Q6UN15 (FIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	FIP1L1
Synonyms:	FIP1, RHE

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	594 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mRNA cleavage and polyadenylation specificity factor complex Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 594	594	Pre-mRNA 3'-end-processing factor FIP1		PRO_0000215037
Regions
	Region	1 – 356	356	Necessary for stimulating PAPOLA activity
	Region	1 – 111	111	Sufficient for interaction with PAPOLA
	Region	137 – 243	107	Sufficient for interaction with CPSF4
	Region	443 – 594	152	Sufficient for interaction with CPSF1 and CSTF3
	Compositional bias	356 – 406	51	Pro-rich
	Compositional bias	456 – 562	107	Arg-rich
	Compositional bias	478 – 594	117	Glu-rich
Sites
	Site	339 – 340	2	Breakpoint for interstitial deletion to form the FIP1L1-PDGFRA fusion protein
Amino acid modifications
	Modified residue	85	1	Phosphoserine Ref.13 Ref.15 Ref.18
	Modified residue	87	1	Phosphoserine Ref.13 Ref.15 Ref.18
	Modified residue	89	1	Phosphoserine Ref.13 Ref.15
	Modified residue	259	1	Phosphoserine Ref.13 Ref.17 Ref.18
	Modified residue	294	1	N6-acetyllysine Ref.16
	Modified residue	304	1	Phosphoserine Ref.17 Ref.18
	Modified residue	426	1	Phosphotyrosine Ref.10
	Modified residue	492	1	Phosphoserine Ref.13 Ref.15 Ref.17 Ref.18
	Modified residue	494	1	Phosphothreonine Ref.15
	Modified residue	496	1	Phosphoserine Ref.13 Ref.15 Ref.18
	Modified residue	500	1	Phosphoserine Ref.11 Ref.13 Ref.15
	Modified residue	554	1	Phosphoserine Ref.14 Ref.17
Natural variations
	Alternative sequence	29 – 43	15	Missing in isoform 3, isoform 4 and isoform 5.		VSP_016728
	Alternative sequence	213 – 235	23	Missing in isoform 3.		VSP_016729
	Alternative sequence	272 – 307	36	Missing in isoform 3.		VSP_016730
	Alternative sequence	389	1	P → PPPGIPITVP in isoform 5.		VSP_046213
	Alternative sequence	393	1	F → K in isoform 4.		VSP_016731
	Alternative sequence	394 – 594	201	Missing in isoform 4.		VSP_016732
Experimental info
	Sequence conflict	118	1	V → I in BAG58575. Ref.3
	Sequence conflict	312	1	G → R in AAH24016. Ref.6
	Sequence conflict	312	1	G → R in AAH52959. Ref.6
	Sequence conflict	524	1	K → R in AAH52959. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: B391D142419ED061	FASTA	594	66,526
	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
	Isoform 3 [UniParc]. Checksum: 55D48285A046A783	FASTA	520	58,376
	10 20 30 40 50 60 MSAGEVERLV SELSGGTGGD EEEEWLYGDE NEVERPEEEN ASANPPSGIE DETAENGVPK 70 80 90 100 110 120 PKVTETEDDS DSDSDDDEDD VHVTIGDIKT GAPQYGSYGT APVNLNIKTG GRVYGTTGTK 130 140 150 160 170 180 VKGVDLDAPG SINGVPLLEV DLDSFEDKPW RKPGADLSDY FNYGFNEDTW KAYCEKQKRI 190 200 210 220 230 240 RMGLEVIPVT STTNKITVQQ GRTGNSEKET ALPSTKAEFT SPPSLFKTGL PPSRRLPGAI 250 260 270 280 290 300 DVIGQTITIS RVEGRRRANE NSNIQVLSER SATEVDNNFS KPPPFFPPGA PPTHLPPPPF 310 320 330 340 350 360 LPPPPTVSTA PPLIPPPGFP PPPGAPPPSL IPTIESGHSS GYDSRSARAF PYGNVAFPHL 370 380 390 400 410 420 PGSAPSWPSL VDTSKQWDYY ARREKDRDRE RDRDRERDRD RDRERERTRE RERERDHSPT 430 440 450 460 470 480 PSVFNSDEER YRYREYAERG YERHRASREK EERHRERRHR EKEETRHKSS RSNSRRRHES 490 500 510 520 EEGDSHRRHK HKKSKRSKEG KEAGSEPAPE QESTEATPAE
	Isoform 4 [UniParc]. Checksum: 1B699B114C9560D4	FASTA	378	40,835
	10 20 30 40 50 60 MSAGEVERLV SELSGGTGGD EEEEWLYGDE NEVERPEEEN ASANPPSGIE DETAENGVPK 70 80 90 100 110 120 PKVTETEDDS DSDSDDDEDD VHVTIGDIKT GAPQYGSYGT APVNLNIKTG GRVYGTTGTK 130 140 150 160 170 180 VKGVDLDAPG SINGVPLLEV DLDSFEDKPW RKPGADLSDY FNYGFNEDTW KAYCEKQKRI 190 200 210 220 230 240 RMGLEVIPVT STTNKITAED CTMEVTPGAE IQDGRFNLFK VQQGRTGNSE KETALPSTKA 250 260 270 280 290 300 EFTSPPSLFK TGLPPSRNST SSQSQTSTAS RKANSSVGKW QDRYGRAESP DLRRLPGAID 310 320 330 340 350 360 VIGQTITISR VEGRRRANEN SNIQVLSERS ATEVDNNFSK PPPFFPPGAP PTHLPPPPFL 370 PPPPTVSTAP PLIPPPGK
