Q27J81 (INF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inverted formin-2

Alternative name(s):
HBEBP2-binding protein C

Gene names

Name:	INF2
Synonyms:	C14orf151, C14orf173

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	1249 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Severs actin filaments and accelerates their polymerization and depolymerization By similarity.
Enzyme regulation	Phosphate inhibits both the depolymerization and severing activities.
Subunit structure	Interacts with actin at the FH2 domain By similarity.
Subcellular location	Cytoplasm › perinuclear region Ref.16.
Tissue specificity	Widely expressed. In the kidney, expression is apparent in podocytes and some tubule cells. Ref.16
Domain	The WH2 domain acts as the DAD (diaphanous autoregulatory) domain and binds to actin monomers By similarity. Regulated by autoinhibition due to intramolecular GBD-DAD binding By similarity. The severing activity is dependent on covalent attachment of the FH2 domain to the C-terminus By similarity.
Involvement in disease	Focal segmental glomerulosclerosis 5 (FSGS5) [MIM:613237]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.18 Charcot-Marie-Tooth disease, dominant, intermediate type, E (CMTDIE) [MIM:614455]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type E is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec. Patients additionally manifest focal segmental glomerulonephritis, proteinuria, progression to end-stage renal disease, and a characteristic histologic pattern on renal biopsy. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17
Sequence similarities	Belongs to the formin homology family. Contains 1 FH2 (formin homology 2) domain. Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain. Contains 1 WH2 domain.
Sequence caution	The sequence AAH08756.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAH64828.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence ABD59343.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence ABD59344.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence ABD59345.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB15224.1 differs from that shown. Reason: Erroneous termination at positions 636 and 759. Translated as Lys, Gln. The sequence EAW81872.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Charcot-Marie-Tooth disease Disease mutation Neuropathy
Domain	Coiled coil
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from electronic annotation. Source: InterPro
Cellular_component	endoplasmic reticulum Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA perinuclear region of cytoplasm Inferred from direct assay Ref.16. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q27J81-1)

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: Q27J81-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1232-1249: EVPPDSDDNKTKKLCVIQ → GLRPRPKAK

Note: Contains a phosphoserine at position 1229.

Isoform 3 (identifier: Q27J81-3)

