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Q8NE71

- ABCF1_HUMAN

UniProt

Q8NE71 - ABCF1_HUMAN

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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

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. ribosome binding Source: UniProtKB
  5. translation activator activity Source: UniProtKB
  6. 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
Complete GO annotation...

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, UP000005640: Unplaced

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. nucleus Source: UniProtKB-KW
  6. polysomal ribosome Source: UniProtKB
  7. ribosome Source: Ensembl
Complete GO annotation...

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

BgeeiQ8NE71.
CleanExiHS_ABCF1.
ExpressionAtlasiQ8NE71. baseline and differential.
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 281-836.
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.
GeneTreeiENSGT00630000089843.
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

        10         20         30         40         50
MPKAPKQQPP EPEWIGDGES TSPSDKVVKK GKKDKKIKKT FFEELAVEDK
60 70 80 90 100
QAGEEEKVLK EKEQQQQQQQ QQQKKKRDTR KGRRKKDVDD DGEEKELMER
110 120 130 140 150
LKKLSVPTSD EEDEVPAPKP RGGKKTKGGN VFAALIQDQS EEEEEEEKHP
160 170 180 190 200
PKPAKPEKNR INKAVSEEQQ PALKGKKGKE EKSKGKAKPQ NKFAALDNEE
210 220 230 240 250
EDKEEEIIKE KEPPKQGKEK AKKAEQGSEE EGEGEEEEEE GGESKADDPY
260 270 280 290 300
AHLSKKEKKK LKKQMEYERQ VASLKAANAA ENDFSVSQAE MSSRQAMLEN
310 320 330 340 350
ASDIKLEKFS ISAHGKELFV NADLYIVAGR RYGLVGPNGK GKTTLLKHIA
360 370 380 390 400
NRALSIPPNI DVLLCEQEVV ADETPAVQAV LRADTKRLKL LEEERRLQGQ
410 420 430 440 450
LEQGDDTAAE RLEKVYEELR ATGAAAAEAK ARRILAGLGF DPEMQNRPTQ
460 470 480 490 500
KFSGGWRMRV SLARALFMEP TLLMLDEPTN HLDLNAVIWL NNYLQGWRKT
510 520 530 540 550
LLIVSHDQGF LDDVCTDIIH LDAQRLHYYR GNYMTFKKMY QQKQKELLKQ
560 570 580 590 600
YEKQEKKLKE LKAGGKSTKQ AEKQTKEALT RKQQKCRRKN QDEESQEAPE
610 620 630 640 650
LLKRPKEYTV RFTFPDPPPL SPPVLGLHGV TFGYQGQKPL FKNLDFGIDM
660 670 680 690 700
DSRICIVGPN GVGKSTLLLL LTGKLTPTHG EMRKNHRLKI GFFNQQYAEQ
710 720 730 740 750
LRMEETPTEY LQRGFNLPYQ DARKCLGRFG LESHAHTIQI CKLSGGQKAR
760 770 780 790 800
VVFAELACRE PDVLILDEPT NNLDIESIDA LGEAINEYKG AVIVVSHDAR
810 820 830 840
LITETNCQLW VVEEQSVSQI DGDFEDYKRE VLEALGEVMV SRPRE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 281-836.
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.
GeneTreei ENSGT00630000089843.
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

Bgeei Q8NE71.
CleanExi HS_ABCF1.
ExpressionAtlasi Q8NE71. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 122 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

Dasty 3