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Q6UN15 (FIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:FIP1L1
Synonyms:FIP1, RHE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

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. Ref.1

Subcellular location

Nucleus.

Involvement in disease

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). Ref.7 Ref.9

Sequence similarities

Belongs to the FIP1 family.

Sequence caution

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

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

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmRNA cleavage and polyadenylation specificity factor complex

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6UN15-1)

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.
Isoform 3 (identifier: Q6UN15-3)

The sequence of this isoform differs from the canonical sequence as follows:
     29-43: Missing.
     213-235: Missing.
     272-307: Missing.
Isoform 4 (identifier: Q6UN15-4)

The sequence of this isoform differs from the canonical sequence as follows:
     29-43: Missing.
     393-393: F → K
     394-594: Missing.
Isoform 5 (identifier: Q6UN15-5)

The sequence of this isoform differs from the canonical sequence as follows:
     29-43: Missing.
     389-389: P → PPPGIPITVP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 594594Pre-mRNA 3'-end-processing factor FIP1
PRO_0000215037

Regions

Region1 – 356356Necessary for stimulating PAPOLA activity
Region1 – 111111Sufficient for interaction with PAPOLA
Region137 – 243107Sufficient for interaction with CPSF4
Region443 – 594152Sufficient for interaction with CPSF1 and CSTF3
Compositional bias356 – 40651Pro-rich
Compositional bias456 – 562107Arg-rich
Compositional bias478 – 594117Glu-rich

Sites

Site339 – 3402Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein

Amino acid modifications

Modified residue851Phosphoserine Ref.13 Ref.16 Ref.19
Modified residue871Phosphoserine Ref.13 Ref.16 Ref.19
Modified residue891Phosphoserine Ref.13 Ref.16
Modified residue2591Phosphoserine Ref.13 Ref.18 Ref.19
Modified residue2941N6-acetyllysine Ref.17
Modified residue3041Phosphoserine Ref.18 Ref.19
Modified residue4261Phosphotyrosine Ref.10
Modified residue4921Phosphoserine Ref.13 Ref.16 Ref.18 Ref.19
Modified residue4941Phosphothreonine Ref.16
Modified residue4961Phosphoserine Ref.13 Ref.16 Ref.19
Modified residue5001Phosphoserine Ref.11 Ref.13 Ref.16
Modified residue5541Phosphoserine Ref.14 Ref.18

Natural variations

Alternative sequence29 – 4315Missing in isoform 3, isoform 4 and isoform 5.
VSP_016728
Alternative sequence213 – 23523Missing in isoform 3.
VSP_016729
Alternative sequence272 – 30736Missing in isoform 3.
VSP_016730
Alternative sequence3891P → PPPGIPITVP in isoform 5.
VSP_046213
Alternative sequence3931F → K in isoform 4.
VSP_016731
Alternative sequence394 – 594201Missing in isoform 4.
VSP_016732

Experimental info

Sequence conflict1181V → I in BAG58575. Ref.3
Sequence conflict3121G → R in AAH24016. Ref.6
Sequence conflict3121G → R in AAH52959. Ref.6
Sequence conflict5241K → R in AAH52959. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B391D142419ED061

FASTA59466,526
        10         20         30         40         50         60 
MSAGEVERLV SELSGGTGGD EEEEWLYGGP WDVHVHSDLA KDLDENEVER PEEENASANP 

        70         80         90        100        110        120 
PSGIEDETAE NGVPKPKVTE TEDDSDSDSD DDEDDVHVTI GDIKTGAPQY GSYGTAPVNL 

       130        140        150        160        170        180 
NIKTGGRVYG TTGTKVKGVD LDAPGSINGV PLLEVDLDSF EDKPWRKPGA DLSDYFNYGF 

       190        200        210        220        230        240 
NEDTWKAYCE KQKRIRMGLE VIPVTSTTNK ITAEDCTMEV TPGAEIQDGR FNLFKVQQGR 

       250        260        270        280        290        300 
TGNSEKETAL PSTKAEFTSP PSLFKTGLPP SRNSTSSQSQ TSTASRKANS SVGKWQDRYG 

       310        320        330        340        350        360 
RAESPDLRRL PGAIDVIGQT ITISRVEGRR RANENSNIQV LSERSATEVD NNFSKPPPFF 