The sequence of this isoform differs from the canonical sequence as follows:
     235-1249: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1249	1249	Inverted formin-2		PRO_0000310963
Regions
	Domain	1 – 330	330	GBD/FH3
	Domain	554 – 946	393	FH2
	Domain	974 – 989	16	WH2
	Coiled coil	874 – 951	78	Potential
	Compositional bias	389 – 393	5	Poly-Ala
	Compositional bias	421 – 520	100	Pro-rich
Amino acid modifications
	Modified residue	1147	1	Phosphoserine Ref.10
	Modified residue	1149	1	Phosphoserine Ref.10
	Modified residue	1179	1	Phosphothreonine Ref.11 Ref.13
	Modified residue	1192	1	Phosphoserine Ref.15
	Modified residue	1206	1	Phosphothreonine Ref.12
Natural variations
	Alternative sequence	235 – 1249	1015	Missing in isoform 3.		VSP_029360
	Alternative sequence	1232 – 1249	18	EVPPD…LCVIQ → GLRPRPKAK in isoform 2.		VSP_029361
	Natural variant	13	1	A → T in FSGS5. Ref.16		VAR_063075
	Natural variant	42	1	L → P in FSGS5. Ref.16		VAR_063076
	Natural variant	104	1	C → F in CMTDIE. Ref.17		VAR_067589
	Natural variant	104	1	C → R in CMTDIE. Ref.17		VAR_067590
	Natural variant	104	1	C → W in CMTDIE. Ref.17		VAR_067591
	Natural variant	128	1	L → P in CMTDIE. Ref.17		VAR_067592
	Natural variant	132	1	L → R in CMTDIE. Ref.17		VAR_067593
	Natural variant	164 – 166	3	Missing in CMTDIE.		VAR_067594
	Natural variant	184	1	E → K in FSGS5. Ref.16		VAR_063077
	Natural variant	186	1	S → P in FSGS5. Ref.16		VAR_063078
	Natural variant	198	1	L → R in FSGS5. Ref.16		VAR_063079
	Natural variant	214	1	R → H in FSGS5. Ref.16		VAR_063080
	Natural variant	218	1	R → Q in FSGS5. Ref.16		VAR_063081
	Natural variant	218	1	R → W in FSGS5. Ref.16		VAR_063082
	Natural variant	220	1	E → K in FSGS5. Ref.16		VAR_063083
	Natural variant	245	1	L → P in FSGS5. Ref.18		VAR_068845
	Natural variant	1096	1	P → S. Corresponds to variant rs34251364 [ dbSNP | Ensembl ].		VAR_037117
	Natural variant	1135	1	T → M. Corresponds to variant rs3803311 [ dbSNP | Ensembl ].		VAR_037118
Experimental info
	Sequence conflict	832	1	N → S in BAB15224. Ref.1
	Sequence conflict	880	1	D → V in BAB15224. Ref.1
	Sequence conflict	1129	1	Q → K in CAH10628. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: 120BE3E0D209BFC0	FASTA	1,249	135,624
	10 20 30 40 50 60 MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESADPELCIR LLQMPSVVNY SGLRKRLEGS 70 80 90 100 110 120 DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT CVSCVRAVMN SRQGIEYILS 130 140 150 160 170 180 NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHVL TLDALDHYKT VCSQQYRFSI 190 200 210 220 230 240 VMNELSGSDN VPYVVTLLSV INAVILGPED LRARTQLRNE FIGLQLLDVL ARLRDLEDAD 250 260 270 280 290 300 LLIQLEAFEE AKAEDEEELL RVSGGVDMSS HQEVFASLFH KVSCSPVSAQ LLSVLQGLLH 310 320 330 340 350 360 LEPTLRSSQL LWEALESLVN RAVLLASDAQ ECTLEEVVER LLSVKGRPRP SPLVKAHKSV 370 380 390 400 410 420 QANLDQSQRG SSPQNTTTPK PSVEGQQPAA AAACEPVDHA QSESILKVSQ PRALEQQAST 430 440 450 460 470 480 PPPPPPPPLL PGSSAEPPPP PPPPPLPSVG AKALPTAPPP PPLPGLGAMA PPAPPLPPPL 490 500 510 520 530 540 PGSCEFLPPP PPPLPGLGCP PPPPPLLPGM GWGPPPPPPP LLPCTCSPPV AGGMEEVIVA 550 560 570 580 590 600 QVDHGLGSAW VPSHRRVNPP TLRMKKLNWQ KLPSNVAREH NSMWASLSSP DAEAVEPDFS 610 620 630 640 650 660 SIERLFSFPA AKPKEPTMVA PRARKEPKEI TFLDAKKSLN LNIFLKQFKC SNEEVAAMIR 670 680 690 700 710 720 AGDTTKFDVE VLKQLLKLLP EKHEIENLRA FTEERAKLAS ADHFYLLLLA IPCYQLRIEC 730 740 750 760 770 780 MLLCEGAAAV LDMVRPKAQL VLAACESLLT SRQLPIFCQL ILRIGNFLNY GSHTGDADGF 790 800 810 820 830 840 KISTLLKLTE TKSQQNRVTL LHHVLEEAEK SHPDLLQLPR DLEQPSQAAG INLEIIRSEA 850 860 870 880 890 900 SSNLKKLLET ERKVSASVAE VQEQYTERLQ ASISAFRALD ELFEAIEQKQ RELADYLCED 910 920 930 940 950 960 AQQLSLEDTF STMKAFRDLF LRALKENKDR KEQAAKAERR KQQLAEEEAR RPRGEDGKPV 970 980 990 1000 1010 1020 RKGPGKQEEV CVIDALLADI RKGFQLRKTA RGRGDTDGGS KAASMDPPRA TEPVATSNPA 1030 1040 1050 1060 1070 1080 GDPVGSTRCP ASEPGLDATT ASESRGWDLV DAVTPGPQPT LEQLEEGGPR PLERRSSWYV 1090 1100 1110 1120 1130 1140 DASDVLTTED PQCPQPLEGA WPVTLGDAQA LKPLKFSSNQ PPAAGSSRQD AKDPTSLLGV 1150 1160 1170 1180 1190 1200 LQAEADSTSE GLEDAVHSRG ARPPAAGPGG DEDEDEEDTA PESALDTSLD KSFSEDAVTD 1210 1220 1230 1240 SSGSGTLPRA RGRASKGTGK RRKKRPSRSQ EEVPPDSDDN KTKKLCVIQ
	Isoform 2 [UniParc]. Checksum: 3D8D4B942072E19E	FASTA	1,240	134,617
	10 20 30 40 50 60 MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESADPELCIR LLQMPSVVNY SGLRKRLEGS 70 80 90 100 110 120 DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT CVSCVRAVMN SRQGIEYILS 130 140 150 160 170 180 NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHVL TLDALDHYKT VCSQQYRFSI 190 200 210 220 230 240 VMNELSGSDN VPYVVTLLSV INAVILGPED LRARTQLRNE FIGLQLLDVL ARLRDLEDAD 250 260 270 280 290 300 LLIQLEAFEE AKAEDEEELL RVSGGVDMSS HQEVFASLFH KVSCSPVSAQ LLSVLQGLLH 310 320 330 340 350 360 LEPTLRSSQL LWEALESLVN RAVLLASDAQ ECTLEEVVER LLSVKGRPRP SPLVKAHKSV 370 380 390 400 410 420 QANLDQSQRG SSPQNTTTPK PSVEGQQPAA AAACEPVDHA QSESILKVSQ PRALEQQAST 430 440 450 460 470 480 PPPPPPPPLL PGSSAEPPPP PPPPPLPSVG AKALPTAPPP PPLPGLGAMA PPAPPLPPPL 490 500 510 520 530 540 PGSCEFLPPP PPPLPGLGCP PPPPPLLPGM GWGPPPPPPP LLPCTCSPPV AGGMEEVIVA 550 560 570 580 590 600 QVDHGLGSAW VPSHRRVNPP TLRMKKLNWQ KLPSNVAREH NSMWASLSSP DAEAVEPDFS 610 620 630 640 650 660 SIERLFSFPA AKPKEPTMVA PRARKEPKEI TFLDAKKSLN LNIFLKQFKC SNEEVAAMIR 670 680 690 700 710 720 AGDTTKFDVE VLKQLLKLLP EKHEIENLRA FTEERAKLAS ADHFYLLLLA IPCYQLRIEC 730 740 750 760 770 780 MLLCEGAAAV LDMVRPKAQL VLAACESLLT SRQLPIFCQL ILRIGNFLNY GSHTGDADGF 790 800 810 820 830 840 KISTLLKLTE TKSQQNRVTL LHHVLEEAEK SHPDLLQLPR DLEQPSQAAG INLEIIRSEA 850 860 870 880 890 900 SSNLKKLLET ERKVSASVAE VQEQYTERLQ ASISAFRALD ELFEAIEQKQ RELADYLCED 910 920 930 940 950 960 AQQLSLEDTF STMKAFRDLF LRALKENKDR KEQAAKAERR KQQLAEEEAR RPRGEDGKPV 970 980 990 1000 1010 1020 RKGPGKQEEV CVIDALLADI RKGFQLRKTA RGRGDTDGGS KAASMDPPRA TEPVATSNPA 1030 1040 1050 1060 1070 1080 GDPVGSTRCP ASEPGLDATT ASESRGWDLV DAVTPGPQPT LEQLEEGGPR PLERRSSWYV 1090 1100 1110 1120 1130 1140 DASDVLTTED PQCPQPLEGA WPVTLGDAQA LKPLKFSSNQ PPAAGSSRQD AKDPTSLLGV 1150 1160 1170 1180 1190 1200 LQAEADSTSE GLEDAVHSRG ARPPAAGPGG DEDEDEEDTA PESALDTSLD KSFSEDAVTD 1210 1220 1230 1240 SSGSGTLPRA RGRASKGTGK RRKKRPSRSQ EGLRPRPKAK
	Isoform 3 [UniParc]. Checksum: 76C59D96787B51E7	FASTA	234	25,954
	10 20 30 40 50 60 MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESADPELCIR LLQMPSVVNY SGLRKRLEGS 70 80 90 100 110 120 DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT CVSCVRAVMN SRQGIEYILS 130 140 150 160 170 180 NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHVL TLDALDHYKT VCSQQYRFSI 190 200 210 220 230 VMNELSGSDN VPYVVTLLSV INAVILGPED LRARTQLRNE FIGLQLLDVL ARLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 633-1249 (ISOFORM 1).
[2]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.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].
[4]	"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 650-1249 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 851-1249 (ISOFORM 1). Tissue: Eye, PNS and Uterus.
[5]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-279. Tissue: Fetal brain.
[6]	"Cloning of human chromosome 14 open reading frame 173 (C14orf173)." Wang P., Deng W., Shi T., Ma D. Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 533-1249 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 533-1249 (ISOFORM 2).
[7]	Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 661-673; 764-781 AND 869-889, MASS SPECTROMETRY. Tissue: Mammary carcinoma.
[8]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1128-1249 (ISOFORM 2). Tissue: Melanoma.
[9]	"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-1229 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-1147 AND SER-1149, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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 THR-1179, MASS SPECTROMETRY. Tissue: Liver.
[12]	"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 THR-1206, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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 THR-1179, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"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-1192, MASS SPECTROMETRY.
[16]	"Mutations in the formin gene INF2 cause focal segmental glomerulosclerosis." Brown E.J., Schlondorff J.S., Becker D.J., Tsukaguchi H., Tonna S.J., Uscinski A.L., Higgs H.N., Henderson J.M., Pollak M.R. Nat. Genet. 42:72-76(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FSGS5 THR-13; PRO-42; LYS-184; PRO-186; ARG-198; HIS-214; TRP-218; GLN-218 AND LYS-220, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[17]	"INF2 mutations in Charcot-Marie-Tooth disease with glomerulopathy." Boyer O., Nevo F., Plaisier E., Funalot B., Gribouval O., Benoit G., Cong E.H., Arrondel C., Tete M.J., Montjean R., Richard L., Karras A., Pouteil-Noble C., Balafrej L., Bonnardeaux A., Canaud G., Charasse C., Dantal J. , Deschenes G., Deteix P., Dubourg O., Petiot P., Pouthier D., Leguern E., Guiochon-Mantel A., Broutin I., Gubler M.C., Saunier S., Ronco P., Vallat J.M., Alonso M.A., Antignac C., Mollet G. N. Engl. J. Med. 365:2377-2388(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMTDIE ARG-104; PHE-104; TRP-104; PRO-128; ARG-132 AND 164-ALA--ASP-166 DEL.
[18]	"A novel mutation, outside of the candidate region for diagnosis, in the inverted formin 2 gene can cause focal segmental glomerulosclerosis." Sanchez-Ares M., Garcia-Vidal M., Antucho E.E., Julio P., Eduardo V.M., Lens X.M., Garcia-Gonzalez M.A. Kidney Int. 83:153-159(2013) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FSGS5 PRO-245.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK025709 mRNA. Translation: BAB15224.1. Sequence problems. AK290083 mRNA. Translation: BAF82772.1. AL583722 Genomic DNA. No translation available. CH471061 Genomic DNA. Translation: EAW81872.1. Sequence problems. BC006173 mRNA. Translation: AAH06173.1. BC008756 mRNA. Translation: AAH08756.2. Different initiation. BC064828 mRNA. Translation: AAH64828.1. Different initiation. BX248757 mRNA. Translation: CAD66564.1. DQ395338 mRNA. Translation: ABD59343.1. Different initiation. DQ395339 mRNA. Translation: ABD59344.1. Different initiation. DQ395340 mRNA. Translation: ABD59345.1. Different initiation. AL832905 mRNA. Translation: CAH10628.1.
IPI	IPI00876962. IPI00895800. IPI00937711.
RefSeq	NP_001026884.3. NM_001031714.3. NP_071934.3. NM_022489.3. NP_116103.1. NM_032714.2.
UniGene	Hs.24956.
3D structure databases
ProteinModelPortal	Q27J81.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q27J81. 4 interactions.
MINT	MINT-7034523.
STRING	9606.ENSP00000376410.
PTM databases
PhosphoSite	Q27J81.
Polymorphism databases
DMDM	166215588.
Proteomic databases
PaxDb	Q27J81.
PRIDE	Q27J81.
Protocols and materials databases
DNASU	64423.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000330634; ENSP00000376406; ENSG00000203485. ENST00000392634; ENSP00000376410; ENSG00000203485. ENST00000398337; ENSP00000381380; ENSG00000203485.
GeneID	64423.
KEGG	hsa:64423.
UCSC	uc001yoy.4. human. uc001ypb.2. human. uc001ypc.2. human.
Organism-specific databases
CTD	64423.
GeneCards	GC14P105155.
HGNC	HGNC:23791. INF2.
HPA	HPA000724.
MIM	610982. gene. 613237. phenotype. 614455. phenotype.
neXtProt	NX_Q27J81.
Orphanet	93114. Charcot-Marie-Tooth disease - nephropathy. 93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKB	PA162392025.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG149898.
HOVERGEN	HBG081794.
InParanoid	Q27J81.
OMA	ASDAQEC.
OrthoDB	EOG49W2DN.
Gene expression databases
ArrayExpress	Q27J81.
Bgee	Q27J81.
CleanEx	HS_INF2.
Genevestigator	Q27J81.
Family and domain databases
InterPro	IPR003104. Actin-bd_FH2/DRF_autoreg. IPR016024. ARM-type_fold. IPR010472. Drf_FH3. IPR010473. Drf_GTPase-bd. IPR015425. FH2_actin-bd. IPR014768. GTPase-bd/formin_homology_3. IPR003124. WH2_dom. [Graphical view]
Pfam	PF06367. Drf_FH3. 1 hit. PF06371. Drf_GBD. 1 hit. PF02181. FH2. 1 hit. PF02205. WH2. 1 hit. [Graphical view]
SMART	SM00498. FH2. 1 hit. SM00246. WH2. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF101447. FH2_actin_bd. 1 hit.
PROSITE	PS51444. FH2. 1 hit. PS51232. GBD_FH3. 1 hit. PS51082. WH2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	INF2. human.
GenomeRNAi	64423.
NextBio	66417.
PMAP-CutDB	Q27J81.
SOURCE	Search...

Entry information

Entry name

INF2_HUMAN

Accession

Primary (citable) accession number: Q27J81
Secondary accession number(s): Q27J83 , Q69YL8, Q6P1X7, Q6PK22, Q86TR7, Q9BRM1, Q9H6N1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	May 1, 2013
This is version 74 of the entry and version 2 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.