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Q9P278 (FNIP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Folliculin-interacting protein 2
Alternative name(s):
FNIP1-like protein
O6-methylguanine-induced apoptosis 1 protein
Gene names
Name:FNIP2
Synonyms:FNIPL, KIAA1450, MAPO1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1114 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the signal transduction pathway of apoptosis induced by O6-methylguanine-mispaired lesions By similarity. May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1. Ref.4 Ref.5

Subunit structure

Forms homomultimers and heteromultimers with FNIP1. Interacts (via C-terminus) with FLCN (via C-terminus). Phosphorylated FLCN is preferentially bound. Interacts with PRKAA1, PRKAB1 and PRKAG1 subunits of 5'-AMP-activated protein kinase. Ref.4 Ref.5

Subcellular location

Cytoplasm. Note: Colocalizes with FLCN in the cytoplasm. Ref.4 Ref.5 Ref.6

Tissue specificity

Widely expressed with highest levels in muscle, nasal mucosa, salivary gland, uvula, fat, liver, heart, placenta and pancreas. Moderately expressed in the lung, small intestine, kidney and brain. Lower levels detected in renal cell carcinoma than in normal kidney tissue. Higher levels detected in oncocytoma than in normal kidney. Ref.4 Ref.5

Post-translational modification

Phosphorylated by AMPK. Ref.5

Miscellaneous

Elevated expression levels in histologic variants of renal tumors.

Sequence similarities

Belongs to the FNIP family.

Sequence caution

The sequence AAH07861.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH16638.1 differs from that shown. Reason: Potential poly-A sequence.

The sequence BAA95974.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB14338.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P278-1)

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 2 (identifier: Q9P278-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MAPTLLQKLFNKRGSSGSSAAASAQGRAPKEGPAF → MCGGTANTTN...RSTDHTELDN

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11141114Folliculin-interacting protein 2
PRO_0000320553

Regions

Region544 – 911368Interaction with PRKAA1
Compositional bias95 – 11622Ser-rich
Compositional bias242 – 26524Ser-rich

Amino acid modifications

Modified residue7231Phosphoserine Ref.7
Modified residue7261Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 3535MAPTL…EGPAF → MCGGTANTTNQPESWQDSAR CVSDAVPGAGRIYRALLCTK IKKHTGVDRSTDHTELDN in isoform 2.
VSP_031656
Natural variant2981T → S.
Corresponds to variant rs2276938 [ dbSNP | Ensembl ].
VAR_045612

Sequences

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

Last modified February 26, 2008. Version 2.
Checksum: 8951340C11EE0D5B

FASTA1,114122,115
        10         20         30         40         50         60 
MAPTLLQKLF NKRGSSGSSA AASAQGRAPK EGPAFSWSCS EFDLNEIRLI VYQDCDRRGR 

        70         80         90        100        110        120 
QVLFDSKAVQ KIEEVTAQKT EDVPIKISAK CCQGSSSVSS SSSSSISSHS SSGGSSHHAK 

       130        140        150        160        170        180 
EQLPKYQYTR PASDVNMLGE MMFGSVAMSY KGSTLKIHYI RSPPQLMISK VFSARMGSFC 

       190        200        210        220        230        240 
GSTNNLQDSF EYINQDPNLG KLNTNQNSLG PCRTGSNLAH STPVDMPSRG QNEDRDSGIA 

       250        260        270        280        290        300 
RSASLSSLLI TPFPSPSSST SSSSSYQRRW LRSQTTSLEN GIIPRRSTDE TFSLAEETCS 

       310        320        330        340        350        360 
SNPAMVRRKK IAISIIFSLC EKEEAQRNFQ DFFFSHFPLF ESHMNRLKSA IEKAMISCRK 

       370        380        390        400        410        420 
IAESSLRVQF YVSRLMEALG EFRGTIWNLY SVPRIAEPVW LTMMSGTLEK NQLCQRFLKE 

       430        440        450        460        470        480 
FTLLIEQINK NQFFAALLTA VLTYHLAWVP TVMPVDHPPI KAFSEKRTSQ SVNMLAKTHP 

       490        500        510        520        530        540 
YNPLWAQLGD LYGAIGSPVR LTRTVVVGKQ KDLVQRILYV LTYFLRCSEL QENQLTWSGN 

       550        560        570        580        590        600 
HGEGDQVLNG SKIITALEKG EVEESEYVVI TVRNEPALVP PILPPTAAER HNPWPTGFPE 

       610        620        630        640        650        660 
CPEGTDSRDL GLKPDKEANR RPEQGSEACS AGCLGPASDA SWKPQNAFCG DEKNKEAPQD 

       670        680        690        700        710        720 
GSSRLPSCEV LGAGMKMDQQ AVCELLKVEM PTRLPDRSVA WPCPDRHLRE KPSLEKVTFQ 

       730        740        750        760        770        780 
IGSFASPESD FESRMKKMEE RVKACGPSLE ASEAADVAQD PQVSRSPFKP GFQENVCCPQ 