       370        380        390        400        410        420 
PPGAPPTHLP PPPFLPPPPT VSTAPPLIPP PGFPPPPGAP PPSLIPTIES GHSSGYDSRS 

       430        440        450        460        470        480 
ARAFPYGNVA FPHLPGSAPS WPSLVDTSKQ WDYYARREKD RDRERDRDRE RDRDRDRERE 

       490        500        510        520        530        540 
RTRERERERD HSPTPSVFNS DEERYRYREY AERGYERHRA SREKEERHRE RRHREKEETR 

       550        560        570        580        590 
HKSSRSNSRR RHESEEGDSH RRHKHKKSKR SKEGKEAGSE PAPEQESTEA TPAE 

« Hide

Isoform 3 [UniParc].

Checksum: 55D48285A046A783
Show »

FASTA52058,376
Isoform 4 [UniParc].

Checksum: 1B699B114C9560D4
Show »

FASTA37840,835
Isoform 5 [UniParc].

Checksum: 0E9D598DEAF3C752
Show »

FASTA58865,728

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as a therapeutic target of imatinib in idiopathic hypereosinophilic syndrome."
Cools J., DeAngelo D.J., Gotlib J., Stover E.H., Legare R.D., Cortes J., Kutok J., Clark J., Galinsky I., Griffin J.D., Cross N.C., Tefferi A., Malone J., Alam R., Schrier S.L., Schmid J., Rose M., Vandenberghe P. expand/collapse author list , Verhoef G., Boogaerts M., Wlodarska I., Kantarjian H., Marynen P., Coutre S.E., Stone R., Gilliland D.G.
N. Engl. J. Med. 348:1201-1214(2003) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001128409.1. NM_001134937.1.
NP_001128410.1. NM_001134938.1.
NP_112179.2. NM_030917.3.
UniGeneHs.624245.

3D structure databases

ProteinModelPortalQ6UN15.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123545. 19 interactions.
DIPDIP-42503N.
IntActQ6UN15. 13 interactions.
MINTMINT-1475441.
STRING9606.ENSP00000336752.

PTM databases

PhosphoSiteQ6UN15.

Polymorphism databases

DMDM74749365.

Proteomic databases

PaxDbQ6UN15.
PeptideAtlasQ6UN15.
PRIDEQ6UN15.

Protocols and materials databases

DNASU81608.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306932; ENSP00000302993; ENSG00000145216. [Q6UN15-3]
ENST00000337488; ENSP00000336752; ENSG00000145216. [Q6UN15-1]
ENST00000358575; ENSP00000351383; ENSG00000145216. [Q6UN15-5]
ENST00000507922; ENSP00000425456; ENSG00000145216. [Q6UN15-4]
GeneID81608.
KEGGhsa:81608.
UCSCuc003gzx.4. human. [Q6UN15-4]
uc003gzy.3. human. [Q6UN15-1]
uc003gzz.3. human. [Q6UN15-3]
uc011bzu.2. human.

Organism-specific databases

CTD81608.
GeneCardsGC04P054159.
HGNCHGNC:19124. FIP1L1.
HPAHPA037475.
MIM607685. phenotype.
607686. gene.
neXtProtNX_Q6UN15.
Orphanet3260. Idiopathic hypereosinophilic syndrome.
PharmGKBPA134875694.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5213.
HOVERGENHBG059889.
InParanoidQ6UN15.
KOK14405.
OMAGNNIQVI.
OrthoDBEOG7Z3F5S.
PhylomeDBQ6UN15.
TreeFamTF318610.

Gene expression databases

ArrayExpressQ6UN15.
BgeeQ6UN15.
CleanExHS_FIP1L1.
GenevestigatorQ6UN15.

Family and domain databases

InterProIPR007854. Fip1.
[Graphical view]
PfamPF05182. Fip1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFIP1L1. human.
GeneWikiFIP1L1.
GenomeRNAi81608.
NextBio71928.
PMAP-CutDBQ6UN15.
PROQ6UN15.
SOURCESearch...

Entry information

Entry nameFIP1_HUMAN
AccessionPrimary (citable) accession number: Q6UN15
Secondary accession number(s): B4DIR3 expand/collapse secondary AC list , G3XAD6, Q0VGE0, Q499Y4, Q49AU3, Q7Z608, Q8WVN3, Q96F80, Q9H077
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM