .
    BX000357 Genomic DNA. Translation: CAI18562.1 .
    BX000357 Genomic DNA. Translation: CAI18563.1 .
    BX119957 , BX248518 Genomic DNA. Translation: CAM25907.1 .
    BX248518 , BX119957 Genomic DNA. Translation: CAM26017.1 .
    CR753328 , CR388372 Genomic DNA. Translation: CAQ07804.1 .
    CR388372 , CR753328 Genomic DNA. Translation: CAQ07873.1 .
    BX927220 Genomic DNA. Translation: CAQ09058.1 .
    CR759778 , CR847863 Genomic DNA. Translation: CAQ09401.1 .
    CR847863 , CR759778 Genomic DNA. Translation: CAQ10059.1 .
    BC034488 mRNA. Translation: AAH34488.1 .
    BC112923 mRNA. Translation: AAI12924.1 .
    AL832430 mRNA. Translation: CAH10648.1 .
    CCDSi CCDS34380.1. [Q8NE71-1 ]
    CCDS34381.1. [Q8NE71-2 ]
    RefSeqi NP_001020262.1. NM_001025091.1. [Q8NE71-1 ]
    NP_001081.1. NM_001090.2. [Q8NE71-2 ]
    UniGenei Hs.655285.

    3D structure databases

    ProteinModelPortali Q8NE71.
    SMRi Q8NE71. Positions 301-834.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106541. 47 interactions.
    IntActi Q8NE71. 6 interactions.
    MINTi MINT-1392646.
    STRINGi 9606.ENSP00000412553.

    PTM databases

    PhosphoSitei Q8NE71.

    Polymorphism databases

    DMDMi 56417894.

    Proteomic databases

    MaxQBi Q8NE71.
    PaxDbi Q8NE71.
    PRIDEi Q8NE71.

    Protocols and materials databases

    DNASUi 23.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326195 ; ENSP00000313603 ; ENSG00000204574 . [Q8NE71-1 ]
    ENST00000376545 ; ENSP00000365728 ; ENSG00000204574 . [Q8NE71-2 ]
    ENST00000383587 ; ENSP00000373081 ; ENSG00000206490 . [Q8NE71-2 ]
    ENST00000383588 ; ENSP00000373082 ; ENSG00000206490 . [Q8NE71-1 ]
    ENST00000412443 ; ENSP00000404726 ; ENSG00000236342 . [Q8NE71-2 ]
    ENST00000419893 ; ENSP00000389065 ; ENSG00000232169 . [Q8NE71-1 ]
    ENST00000420257 ; ENSP00000391102 ; ENSG00000225989 . [Q8NE71-2 ]
    ENST00000421042 ; ENSP00000393143 ; ENSG00000231129 . [Q8NE71-2 ]
    ENST00000423247 ; ENSP00000411327 ; ENSG00000225989 . [Q8NE71-1 ]
    ENST00000426219 ; ENSP00000414373 ; ENSG00000231129 . [Q8NE71-1 ]
    ENST00000448939 ; ENSP00000403526 ; ENSG00000232169 . [Q8NE71-2 ]
    ENST00000452530 ; ENSP00000389472 ; ENSG00000236149 . [Q8NE71-2 ]
    ENST00000457078 ; ENSP00000412553 ; ENSG00000236342 . [Q8NE71-1 ]
    ENST00000457111 ; ENSP00000413319 ; ENSG00000236149 . [Q8NE71-1 ]
    GeneIDi 23.
    KEGGi hsa:23.
    UCSCi uc003nqk.2. human. [Q8NE71-1 ]

    Organism-specific databases

    CTDi 23.
    GeneCardsi GC06P030539.
    GC06Pj30529.
    GC06Pk30529.
    GC06Pl30583.
    GC06Pm30617.
    GC06Pn30528.
    GC06Po30530.
    HGNCi HGNC:70. ABCF1.
    HPAi HPA017578.
    MIMi 603429. gene.
    neXtProti NX_Q8NE71.
    PharmGKBi PA24405.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0488.
    HOGENOMi HOG000271637.
    HOVERGENi HBG050440.
    InParanoidi Q8NE71.
    KOi K06184.
    OMAi FNELVIP.
    PhylomeDBi Q8NE71.
    TreeFami TF105207.

    Miscellaneous databases

    ChiTaRSi ABCF1. human.
    GeneWikii ABCF1.
    GenomeRNAii 23.
    NextBioi 69.
    PROi Q8NE71.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8NE71.
    Bgeei Q8NE71.
    CleanExi HS_ABCF1.
    Genevestigatori Q8NE71.

    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. 3 hits.
    PROSITEi PS00211. ABC_TRANSPORTER_1. 2 hits.
    PS50893. ABC_TRANSPORTER_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ABC50, a novel human ATP-binding cassette protein found in tumor necrosis factor-alpha-stimulated synoviocytes."
      Richard M., Drouin R., Beaulieu A.D.
      Genomics 53:137-145(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    2. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
      Shiina S., Tamiya G., Oka A., Inoko H.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Genome diversity in HLA: a new strategy for detection of genetic polymorphisms in expressed genes within the HLA class III and class I regions."
      Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Embryonic stem cell and Testis.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-845 (ISOFORM 1).
      Tissue: Melanoma.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-108; SER-109; SER-140 AND SER-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573 AND LYS-582.
      Tissue: Mammary cancer.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "The N-terminal region of ABC50 interacts with eukaryotic initiation factor eIF2 and is a target for regulatory phosphorylation by CK2."
      Paytubi S., Morrice N.A., Boudeau J., Proud C.G.
      Biochem. J. 409:223-231(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF2S1, ASSOCIATION WITH RIBOSOMES, PHOSPHORYLATION AT SER-109 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-109 AND SER-140.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: FUNCTION, ATP-BINDING, ASSOCIATION WITH RIBOSOMES, MUTAGENESIS OF LYS-342; GLN-367; GLY-454; GLU-477; HIS-506; LYS-664; GLN-695; GLY-745; GLU-768 AND HIS-797, 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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140 AND SER-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-105; THR-108; SER-109; SER-140 AND SER-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140; SER-166 AND SER-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiABCF1_HUMAN
    AccessioniPrimary (citable) accession number: Q8NE71
    Secondary accession number(s): A2BF75, O14897, Q69YP6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 121 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

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