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Protein

Inverted formin-2

Gene

INF2

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

Functioni

Severs actin filaments and accelerates their polymerization and depolymerization.By similarity

Enzyme regulationi

Phosphate inhibits both the depolymerization and severing activities.

GO - Biological processi

  • actin cytoskeleton organization Source: InterPro
  • regulation of cellular component size Source: Ensembl
  • regulation of mitochondrial fission Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Inverted formin-2
Alternative name(s):
HBEBP2-binding protein C
Gene namesi
Name:INF2
Synonyms:C14orf151, C14orf173
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:23791. INF2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • endoplasmic reticulum Source: HPA
  • nucleus Source: HPA
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Focal segmental glomerulosclerosis 5 (FSGS5)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:613237
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131A → T in FSGS5. 1 Publication
VAR_063075
Natural varianti42 – 421L → P in FSGS5. 1 Publication
VAR_063076
Natural varianti76 – 761L → P in FSGS5. 1 Publication
VAR_072229
Natural varianti177 – 1771R → H in FSGS5. 2 Publications
VAR_072230
Natural varianti184 – 1841E → K in FSGS5. 1 Publication
VAR_063077
Natural varianti184 – 1841E → Q in FSGS5. 1 Publication
VAR_072232
Natural varianti186 – 1861S → P in FSGS5. 1 Publication
VAR_063078
Natural varianti193 – 1931Y → H in FSGS5. 1 Publication
VAR_072233
Natural varianti198 – 1981L → R in FSGS5. 2 Publications
VAR_063079
Natural varianti202 – 2021N → D in FSGS5. 1 Publication
VAR_072234
Natural varianti203 – 2031A → D in FSGS5. 1 Publication
VAR_072235
Natural varianti214 – 2141R → C in FSGS5. 2 Publications
VAR_072236
Natural varianti214 – 2141R → H in FSGS5. 2 Publications
VAR_063080
Natural varianti218 – 2181R → Q in FSGS5. 3 Publications
VAR_063081
Natural varianti218 – 2181R → W in FSGS5. 1 Publication
VAR_063082
Natural varianti220 – 2201E → K in FSGS5. 2 Publications
VAR_063083
Natural varianti245 – 2451L → P in FSGS5. 1 Publication
VAR_068845
Charcot-Marie-Tooth disease, dominant, intermediate type, E (CMTDIE)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:614455
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti104 – 1041C → F in CMTDIE. 1 Publication
VAR_067589
Natural varianti104 – 1041C → R in CMTDIE. 1 Publication
VAR_067590
Natural varianti104 – 1041C → W in CMTDIE. 1 Publication
VAR_067591
Natural varianti128 – 1281L → P in CMTDIE. 1 Publication
VAR_067592
Natural varianti132 – 1321L → R in CMTDIE. 1 Publication
VAR_067593
Natural varianti164 – 1663Missing in CMTDIE. 1 Publication
VAR_067594

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi613237. phenotype.
614455. phenotype.
Orphaneti93114. Autosomal dominant intermediate Charcot-Marie-Tooth disease type E.
93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA162392025.

Polymorphism and mutation databases

BioMutaiINF2.
DMDMi166215588.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12491248Inverted formin-2PRO_0000310963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei1147 – 11471Phosphoserine1 Publication
Modified residuei1149 – 11491Phosphoserine1 Publication
Modified residuei1179 – 11791Phosphothreonine3 Publications
Modified residuei1192 – 11921Phosphoserine1 Publication
Modified residuei1206 – 12061Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ27J81.
PaxDbiQ27J81.
PRIDEiQ27J81.

PTM databases

PhosphoSiteiQ27J81.

Miscellaneous databases

PMAP-CutDBQ27J81.

Expressioni

Tissue specificityi

Widely expressed. In the kidney, expression is apparent in podocytes and some tubule cells.1 Publication

Gene expression databases

BgeeiQ27J81.
CleanExiHS_INF2.
ExpressionAtlasiQ27J81. baseline and differential.
GenevisibleiQ27J81. HS.

Organism-specific databases

HPAiHPA000724.

Interactioni

Subunit structurei

Interacts with actin at the FH2 domain.By similarity

Protein-protein interaction databases

BioGridi122172. 9 interactions.
IntActiQ27J81. 6 interactions.
MINTiMINT-7034523.
STRINGi9606.ENSP00000376410.

