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Q6UN15

- FIP1_HUMAN

UniProt

Q6UN15 - FIP1_HUMAN

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Protein

Pre-mRNA 3'-end-processing factor FIP1

Gene

FIP1L1

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

Functioni

Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei339 – 3402Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA 3'-end-processing factor FIP1
Short name:
hFip1
Alternative name(s):
FIP1-like 1 protein
Factor interacting with PAP
Rearranged in hypereosinophilia
Gene namesi
Name:FIP1L1
Synonyms:FIP1, RHE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:19124. FIP1L1.

Subcellular locationi

GO - Cellular componenti

  1. mRNA cleavage and polyadenylation specificity factor complex Source: Ensembl
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving FIP1L1 is found in some cases of hypereosinophilic syndrome. Interstitial chromosomal deletion del4(q12q12) causes the fusion of FIP1L1 and PDGFRA (FIP1L1-PDGFRA).2 Publications

Organism-specific databases

MIMi607685. phenotype.
Orphaneti520. Acute promyelocytic leukemia.
3260. Idiopathic hypereosinophilic syndrome.
PharmGKBiPA134875694.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 594594Pre-mRNA 3'-end-processing factor FIP1PRO_0000215037Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei85 – 851Phosphoserine3 Publications
Modified residuei87 – 871Phosphoserine3 Publications
Modified residuei89 – 891Phosphoserine2 Publications
Modified residuei259 – 2591Phosphoserine3 Publications
Modified residuei294 – 2941N6-acetyllysine1 Publication
Modified residuei304 – 3041Phosphoserine2 Publications
Modified residuei426 – 4261Phosphotyrosine1 Publication
Modified residuei492 – 4921Phosphoserine4 Publications
Modified residuei494 – 4941Phosphothreonine1 Publication
Modified residuei496 – 4961Phosphoserine3 Publications
Modified residuei500 – 5001Phosphoserine3 Publications
Modified residuei554 – 5541Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ6UN15.
PaxDbiQ6UN15.
PeptideAtlasiQ6UN15.
PRIDEiQ6UN15.

PTM databases

PhosphoSiteiQ6UN15.

Miscellaneous databases

PMAP-CutDBQ6UN15.

Expressioni

Gene expression databases

BgeeiQ6UN15.
CleanExiHS_FIP1L1.
ExpressionAtlasiQ6UN15. baseline and differential.
GenevestigatoriQ6UN15.

Organism-specific databases

HPAiHPA037475.

Interactioni

Subunit structurei

Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with CPSF1, CPSF4, CSTF2, CSTF3 and PAPOLA.1 Publication

Protein-protein interaction databases

BioGridi123545. 25 interactions.
DIPiDIP-42503N.
IntActiQ6UN15. 14 interactions.
MINTiMINT-1475441.
STRINGi9606.ENSP00000336752.

Structurei

3D structure databases

ProteinModelPortaliQ6UN15.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 356356Necessary for stimulating PAPOLA activityAdd
BLAST
Regioni1 – 111111Sufficient for interaction with PAPOLAAdd
BLAST
Regioni137 – 243107Sufficient for interaction with CPSF4Add
BLAST
Regioni443 – 594152Sufficient for interaction with CPSF1 and CSTF3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi356 – 40651Pro-richAdd
BLAST
Compositional biasi456 – 562107Arg-richAdd
BLAST
Compositional biasi478 – 594117Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the FIP1 family.Curated

Phylogenomic databases

eggNOGiCOG5213.
GeneTreeiENSGT00730000111028.
HOVERGENiHBG059889.
KOiK14405.
OMAiGNNIQVI.
OrthoDBiEOG7Z3F5S.
PhylomeDBiQ6UN15.
TreeFamiTF318610.

Family and domain databases

InterProiIPR007854. Fip1.
[Graphical view]
PfamiPF05182. Fip1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6UN15-1) [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
MSAGEVERLV SELSGGTGGD EEEEWLYGGP WDVHVHSDLA KDLDENEVER
60 70 80 90 100
PEEENASANP PSGIEDETAE NGVPKPKVTE TEDDSDSDSD DDEDDVHVTI
110 120 130 140 150
GDIKTGAPQY GSYGTAPVNL NIKTGGRVYG TTGTKVKGVD LDAPGSINGV
160 170 180 190 200
PLLEVDLDSF EDKPWRKPGA DLSDYFNYGF NEDTWKAYCE KQKRIRMGLE
210 220 230 240 250
VIPVTSTTNK ITAEDCTMEV TPGAEIQDGR FNLFKVQQGR TGNSEKETAL
260 270 280 290 300
PSTKAEFTSP PSLFKTGLPP SRNSTSSQSQ TSTASRKANS SVGKWQDRYG
310 320 330 340 350
RAESPDLRRL PGAIDVIGQT ITISRVEGRR RANENSNIQV LSERSATEVD
360 370 380 390 400
NNFSKPPPFF PPGAPPTHLP PPPFLPPPPT VSTAPPLIPP PGFPPPPGAP
410 420 430 440 450
PPSLIPTIES GHSSGYDSRS ARAFPYGNVA FPHLPGSAPS WPSLVDTSKQ
460 470 480 490 500
WDYYARREKD RDRERDRDRE RDRDRDRERE RTRERERERD HSPTPSVFNS
510 520 530 540 550
DEERYRYREY AERGYERHRA SREKEERHRE RRHREKEETR HKSSRSNSRR
560 570 580 590
RHESEEGDSH RRHKHKKSKR SKEGKEAGSE PAPEQESTEA TPAE
Length:594
Mass (Da):66,526
Last modified:July 5, 2004 - v1
Checksum:iB391D142419ED061
GO
Isoform 3 (identifier: Q6UN15-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     29-43: Missing.
     213-235: Missing.
     272-307: Missing.

Show »
Length:520
Mass (Da):58,376
Checksum:i55D48285A046A783
GO
Isoform 4 (identifier: Q6UN15-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     29-43: Missing.
     393-393: F → K
     394-594: Missing.

Show »
Length:378
Mass (Da):40,835
Checksum:i1B699B114C9560D4
GO
Isoform 5 (identifier: Q6UN15-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     29-43: Missing.
     389-389: P → PPPGIPITVP

Note: No experimental confirmation available.

Show »
Length:588
Mass (Da):65,728
Checksum:i0E9D598DEAF3C752
GO

Sequence cautioni

The sequence AAH24016.1 differs from that shown. Reason: Intron retention.
The sequence AAH52959.1 differs from that shown. Reason: Intron retention.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181V → I in BAG58575. (PubMed:14702039)Curated
Sequence conflicti312 – 3121G → R in AAH24016. (PubMed:15489334)Curated
Sequence conflicti312 – 3121G → R in AAH52959. (PubMed:15489334)Curated
Sequence conflicti524 – 5241K → R in AAH52959. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei29 – 4315Missing in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_016728Add
BLAST
Alternative sequencei213 – 23523Missing in isoform 3. 1 PublicationVSP_016729Add
BLAST
Alternative sequencei272 – 30736Missing in isoform 3. 1 PublicationVSP_016730Add
BLAST
Alternative sequencei389 – 3891P → PPPGIPITVP in isoform 5. 1 PublicationVSP_046213
Alternative sequencei393 – 3931F → K in isoform 4. 1 PublicationVSP_016731
Alternative sequencei394 – 594201Missing in isoform 4. 1 PublicationVSP_016732Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY366510 mRNA. Translation: AAQ88277.1.
AL136910 mRNA. Translation: CAB66844.1.
AK295737 mRNA. Translation: BAG58575.1.
AC058822 Genomic DNA. No translation available.
AC095040 Genomic DNA. No translation available.
AC098587 Genomic DNA. No translation available.
AC098821 Genomic DNA. No translation available.
AC105384 Genomic DNA. No translation available.
AC110298 Genomic DNA. No translation available.
AC110792 Genomic DNA. No translation available.
AC124017 Genomic DNA. No translation available.
AC138607 Genomic DNA. No translation available.
AC138779 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05448.1.
BC011543 mRNA. Translation: AAH11543.1.
BC017724 mRNA. Translation: AAH17724.1.
BC024016 mRNA. Translation: AAH24016.1. Sequence problems.
BC052959 mRNA. Translation: AAH52959.1. Sequence problems.
BC110383 mRNA. Translation: AAI10384.1.
AY229892 mRNA. Translation: AAP69563.1. Different termination.
CCDSiCCDS3491.1. [Q6UN15-1]
CCDS47055.1. [Q6UN15-5]
CCDS47056.1. [Q6UN15-3]
RefSeqiNP_001128409.1. NM_001134937.1. [Q6UN15-5]
NP_001128410.1. NM_001134938.1. [Q6UN15-3]
NP_112179.2. NM_030917.3. [Q6UN15-1]
UniGeneiHs.624245.