       790        800        810        820        830        840 
NRLSEGDEGE SDKGFAEDRG SRNDMAADIA GQLSHAADLG TASHGAGGTG GRRLEATRGL 

       850        860        870        880        890        900 
YVKAAEGPVL EPVAPRCVQR GPGLVAGANI PCGDDNKKAN FRTEGDIPRN ESSDSALGDS 

       910        920        930        940        950        960 
DDEACASAML DLGHGGDRTG GSLEVELPLP RSQSISTQNV RNFGRSLLAG YCPTYMPDLV 

       970        980        990       1000       1010       1020 
LHGTGSDEKL KQCLVADLVH TVHHPVLDEP IAEAVCIIAD TDKWSVQVAT SQRKVTDNMK 

      1030       1040       1050       1060       1070       1080 
LGQDVLVSSQ VSSLLQSILQ LYKLHLPADF CIMHLEDRLQ EMYLKSKMLS EYLRGHTRVH 

      1090       1100       1110 
VKELGVVLGI ESNDLPLLTA IASTHSPYVA QILL 

« Hide

Isoform 2 [UniParc].

Checksum: EE3CE381023899EC
Show »

FASTA1,137124,860

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"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] OF 1-650 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 787-983 (ISOFORM 1).
Tissue: Lymph and 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] OF 663-1114 (ISOFORM 1).
[4]"Identification and characterization of a novel folliculin-interacting protein FNIP2."
Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M., Valera V.A., Linehan W.M., Schmidt L.S.
Gene 415:60-67(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH FLCN; PRKAA1; PRKAB1 AND PRKAG1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]"Interaction of folliculin (Birt-Hogg-Dube gene product) with a novel Fnip1-like (FnipL/Fnip2) protein."
Takagi Y., Kobayashi T., Shiono M., Wang L., Piao X., Sun G., Zhang D., Abe M., Hagiwara Y., Takahashi K., Hino O.
Oncogene 27:5339-5347(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FLCN AND PRKAA1, TISSUE SPECIFICITY, PHOSPHORYLATION.
[6]"A novel protein, MAPO1, that functions in apoptosis triggered by O6-methylguanine mispair in DNA."
Komori K., Takagi Y., Sanada M., Lim T.H., Nakatsu Y., Tsuzuki T., Sekiguchi M., Hidaka M.
Oncogene 28:1142-1150(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"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-723 AND SER-726, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB040883 mRNA. Translation: BAA95974.1. Different initiation.
BC007861 mRNA. Translation: AAH07861.1. Different initiation.
BC016638 mRNA. Translation: AAH16638.1. Sequence problems.
AK022968 mRNA. Translation: BAB14338.1. Different initiation.
CCDSCCDS47155.1. [Q9P278-1]
RefSeqNP_065891.1. NM_020840.1. [Q9P278-1]
XP_005263216.1. XM_005263159.1. [Q9P278-2]
UniGeneHs.652441.
Hs.731810.

3D structure databases

ProteinModelPortalQ9P278.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9P278. 1 interaction.
MINTMINT-7298240.
STRING9606.ENSP00000264433.

PTM databases

PhosphoSiteQ9P278.

Polymorphism databases

DMDM189035874.

Proteomic databases

MaxQBQ9P278.
PaxDbQ9P278.
PRIDEQ9P278.

Protocols and materials databases

DNASU57600.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264433; ENSP00000264433; ENSG00000052795. [Q9P278-1]
ENST00000379346; ENSP00000368651; ENSG00000052795. [Q9P278-2]
GeneID57600.
KEGGhsa:57600.
UCSCuc003iqe.4. human. [Q9P278-1]

Organism-specific databases

CTD57600.
GeneCardsGC04P159690.
HGNCHGNC:29280. FNIP2.
HPAHPA042779.
HPA052758.
MIM612768. gene.
neXtProtNX_Q9P278.
PharmGKBPA162388758.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG330489.
HOGENOMHOG000112624.
HOVERGENHBG059425.
InParanoidQ9P278.
OMAENQLTWS.
OrthoDBEOG7JMGCQ.
PhylomeDBQ9P278.
TreeFamTF324090.

Gene expression databases

ArrayExpressQ9P278.
BgeeQ9P278.
CleanExHS_FNIP2.
GenevestigatorQ9P278.

Family and domain databases

InterProIPR028086. FNIP_C_dom.
IPR026156. FNIP_fam.
IPR028085. FNIP_mid_dom.
IPR028084. FNIP_N_dom.
[Graphical view]
PANTHERPTHR21634. PTHR21634. 1 hit.
PfamPF14638. FNIP_C. 1 hit.
PF14637. FNIP_M. 1 hit.
PF14636. FNIP_N. 1 hit.
[Graphical view]
PRINTSPR02073. FOLLICULNIP1.
ProtoNetSearch...

Other

ChiTaRSFNIP2. human.
GenomeRNAi57600.
NextBio64218.
PROQ9P278.
SOURCESearch...

Entry information

Entry nameFNIP2_HUMAN
AccessionPrimary (citable) accession number: Q9P278
Secondary accession number(s): Q05DC3, Q96I31, Q9H994
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: July 9, 2014
This is version 79 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

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