Structurei

3D structure databases

ProteinModelPortaliQ27J81.
SMRiQ27J81. Positions 53-324, 555-988.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 330329GBD/FH3PROSITE-ProRule annotationAdd
BLAST
Domaini554 – 946393FH2PROSITE-ProRule annotationAdd
BLAST
Domaini974 – 98916WH2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili874 – 95178Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi389 – 3935Poly-Ala
Compositional biasi421 – 520100Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the formin homology family.Curated
Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation
Contains 1 WH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG149898.
GeneTreeiENSGT00760000118986.
HOVERGENiHBG081794.
InParanoidiQ27J81.
OMAiQPVDHAQ.
OrthoDBiEOG7T4MN4.
PhylomeDBiQ27J81.
TreeFamiTF326300.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
IPR027649. Inf2.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR23213:SF5. PTHR23213:SF5. 1 hit.
PfamiPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
PF02205. WH2. 1 hit.
[Graphical view]
SMARTiSM00498. FH2. 1 hit.
SM00246. WH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
PS51082. WH2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q27J81-1) [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
MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESADPELCIR LLQMPSVVNY
60 70 80 90 100
SGLRKRLEGS DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT
110 120 130 140 150
CVSCVRAVMN SRQGIEYILS NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL
160 170 180 190 200
CIYSPEGHVL TLDALDHYKT VCSQQYRFSI VMNELSGSDN VPYVVTLLSV
210 220 230 240 250
INAVILGPED LRARTQLRNE FIGLQLLDVL ARLRDLEDAD LLIQLEAFEE
260 270 280 290 300
AKAEDEEELL RVSGGVDMSS HQEVFASLFH KVSCSPVSAQ LLSVLQGLLH
310 320 330 340 350
LEPTLRSSQL LWEALESLVN RAVLLASDAQ ECTLEEVVER LLSVKGRPRP
360 370 380 390 400
SPLVKAHKSV QANLDQSQRG SSPQNTTTPK PSVEGQQPAA AAACEPVDHA
410 420 430 440 450
QSESILKVSQ PRALEQQAST PPPPPPPPLL PGSSAEPPPP PPPPPLPSVG
460 470 480 490 500
AKALPTAPPP PPLPGLGAMA PPAPPLPPPL PGSCEFLPPP PPPLPGLGCP
510 520 530 540 550
PPPPPLLPGM GWGPPPPPPP LLPCTCSPPV AGGMEEVIVA QVDHGLGSAW
560 570 580 590 600
VPSHRRVNPP TLRMKKLNWQ KLPSNVAREH NSMWASLSSP DAEAVEPDFS
610 620 630 640 650
SIERLFSFPA AKPKEPTMVA PRARKEPKEI TFLDAKKSLN LNIFLKQFKC
660 670 680 690 700
SNEEVAAMIR AGDTTKFDVE VLKQLLKLLP EKHEIENLRA FTEERAKLAS
710 720 730 740 750
ADHFYLLLLA IPCYQLRIEC MLLCEGAAAV LDMVRPKAQL VLAACESLLT
760 770 780 790 800
SRQLPIFCQL ILRIGNFLNY GSHTGDADGF KISTLLKLTE TKSQQNRVTL
810 820 830 840 850
LHHVLEEAEK SHPDLLQLPR DLEQPSQAAG INLEIIRSEA SSNLKKLLET
860 870 880 890 900
ERKVSASVAE VQEQYTERLQ ASISAFRALD ELFEAIEQKQ RELADYLCED
910 920 930 940 950
AQQLSLEDTF STMKAFRDLF LRALKENKDR KEQAAKAERR KQQLAEEEAR
960 970 980 990 1000
RPRGEDGKPV RKGPGKQEEV CVIDALLADI RKGFQLRKTA RGRGDTDGGS
1010 1020 1030 1040 1050
KAASMDPPRA TEPVATSNPA GDPVGSTRCP ASEPGLDATT ASESRGWDLV
1060 1070 1080 1090 1100
DAVTPGPQPT LEQLEEGGPR PLERRSSWYV DASDVLTTED PQCPQPLEGA
1110 1120 1130 1140 1150
WPVTLGDAQA LKPLKFSSNQ PPAAGSSRQD AKDPTSLLGV LQAEADSTSE
1160 1170 1180 1190 1200
GLEDAVHSRG ARPPAAGPGG DEDEDEEDTA PESALDTSLD KSFSEDAVTD
1210 1220 1230 1240
SSGSGTLPRA RGRASKGTGK RRKKRPSRSQ EEVPPDSDDN KTKKLCVIQ
Length:1,249
Mass (Da):135,624
Last modified:January 15, 2008 - v2
Checksum:i120BE3E0D209BFC0
GO
Isoform 2 (identifier: Q27J81-2) [UniParc]FASTAAdd to basket

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

Note: Contains a phosphoserine at position 1229.1 Publication
Show »
Length:1,240
Mass (Da):134,617
Checksum:i3D8D4B942072E19E
GO
Isoform 3 (identifier: Q27J81-3) [UniParc]FASTAAdd to basket

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

Show »
Length:234
Mass (Da):25,954
Checksum:i76C59D96787B51E7
GO

Sequence cautioni

The sequence AAH08756.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH64828.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence ABD59343.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence ABD59344.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence ABD59345.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15224.1 differs from that shown. Reason: Erroneous termination at positions 636 and 759. Translated as Lys, Gln.Curated
The sequence EAW81872.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti832 – 8321N → S in BAB15224 (PubMed:14702039).Curated
Sequence conflicti880 – 8801D → V in BAB15224 (PubMed:14702039).Curated
Sequence conflicti1129 – 11291Q → K in CAH10628 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131A → T in FSGS5. 1 Publication
VAR_063075
Natural varianti42 – 421L → P in FSGS5. 1 Publication
VAR_063076
Natural varianti76 – 761L → P in FSGS5. 1 Publication
VAR_072229
Natural varianti104 – 1041C → F in CMTDIE. 1 Publication
VAR_067589
Natural varianti104 – 1041C → R in CMTDIE. 1 Publication
VAR_067590
Natural varianti104 – 1041C → W in CMTDIE. 1 Publication
VAR_067591
Natural varianti128 – 1281L → P in CMTDIE. 1 Publication
VAR_067592
Natural varianti132 – 1321L → R in CMTDIE. 1 Publication
VAR_067593
Natural varianti164 – 1663Missing in CMTDIE. 1 Publication
VAR_067594
Natural varianti177 – 1771R → H in FSGS5. 2 Publications
VAR_072230
Natural varianti183 – 1831N → K.1 Publication
VAR_072231
Natural varianti184 – 1841E → K in FSGS5. 1 Publication
VAR_063077
Natural varianti184 – 1841E → Q in FSGS5. 1 Publication
VAR_072232
Natural varianti186 – 1861S → P in FSGS5. 1 Publication
VAR_063078
Natural varianti193 – 1931Y → H in FSGS5. 1 Publication
VAR_072233
Natural varianti198 – 1981L → R in FSGS5. 2 Publications
VAR_063079
Natural varianti202 – 2021N → D in FSGS5. 1 Publication
VAR_072234
Natural varianti203 – 2031A → D in FSGS5. 1 Publication
VAR_072235
Natural varianti214 – 2141R → C in FSGS5. 2 Publications
VAR_072236
Natural varianti214 – 2141R → H in FSGS5. 2 Publications
VAR_063080
Natural varianti218 – 2181R → Q in FSGS5. 3 Publications
VAR_063081
Natural varianti218 – 2181R → W in FSGS5. 1 Publication
VAR_063082
Natural varianti220 – 2201E → K in FSGS5. 2 Publications
VAR_063083
Natural varianti245 – 2451L → P in FSGS5. 1 Publication
VAR_068845
Natural varianti547 – 5471G → D.1 Publication
VAR_072237
Natural varianti1096 – 10961P → S.1 Publication
Corresponds to variant rs34251364 [ dbSNP | Ensembl ].
VAR_037117
Natural varianti1135 – 11351T → M.
Corresponds to variant rs3803311 [ dbSNP | Ensembl ].
VAR_037118
Natural varianti1160 – 11601G → S.1 Publication
VAR_072238

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei235 – 12491015Missing in isoform 3. 2 PublicationsVSP_029360Add
BLAST
Alternative sequencei1232 – 124918EVPPD…LCVIQ → GLRPRPKAK in isoform 2. 3 PublicationsVSP_029361Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41999.1. [Q27J81-3]
CCDS45173.1. [Q27J81-2]
CCDS9989.2. [Q27J81-1]
RefSeqiNP_001026884.3. NM_001031714.3. [Q27J81-2]
NP_071934.3. NM_022489.3. [Q27J81-1]
NP_116103.1. NM_032714.2. [Q27J81-3]
UniGeneiHs.24956.