Genome annotation databases

EnsembliENST00000306932; ENSP00000302993; ENSG00000145216. [Q6UN15-3]
ENST00000337488; ENSP00000336752; ENSG00000145216. [Q6UN15-1]
ENST00000358575; ENSP00000351383; ENSG00000145216. [Q6UN15-5]
ENST00000507166; ENSP00000423325; ENSG00000145216.
ENST00000507922; ENSP00000425456; ENSG00000145216. [Q6UN15-4]
GeneIDi81608.
KEGGihsa:81608.
UCSCiuc003gzx.4. human. [Q6UN15-4]
uc003gzy.3. human. [Q6UN15-1]
uc003gzz.3. human. [Q6UN15-3]
uc011bzu.2. human.

Polymorphism databases

DMDMi74749365.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY366510 mRNA. Translation: AAQ88277.1 .
AL136910 mRNA. Translation: CAB66844.1 .
AK295737 mRNA. Translation: BAG58575.1 .
AC058822 Genomic DNA. No translation available.
AC095040 Genomic DNA. No translation available.
AC098587 Genomic DNA. No translation available.
AC098821 Genomic DNA. No translation available.
AC105384 Genomic DNA. No translation available.
AC110298 Genomic DNA. No translation available.
AC110792 Genomic DNA. No translation available.
AC124017 Genomic DNA. No translation available.
AC138607 Genomic DNA. No translation available.
AC138779 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05448.1 .
BC011543 mRNA. Translation: AAH11543.1 .
BC017724 mRNA. Translation: AAH17724.1 .
BC024016 mRNA. Translation: AAH24016.1 . Sequence problems.
BC052959 mRNA. Translation: AAH52959.1 . Sequence problems.
BC110383 mRNA. Translation: AAI10384.1 .
AY229892 mRNA. Translation: AAP69563.1 . Different termination.
CCDSi CCDS3491.1. [Q6UN15-1 ]
CCDS47055.1. [Q6UN15-5 ]
CCDS47056.1. [Q6UN15-3 ]
RefSeqi NP_001128409.1. NM_001134937.1. [Q6UN15-5 ]
NP_001128410.1. NM_001134938.1. [Q6UN15-3 ]
NP_112179.2. NM_030917.3. [Q6UN15-1 ]
UniGenei Hs.624245.

3D structure databases

ProteinModelPortali Q6UN15.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123545. 25 interactions.
DIPi DIP-42503N.
IntActi Q6UN15. 14 interactions.
MINTi MINT-1475441.
STRINGi 9606.ENSP00000336752.

PTM databases

PhosphoSitei Q6UN15.

Polymorphism databases

DMDMi 74749365.

Proteomic databases

MaxQBi Q6UN15.
PaxDbi Q6UN15.
PeptideAtlasi Q6UN15.
PRIDEi Q6UN15.

Protocols and materials databases

DNASUi 81608.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306932 ; ENSP00000302993 ; ENSG00000145216 . [Q6UN15-3 ]
ENST00000337488 ; ENSP00000336752 ; ENSG00000145216 . [Q6UN15-1 ]
ENST00000358575 ; ENSP00000351383 ; ENSG00000145216 . [Q6UN15-5 ]
ENST00000507166 ; ENSP00000423325 ; ENSG00000145216 .
ENST00000507922 ; ENSP00000425456 ; ENSG00000145216 . [Q6UN15-4 ]
GeneIDi 81608.
KEGGi hsa:81608.
UCSCi uc003gzx.4. human. [Q6UN15-4 ]
uc003gzy.3. human. [Q6UN15-1 ]
uc003gzz.3. human. [Q6UN15-3 ]
uc011bzu.2. human.

Organism-specific databases

CTDi 81608.
GeneCardsi GC04P054159.
HGNCi HGNC:19124. FIP1L1.
HPAi HPA037475.
MIMi 607685. phenotype.
607686. gene.
neXtProti NX_Q6UN15.
Orphaneti 520. Acute promyelocytic leukemia.
3260. Idiopathic hypereosinophilic syndrome.
PharmGKBi PA134875694.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5213.
GeneTreei ENSGT00730000111028.
HOVERGENi HBG059889.
KOi K14405.
OMAi GNNIQVI.
OrthoDBi EOG7Z3F5S.
PhylomeDBi Q6UN15.
TreeFami TF318610.

Miscellaneous databases

ChiTaRSi FIP1L1. human.
GeneWikii FIP1L1.
GenomeRNAii 81608.
NextBioi 71928.
PMAP-CutDB Q6UN15.
PROi Q6UN15.
SOURCEi Search...

Gene expression databases

Bgeei Q6UN15.
CleanExi HS_FIP1L1.
ExpressionAtlasi Q6UN15. baseline and differential.
Genevestigatori Q6UN15.

Family and domain databases

InterProi IPR007854. Fip1.
[Graphical view ]
Pfami PF05182. Fip1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase."
    Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.
    EMBO J. 23:616-626(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PRE-MRNA 3'-END PROCESSING, IDENTIFICATION IN THE CPSF COMPLEX, IDENTIFICATION IN A COMPLEX WITH CPSF1 AND PAPOLA, INTERACTION WITH CPSF1; CPSF4; CSTF2; CSTF3 AND PAPOLA, RNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Uterus.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Hippocampus.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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] (ISOFORMS 1 AND 4).
    Tissue: Brain, Eye, Placenta and Testis.
  7. "Discovery of a fusion kinase in EOL-1 cells and idiopathic hypereosinophilic syndrome."
    Griffin J.H., Leung J., Bruner R.J., Caligiuri M.A., Briesewitz R.
    Proc. Natl. Acad. Sci. U.S.A. 100:7830-7835(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-339, DISEASE, IDENTIFICATION BY MASS SPECTROMETRY OF THE FIP1L1-PDGFRA FUSION PROTEIN.
    Tissue: Eosinophil.
  8. "A 57-nucleotide upstream early polyadenylation element in human papillomavirus type 16 interacts with hFip1, CstF-64, hnRNP C1/C2, and polypyrimidine tract binding protein."
    Zhao X., Oeberg D., Rush M., Fay J., Lambkin H., Schwartz S.
    J. Virol. 79:4270-4288(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  9. Cited for: DISEASE.
  10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-87; SER-89; SER-259; SER-492; SER-496 AND SER-500, 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-554, 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. "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-85; SER-87; SER-89; SER-492; THR-494; SER-496 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-294, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-259; SER-304; SER-492 AND SER-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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-85; SER-87; SER-259; SER-304; SER-492 AND SER-496, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFIP1_HUMAN
AccessioniPrimary (citable) accession number: Q6UN15
Secondary accession number(s): B4DIR3
, G3XAD6, Q0VGE0, Q499Y4, Q49AU3, Q7Z608, Q8WVN3, Q96F80, Q9H077
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 103 of the entry and version 1 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 4
    Human chromosome 4: 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