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Q27J81

- INF2_HUMAN

UniProt

Q27J81 - INF2_HUMAN

Protein

Inverted formin-2

Gene

INF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    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

    1. actin cytoskeleton organization Source: InterPro
    2. cell death Source: UniProtKB-KW
    3. regulation of cellular component size Source: Ensembl
    4. regulation of mitochondrial fission Source: MGI

    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: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:23791. INF2.

    Subcellular locationi

    Cytoplasmperinuclear region 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. endoplasmic reticulum Source: HPA
    3. nucleus Source: HPA
    4. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 varianti184 – 1841E → K in FSGS5. 1 Publication
    VAR_063077
    Natural varianti186 – 1861S → P in FSGS5. 1 Publication
    VAR_063078
    Natural varianti198 – 1981L → R in FSGS5. 1 Publication
    VAR_063079
    Natural varianti214 – 2141R → H in FSGS5. 1 Publication
    VAR_063080
    Natural varianti218 – 2181R → Q in FSGS5. 1 Publication
    VAR_063081
    Natural varianti218 – 2181R → W in FSGS5. 1 Publication
    VAR_063082
    Natural varianti220 – 2201E → K in FSGS5. 1 Publication
    VAR_063083
    Natural varianti245 – 2451L → P in FSGS5. 1 Publication
    VAR_068845
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.
    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.

    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 – 11791Phosphothreonine2 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.
    GenevestigatoriQ27J81.

    Organism-specific databases

    HPAiHPA000724.

    Interactioni

    Subunit structurei

    Interacts with actin at the FH2 domain.By similarity

    Protein-protein interaction databases

    BioGridi122172. 7 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.
    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. Align

    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

    MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESADPELCIR LLQMPSVVNY     50
    SGLRKRLEGS DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT 100
    CVSCVRAVMN SRQGIEYILS NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL 150
    CIYSPEGHVL TLDALDHYKT VCSQQYRFSI VMNELSGSDN VPYVVTLLSV 200
    INAVILGPED LRARTQLRNE FIGLQLLDVL ARLRDLEDAD LLIQLEAFEE 250
    AKAEDEEELL RVSGGVDMSS HQEVFASLFH KVSCSPVSAQ LLSVLQGLLH 300
    LEPTLRSSQL LWEALESLVN RAVLLASDAQ ECTLEEVVER LLSVKGRPRP 350
    SPLVKAHKSV QANLDQSQRG SSPQNTTTPK PSVEGQQPAA AAACEPVDHA 400
    QSESILKVSQ PRALEQQAST PPPPPPPPLL PGSSAEPPPP PPPPPLPSVG 450
    AKALPTAPPP PPLPGLGAMA PPAPPLPPPL PGSCEFLPPP PPPLPGLGCP 500
    PPPPPLLPGM GWGPPPPPPP LLPCTCSPPV AGGMEEVIVA QVDHGLGSAW 550
    VPSHRRVNPP TLRMKKLNWQ KLPSNVAREH NSMWASLSSP DAEAVEPDFS 600
    SIERLFSFPA AKPKEPTMVA PRARKEPKEI TFLDAKKSLN LNIFLKQFKC 650
    SNEEVAAMIR AGDTTKFDVE VLKQLLKLLP EKHEIENLRA FTEERAKLAS 700
    ADHFYLLLLA IPCYQLRIEC MLLCEGAAAV LDMVRPKAQL VLAACESLLT 750
    SRQLPIFCQL ILRIGNFLNY GSHTGDADGF KISTLLKLTE TKSQQNRVTL 800
    LHHVLEEAEK SHPDLLQLPR DLEQPSQAAG INLEIIRSEA SSNLKKLLET 850
    ERKVSASVAE VQEQYTERLQ ASISAFRALD ELFEAIEQKQ RELADYLCED 900
    AQQLSLEDTF STMKAFRDLF LRALKENKDR KEQAAKAERR KQQLAEEEAR 950
    RPRGEDGKPV RKGPGKQEEV CVIDALLADI RKGFQLRKTA RGRGDTDGGS 1000
    KAASMDPPRA TEPVATSNPA GDPVGSTRCP ASEPGLDATT ASESRGWDLV 1050
    DAVTPGPQPT LEQLEEGGPR PLERRSSWYV DASDVLTTED PQCPQPLEGA 1100
    WPVTLGDAQA LKPLKFSSNQ PPAAGSSRQD AKDPTSLLGV LQAEADSTSE 1150
    GLEDAVHSRG ARPPAAGPGG DEDEDEEDTA PESALDTSLD KSFSEDAVTD 1200
    SSGSGTLPRA RGRASKGTGK RRKKRPSRSQ EEVPPDSDDN KTKKLCVIQ 1249
    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.

    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.
    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.

    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 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.
    VAR_067594
    Natural varianti184 – 1841E → K in FSGS5. 1 Publication
    VAR_063077
    Natural varianti186 – 1861S → P in FSGS5. 1 Publication
    VAR_063078
    Natural varianti198 – 1981L → R in FSGS5. 1 Publication
    VAR_063079
    Natural varianti214 – 2141R → H in FSGS5. 1 Publication
    VAR_063080
    Natural varianti218 – 2181R → Q in FSGS5. 1 Publication
    VAR_063081
    Natural varianti218 – 2181R → W in FSGS5. 1 Publication
    VAR_063082
    Natural varianti220 – 2201E → K in FSGS5. 1 Publication
    VAR_063083
    Natural varianti245 – 2451L → P in FSGS5. 1 Publication
    VAR_068845
    Natural varianti1096 – 10961P → S.
    Corresponds to variant rs34251364 [ dbSNP | Ensembl ].
    VAR_037117
    Natural varianti1135 – 11351T → M.
    Corresponds to variant rs3803311 [ dbSNP | Ensembl ].
    VAR_037118

    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi166215588.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS41999.1. [Q27J81-3 ]
    CCDS45173.1. [Q27J81-2 ]
    CCDS9989.2. [Q27J81-1 ]
    RefSeqi NP_001026884.3. NM_001031714.3. [Q27J81-2 ]
    NP_071934.3. NM_022489.3. [Q27J81-1 ]
    NP_116103.1. NM_032714.2. [Q27J81-3 ]
    UniGenei Hs.24956.

    3D structure databases

    ProteinModelPortali Q27J81.
    SMRi Q27J81. Positions 53-324, 555-988.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122172. 7 interactions.
    IntActi Q27J81. 6 interactions.
    MINTi MINT-7034523.
    STRINGi 9606.ENSP00000376410.

    PTM databases

    PhosphoSitei Q27J81.

    Polymorphism databases

    DMDMi 166215588.

    Proteomic databases

    MaxQBi Q27J81.
    PaxDbi Q27J81.
    PRIDEi Q27J81.

    Protocols and materials databases

    DNASUi 64423.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330634 ; ENSP00000376406 ; ENSG00000203485 . [Q27J81-2 ]
    ENST00000392634 ; ENSP00000376410 ; ENSG00000203485 . [Q27J81-1 ]
    ENST00000398337 ; ENSP00000381380 ; ENSG00000203485 . [Q27J81-3 ]
    GeneIDi 64423.
    KEGGi hsa:64423.
    UCSCi uc001yoy.4. human. [Q27J81-3 ]
    uc001ypb.2. human. [Q27J81-1 ]
    uc001ypc.2. human. [Q27J81-2 ]

    Organism-specific databases

    CTDi 64423.
    GeneCardsi GC14P105155.
    HGNCi HGNC:23791. INF2.
    HPAi HPA000724.
    MIMi 610982. gene.
    613237. phenotype.
    614455. phenotype.
    neXtProti NX_Q27J81.
    Orphaneti 93114. Autosomal dominant intermediate Charcot-Marie-Tooth disease type E.
    93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
    PharmGKBi PA162392025.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG149898.
    HOVERGENi HBG081794.
    InParanoidi Q27J81.
    OMAi QPVDHAQ.
    OrthoDBi EOG7T4MN4.
    PhylomeDBi Q27J81.
    TreeFami TF326300.

    Miscellaneous databases

    ChiTaRSi INF2. human.
    GeneWikii INF2.
    GenomeRNAii 64423.
    NextBioi 66417.
    PMAP-CutDB Q27J81.
    PROi Q27J81.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q27J81.
    CleanExi HS_INF2.
    Genevestigatori Q27J81.

    Family and domain databases

    InterProi IPR016024. 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 ]
    PANTHERi PTHR23213:SF5. PTHR23213:SF5. 1 hit.
    Pfami PF06367. Drf_FH3. 1 hit.
    PF06371. Drf_GBD. 1 hit.
    PF02181. FH2. 1 hit.
    PF02205. WH2. 1 hit.
    [Graphical view ]
    SMARTi SM00498. FH2. 1 hit.
    SM00246. WH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    PS51082. WH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
    18. Cited for: VARIANTS CMTDIE ARG-104; PHE-104; TRP-104; PRO-128; ARG-132 AND 164-ALA--ASP-166 DEL.
    19. "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.

    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: October 1, 2014
    This is version 87 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