Genome annotation databases

EnsembliENST00000330634; ENSP00000376406; ENSG00000203485. [Q27J81-2]
ENST00000392634; ENSP00000376410; ENSG00000203485. [Q27J81-1]
ENST00000398337; ENSP00000381380; ENSG00000203485. [Q27J81-3]
GeneIDi64423.
KEGGihsa:64423.
UCSCiuc001yoy.4. human. [Q27J81-3]
uc001ypb.2. human. [Q27J81-1]
uc001ypc.2. human. [Q27J81-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41999.1. [Q27J81-3]
CCDS45173.1. [Q27J81-2]
CCDS9989.2. [Q27J81-1]
RefSeqiNP_001026884.3. NM_001031714.3. [Q27J81-2]
NP_071934.3. NM_022489.3. [Q27J81-1]
NP_116103.1. NM_032714.2. [Q27J81-3]
UniGeneiHs.24956.

3D structure databases

ProteinModelPortaliQ27J81.
SMRiQ27J81. Positions 53-324, 555-988.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122172. 9 interactions.
IntActiQ27J81. 6 interactions.
MINTiMINT-7034523.
STRINGi9606.ENSP00000376410.

PTM databases

PhosphoSiteiQ27J81.

Polymorphism and mutation databases

BioMutaiINF2.
DMDMi166215588.

Proteomic databases

MaxQBiQ27J81.
PaxDbiQ27J81.
PRIDEiQ27J81.

Protocols and materials databases

DNASUi64423.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330634; ENSP00000376406; ENSG00000203485. [Q27J81-2]
ENST00000392634; ENSP00000376410; ENSG00000203485. [Q27J81-1]
ENST00000398337; ENSP00000381380; ENSG00000203485. [Q27J81-3]
GeneIDi64423.
KEGGihsa:64423.
UCSCiuc001yoy.4. human. [Q27J81-3]
uc001ypb.2. human. [Q27J81-1]
uc001ypc.2. human. [Q27J81-2]

Organism-specific databases

CTDi64423.
GeneCardsiGC14P105155.
HGNCiHGNC:23791. INF2.
HPAiHPA000724.
MIMi610982. gene.
613237. phenotype.
614455. phenotype.
neXtProtiNX_Q27J81.
Orphaneti93114. Autosomal dominant intermediate Charcot-Marie-Tooth disease type E.
93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA162392025.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG149898.
GeneTreeiENSGT00760000118986.
HOVERGENiHBG081794.
InParanoidiQ27J81.
OMAiQPVDHAQ.
OrthoDBiEOG7T4MN4.
PhylomeDBiQ27J81.
TreeFamiTF326300.

Miscellaneous databases

ChiTaRSiINF2. human.
GeneWikiiINF2.
GenomeRNAii64423.
NextBioi66417.
PMAP-CutDBQ27J81.
PROiQ27J81.
SOURCEiSearch...

Gene expression databases

BgeeiQ27J81.
CleanExiHS_INF2.
ExpressionAtlasiQ27J81. baseline and differential.
GenevisibleiQ27J81. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR010473. GTPase-bd.
IPR014768. GTPase-bd/formin_homology_3.
IPR027649. Inf2.
IPR003124. WH2_dom.
[Graphical view]
PANTHERiPTHR23213:SF5. PTHR23213:SF5. 1 hit.
PfamiPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 1 hit.
PF02181. FH2. 1 hit.
PF02205. WH2. 1 hit.
[Graphical view]
SMARTiSM00498. FH2. 1 hit.
SM00246. WH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
PS51082. WH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Mammary carcinoma.
  8. 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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1147 AND SER-1149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. 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.
  19. Cited for: VARIANTS FSGS5 PRO-76; HIS-177; HIS-193; ARG-198; CYS-214; GLN-218 AND LYS-220.
  20. Cited for: VARIANTS CMTDIE ARG-104; PHE-104; TRP-104; PRO-128; ARG-132 AND 164-ALA--ASP-166 DEL.
  21. "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.
  22. "Inverted formin 2 mutations with variable expression in patients with sporadic and hereditary focal and segmental glomerulosclerosis."
    Gbadegesin R.A., Lavin P.J., Hall G., Bartkowiak B., Homstad A., Jiang R., Wu G., Byrd A., Lynn K., Wolfish N., Ottati C., Stevens P., Howell D., Conlon P., Winn M.P.
    Kidney Int. 81:94-99(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FSGS5 HIS-177; GLN-184; ASP-202; ASP-203; CYS-214; HIS-214 AND GLN-218, VARIANTS LYS-183; ASP-547; SER-1096 AND SER-1160.

Entry informationi

Entry nameiINF2_HUMAN
AccessioniPrimary (citable) accession number: Q27J81
Secondary accession number(s): Q27J83
, Q69YL8, Q6P1X7, Q6PK22, Q86TR7, Q9BRM1, Q9H6N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: June 24, 2015
This is version 93 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.