	Isoform 5 [UniParc]. Checksum: 0E9D598DEAF3C752	FASTA	588	65,728
	10 20 30 40 50 60 MSAGEVERLV SELSGGTGGD EEEEWLYGDE NEVERPEEEN ASANPPSGIE DETAENGVPK 70 80 90 100 110 120 PKVTETEDDS DSDSDDDEDD VHVTIGDIKT GAPQYGSYGT APVNLNIKTG GRVYGTTGTK 130 140 150 160 170 180 VKGVDLDAPG SINGVPLLEV DLDSFEDKPW RKPGADLSDY FNYGFNEDTW KAYCEKQKRI 190 200 210 220 230 240 RMGLEVIPVT STTNKITAED CTMEVTPGAE IQDGRFNLFK VQQGRTGNSE KETALPSTKA 250 260 270 280 290 300 EFTSPPSLFK TGLPPSRNST SSQSQTSTAS RKANSSVGKW QDRYGRAESP DLRRLPGAID 310 320 330 340 350 360 VIGQTITISR VEGRRRANEN SNIQVLSERS ATEVDNNFSK PPPFFPPGAP PTHLPPPPFL 370 380 390 400 410 420 PPPPTVSTAP PLIPPPGIPI TVPPPGFPPP PGAPPPSLIP TIESGHSSGY DSRSARAFPY 430 440 450 460 470 480 GNVAFPHLPG SAPSWPSLVD TSKQWDYYAR REKDRDRERD RDRERDRDRD RERERTRERE 490 500 510 520 530 540 RERDHSPTPS VFNSDEERYR YREYAERGYE RHRASREKEE RHRERRHREK EETRHKSSRS 550 560 570 580 NSRRRHESEE GDSHRRHKHK KSKRSKEGKE AGSEPAPEQE STEATPAE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	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. , 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. , 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[15]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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, MASS SPECTROMETRY.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00008449. IPI00395337. IPI00658114. IPI00965581.
RefSeq	NP_001128409.1. NM_001134937.1. NP_001128410.1. NM_001134938.1. NP_112179.2. NM_030917.3.
UniGene	Hs.624245.
3D structure databases
ProteinModelPortal	Q6UN15.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42503N.
IntAct	Q6UN15. 6 interactions.
MINT	MINT-1475441.
STRING	9606.ENSP00000336752.
PTM databases
PhosphoSite	Q6UN15.
Polymorphism databases
DMDM	74749365.
Proteomic databases
PaxDb	Q6UN15.
PeptideAtlas	Q6UN15.
PRIDE	Q6UN15.
Protocols and materials databases
DNASU	81608.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000306932; ENSP00000302993; ENSG00000145216. ENST00000337488; ENSP00000336752; ENSG00000145216. ENST00000358575; ENSP00000351383; ENSG00000145216. ENST00000507166; ENSP00000423325; ENSG00000145216. ENST00000507922; ENSP00000425456; ENSG00000145216.
GeneID	81608.
KEGG	hsa:81608.
UCSC	uc003gzx.4. human. uc003gzy.3. human. uc003gzz.3. human.
Organism-specific databases
CTD	81608.
GeneCards	GC04P054159.
HGNC	HGNC:19124. FIP1L1.
HPA	HPA037475.
MIM	607685. phenotype. 607686. gene.
neXtProt	NX_Q6UN15.
Orphanet	3260. Idiopathic hypereosinophilic syndrome.
PharmGKB	PA134875694.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5213.
HOVERGEN	HBG059889.
InParanoid	Q6UN15.
KO	K14405.
OMA	GNNIQVI.
OrthoDB	EOG4S4PGB.
PhylomeDB	Q6UN15.
Gene expression databases
ArrayExpress	Q6UN15.
Bgee	Q6UN15.
CleanEx	HS_FIP1L1.
Genevestigator	Q6UN15.
GermOnline	ENSG00000145216. Homo sapiens.
Family and domain databases
InterPro	IPR007854. Fip1. [Graphical view]
Pfam	PF05182. Fip1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FIP1L1. human.
GenomeRNAi	81608.
NextBio	71928.
PMAP-CutDB	Q6UN15.
SOURCE	Search...

Entry information

Entry name

FIP1_HUMAN

Accession

Primary (citable) accession number: Q6UN15
Secondary accession number(s): B4DIR3 , 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 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.