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Protein

FK506-binding protein 15

Gene

FKBP15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in the cytoskeletal organization of neuronal growth cones. Seems to be inactive as a PPIase (By similarity). Involved in the transport of early endosomes at the level of transition between microfilament-based and microtubule-based movement.By similarity1 Publication

GO - Biological processi

  • endocytosis Source: UniProtKB-KW
  • negative regulation of phosphatase activity Source: UniProtKB
  • protein folding Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Transport

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
FK506-binding protein 15
Short name:
FKBP-15
Alternative name(s):
133 kDa FK506-binding protein
Short name:
133 kDa FKBP
Short name:
FKBP-133
WASP and FKBP-like
Short name:
WAFL
Gene namesi
Name:FKBP15
Synonyms:KIAA0674
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:23397. FKBP15.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: Ensembl
  • axon Source: UniProtKB-SubCell
  • early endosome Source: UniProtKB-SubCell
  • growth cone Source: Ensembl
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Endosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162388608.

Polymorphism and mutation databases

BioMutaiFKBP15.
DMDMi158563913.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12191219FK506-binding protein 15PRO_0000299556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei23 – 231PhosphoserineCombined sources
Modified residuei92 – 921N6-acetyllysineCombined sources
Modified residuei307 – 3071PhosphoserineBy similarity
Modified residuei311 – 3111PhosphoserineBy similarity
Modified residuei326 – 3261PhosphoserineCombined sources
Modified residuei346 – 3461PhosphoserineCombined sources
Modified residuei356 – 3561PhosphoserineCombined sources
Modified residuei619 – 6191PhosphoserineBy similarity
Modified residuei939 – 9391PhosphoserineCombined sources
Modified residuei940 – 9401PhosphoserineCombined sources
Modified residuei941 – 9411PhosphoserineCombined sources
Modified residuei956 – 9561PhosphoserineCombined sources
Modified residuei979 – 9791PhosphoserineCombined sources
Modified residuei1024 – 10241PhosphoserineCombined sources
Modified residuei1056 – 10561PhosphoserineBy similarity
Modified residuei1061 – 10611PhosphoserineCombined sources
Modified residuei1065 – 10651PhosphoserineCombined sources
Modified residuei1097 – 10971PhosphoserineCombined sources
Modified residuei1099 – 10991PhosphothreonineCombined sources
Modified residuei1114 – 11141PhosphoserineCombined sources
Modified residuei1158 – 11581PhosphoserineCombined sources
Modified residuei1161 – 11611PhosphoserineCombined sources
Modified residuei1162 – 11621PhosphoserineCombined sources
Modified residuei1164 – 11641PhosphoserineCombined sources
Modified residuei1195 – 11951PhosphoserineCombined sources
Modified residuei1203 – 12031PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ5T1M5.
MaxQBiQ5T1M5.
PaxDbiQ5T1M5.
PRIDEiQ5T1M5.

PTM databases

iPTMnetiQ5T1M5.
PhosphoSiteiQ5T1M5.

Expressioni

Gene expression databases

BgeeiQ5T1M5.
CleanExiHS_FKBP15.
ExpressionAtlasiQ5T1M5. baseline and differential.
GenevisibleiQ5T1M5. HS.

Organism-specific databases

HPAiHPA007979.

Interactioni

Subunit structurei

Interacts with WIP and actin.1 Publication

Protein-protein interaction databases

BioGridi116899. 28 interactions.
IntActiQ5T1M5. 9 interactions.
STRINGi9606.ENSP00000238256.

Structurei

3D structure databases

ProteinModelPortaliQ5T1M5.
SMRiQ5T1M5. Positions 184-286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini197 – 29094PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 16998Important for function in growth cone organizationBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili522 – 789268Sequence analysisAdd
BLAST
Coiled coili818 – 87861Sequence analysisAdd
BLAST
Coiled coili925 – 95127Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1208 – 12169Poly-Asp

Domaini

The PPIase FKBP-type domain seems to be inactive both for FK506-binding and enzymatic activity.By similarity
The central coiled-coil region is responsible for association with early endosomes.

Sequence similaritiesi

Belongs to the FKBP-type PPIase family.Curated
Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410INYI. Eukaryota.
ENOG4112APP. LUCA.
GeneTreeiENSGT00530000064286.
HOGENOMiHOG000112601.
HOVERGENiHBG067251.
InParanoidiQ5T1M5.
KOiK17478.
OrthoDBiEOG75XGKG.
PhylomeDBiQ5T1M5.
TreeFamiTF328592.

Family and domain databases

InterProiIPR001179. PPIase_FKBP_dom.
[Graphical view]
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5T1M5-1) [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
MFGAGDEDDT DFLSPSGGAR LASLFGLDQA AAGHGNEFFQ YTAPKQPKKG
60 70 80 90 100
QGTAATGNQA TPKTAPATMS TPTILVATAV HAYRYTNGQY VKQGKFGAAV
110 120 130 140 150
LGNHTAREYR ILLYISQQQP VTVARIHVNF ELMVRPNNYS TFYDDQRQNW
160 170 180 190 200
SIMFESEKAA VEFNKQVCIA KCNSTSSLDA VLSQDLIVAD GPAVEVGDSL
210 220 230 240 250
EVAYTGWLFQ NHVLGQVFDS TANKDKLLRL KLGSGKVIKG WEDGMLGMKK
260 270 280 290 300
GGKRLLIVPP ACAVGSEGVI GWTQATDSIL VFEVEVRRVK FARDSGSDGH
310 320 330 340 350
SVSSRDSAAP SPIPGADNLS ADPVVSPPTS IPFKSGEPAL RTKSNSLSEQ
360 370 380 390 400
LAINTSPDAV KAKLISRMAK MGQPMLPILP PQLDSNDSEI EDVNTLQGGG
410 420 430 440 450
QPVVTPSVQP SLHPAHPALP QMTSQAPQPS VTGLQAPSAA LMQVSSLDSH
460 470 480 490 500
SAVSGNAQSF QPYAGMQAYA YPQASAVTSQ LQPVRPLYPA PLSQPPHFQG
510 520 530 540 550
SGDMASFLMT EARQHNTEIR MAVSKVADKM DHLMTKVEEL QKHSAGNSML
560 570 580 590 600
IPSMSVTMET SMIMSNIQRI IQENERLKQE ILEKSNRIEE QNDKISELIE
610 620 630 640 650
RNQRYVEQSN LMMEKRNNSL QTATENTQAR VLHAEQEKAK VTEELAAATA
660 670 680 690 700
QVSHLQLKMT AHQKKETELQ MQLTESLKET DLLRGQLTKV QAKLSELQET
710 720 730 740 750
SEQAQSKFKS EKQNRKQLEL KVTSLEEELT DLRVEKESLE KNLSERKKKS
760 770 780 790 800
AQERSQAEEE IDEIRKSYQE ELDKLRQLLK KTRVSTDQAA AEQLSLVQAE
810 820 830 840 850
LQTQWEAKCE HLLASAKDEH LQQYQEVCAQ RDAYQQKLVQ LQEKCLALQA
860 870 880 890 900
QITALTKQNE QHIKELEKNK SQMSGVEAAA SDPSEKVKKI MNQVFQSLRR
910 920 930 940 950
EFELEESYNG RTILGTIMNT IKMVTLQLLN QQEQEKEESS SEEEEEKAEE
960 970 980 990 1000
RPRRPSQEQS ASASSGQPQA PLNRERPESP MVPSEQVVEE AVPLPPQALT
1010 1020 1030 1040 1050
TSQDGHRRKG DSEAEALSEI KDGSLPPELS CIPSHRVLGP PTSIPPEPLG
1060 1070 1080 1090 1100
PVSMDSECEE SLAASPMAAK PDNPSGKVCV REVAPDGPLQ ESSTRLSLTS
1110 1120 1130 1140 1150
DPEEGDPLAL GPESPGEPQP PQLKKDDVTS STGPHKELSS TEAGSTVAGA
1160 1170 1180 1190 1200
ALRPSHHSQR SSLSGDEEDE LFKGATLKAL RPKAQPEEED EDEVSMKGRP
1210
PPTPLFGDDD DDDDIDWLG
Length:1,219
Mass (Da):133,630
Last modified:September 11, 2007 - v2
Checksum:i86563D82B540B51D
GO
Isoform 2 (identifier: Q5T1M5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     629-638: Missing.

Note: No experimental confirmation available.
Show »
Length:1,209
Mass (Da):132,467
Checksum:iAD3F9C4AA1FD65A6
GO
Isoform 3 (identifier: Q5T1M5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     462-472: PYAGMQAYAYP → VTFYNRINYIL
     473-1219: Missing.

Show »
Length:472
Mass (Da):50,330
Checksum:i2112364B487D6E69
GO

Sequence cautioni

The sequence AAH09609.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA31649.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI10963.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI10964.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti106 – 1061A → T.
Corresponds to variant rs1133618 [ dbSNP | Ensembl ].
VAR_034851
Natural varianti413 – 4131H → Q.2 Publications
Corresponds to variant rs10435864 [ dbSNP | Ensembl ].
VAR_034852
Natural varianti434 – 4341L → F.
Corresponds to variant rs10465129 [ dbSNP | Ensembl ].
VAR_034853
Natural varianti847 – 8471A → S.
Corresponds to variant rs1128116 [ dbSNP | Ensembl ].
VAR_061543
Natural varianti993 – 9931P → T.
Corresponds to variant rs57348436 [ dbSNP | Ensembl ].
VAR_061544

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei462 – 47211PYAGMQAYAYP → VTFYNRINYIL in isoform 3. 1 PublicationVSP_027756Add
BLAST
Alternative sequencei473 – 1219747Missing in isoform 3. 1 PublicationVSP_027757Add
BLAST
Alternative sequencei629 – 63810Missing in isoform 2. 1 PublicationVSP_027758

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014574 mRNA. Translation: BAA31649.1. Different initiation.
AL449305 Genomic DNA. Translation: CAI10963.1. Different initiation.
AL449305, AL449105 Genomic DNA. Translation: CAI10964.1. Different initiation.
AL449105, AL449305 Genomic DNA. Translation: CAI95402.1.
BC009609 mRNA. Translation: AAH09609.1. Different initiation.
BC077732 mRNA. Translation: AAH77732.1.
CCDSiCCDS48007.1. [Q5T1M5-1]
PIRiT00363.
RefSeqiNP_056073.1. NM_015258.1. [Q5T1M5-1]
XP_006717081.1. XM_006717018.1. [Q5T1M5-2]
UniGeneiHs.522351.

Genome annotation databases

EnsembliENST00000238256; ENSP00000238256; ENSG00000119321. [Q5T1M5-1]
GeneIDi23307.
KEGGihsa:23307.
UCSCiuc004bgs.3. human. [Q5T1M5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014574 mRNA. Translation: BAA31649.1. Different initiation.
AL449305 Genomic DNA. Translation: CAI10963.1. Different initiation.
AL449305, AL449105 Genomic DNA. Translation: CAI10964.1. Different initiation.
AL449105, AL449305 Genomic DNA. Translation: CAI95402.1.
BC009609 mRNA. Translation: AAH09609.1. Different initiation.
BC077732 mRNA. Translation: AAH77732.1.
CCDSiCCDS48007.1. [Q5T1M5-1]
PIRiT00363.
RefSeqiNP_056073.1. NM_015258.1. [Q5T1M5-1]
XP_006717081.1. XM_006717018.1. [Q5T1M5-2]
UniGeneiHs.522351.

3D structure databases

ProteinModelPortaliQ5T1M5.
SMRiQ5T1M5. Positions 184-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116899. 28 interactions.
IntActiQ5T1M5. 9 interactions.
STRINGi9606.ENSP00000238256.

PTM databases

iPTMnetiQ5T1M5.
PhosphoSiteiQ5T1M5.

Polymorphism and mutation databases

BioMutaiFKBP15.
DMDMi158563913.

Proteomic databases

EPDiQ5T1M5.
MaxQBiQ5T1M5.
PaxDbiQ5T1M5.
PRIDEiQ5T1M5.

Protocols and materials databases

DNASUi23307.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000238256; ENSP00000238256; ENSG00000119321. [Q5T1M5-1]
GeneIDi23307.
KEGGihsa:23307.
UCSCiuc004bgs.3. human. [Q5T1M5-1]

Organism-specific databases

CTDi23307.
GeneCardsiFKBP15.
H-InvDBHIX0008300.
HIX0153287.
HGNCiHGNC:23397. FKBP15.
HPAiHPA007979.
neXtProtiNX_Q5T1M5.
PharmGKBiPA162388608.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INYI. Eukaryota.
ENOG4112APP. LUCA.
GeneTreeiENSGT00530000064286.
HOGENOMiHOG000112601.
HOVERGENiHBG067251.
InParanoidiQ5T1M5.
KOiK17478.
OrthoDBiEOG75XGKG.
PhylomeDBiQ5T1M5.
TreeFamiTF328592.

Miscellaneous databases

ChiTaRSiFKBP15. human.
GenomeRNAii23307.
NextBioi45162.
PROiQ5T1M5.

Gene expression databases

BgeeiQ5T1M5.
CleanExiHS_FKBP15.
ExpressionAtlasiQ5T1M5. baseline and differential.
GenevisibleiQ5T1M5. HS.

Family and domain databases

InterProiIPR001179. PPIase_FKBP_dom.
[Graphical view]
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-413.
    Tissue: Brain.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 548-1219 (ISOFORM 2), VARIANT GLN-413.
    Tissue: Eye and Prostate.
  4. "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-956, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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-1161 AND SER-1162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; SER-356; SER-939; SER-940; SER-941; SER-956; SER-979; SER-1114 AND SER-1164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "WAFL, a new protein involved in regulation of early endocytic transport at the intersection of actin and microtubule dynamics."
    Viklund I.-M., Aspenstroem P., Meas-Yedid V., Zhang B., Kopec J., Agren D., Schneider G., D'Amato M., Olivo-Marin J.-C., Sansonetti P., Van Nhieu G.T., Pettersson S.
    Exp. Cell Res. 315:1040-1052(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ACTIN AND WIP.
  10. "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 SER-326; SER-356; SER-1114; SER-1164; SER-1195 AND THR-1203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-956; SER-1114 AND SER-1164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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 SER-1164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-956; SER-979; SER-1024; SER-1061; SER-1065; SER-1097; THR-1099; SER-1114 AND SER-1158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFKB15_HUMAN
AccessioniPrimary (citable) accession number: Q5T1M5
Secondary accession number(s): Q05DK8
, Q5T1M2, Q6DD85, Q9Y4D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: May 11, 2016
This is version 107 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 9
    Human chromosome 9: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.