ID A0A0A0MQU1_HUMAN Unreviewed; 717 AA.
AC A0A0A0MQU1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Inverted formin 2 {ECO:0000313|Ensembl:ENSP00000252527.8};
DE Flags: Fragment;
GN Name=INF2 {ECO:0000313|Ensembl:ENSP00000252527.8};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000252527.8, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000252527.8, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2] {ECO:0007829|PubMed:17081983}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [3] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [4] {ECO:0007829|PubMed:18318008}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [5] {ECO:0007829|PubMed:19690332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [6] {ECO:0007829|PubMed:20068231}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8] {ECO:0007829|PubMed:21406692}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11] {ECO:0000313|Ensembl:ENSP00000252527.8}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AL583722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0A0MQU1; -.
DR SMR; A0A0A0MQU1; -.
DR MassIVE; A0A0A0MQU1; -.
DR PeptideAtlas; A0A0A0MQU1; -.
DR Ensembl; ENST00000252527.8; ENSP00000252527.8; ENSG00000203485.14.
DR UCSC; uc059fwk.1; human.
DR HGNC; HGNC:23791; INF2.
DR VEuPathDB; HostDB:ENSG00000203485; -.
DR GeneTree; ENSGT00940000155691; -.
DR HOGENOM; CLU_023293_0_0_1; -.
DR ChiTaRS; INF2; human.
DR Proteomes; UP000005640; Chromosome 14.
DR Bgee; ENSG00000203485; Expressed in sural nerve and 175 other cell types or tissues.
DR ExpressionAtlas; A0A0A0MQU1; baseline and differential.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR CDD; cd22061; WH2_INF2; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR027649; Inf2.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR46345; INVERTED FORMIN-2; 1.
DR PANTHER; PTHR46345:SF5; INVERTED FORMIN-2; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:A0A0A0MQU1,
KW ECO:0007829|MaxQB:A0A0A0MQU1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 22..414
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 442..457
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 396..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSP00000252527.8"
SQ SEQUENCE 717 AA; 78826 MW; 318C8E367F43E2CD CRC64;
GMEEVIVAQV DHGLGSAWVP SHRRVNPPTL RMKKLNWQKL PSNVAREHNS MWASLSSPDA
EAVEPDFSSI ERLFSFPAAK PKEPTMVAPR ARKEPKEITF LDAKKSLNLN IFLKQFKCSN
EEVAAMIRAG DTTKFDVEVL KQLLKLLPEK HEIENLRAFT EERAKLASAD HFYLLLLAIP
CYQLRIECML LCEGAAAVLD MVRPKAQLVL AACESLLTSR QLPIFCQLIL RIGNFLNYGS
HTGDADGFKI STLLKLTETK SQQNRVTLLH HVLEEAEKSH PDLLQLPRDL EQPSQAAGIN
LEIIRSEASS NLKKLLETER KVSASVAEVQ EQYTERLQAS ISAFRALDEL FEAIEQKQRE
LADYLCEDAQ QLSLEDTFST MKAFRDLFLR ALKENKDRKE QAAKAERRKQ QLAEEEARRP
RGEDGKPVRK GPGKQEEVCV IDALLADIRK GFQLRKTARG RGDTDGGSKA ASMDPPRATE
PVATSNPAGD PVGSTRCPAS EPGLDATTAS ESRGWDLVDA VTPGPQPTLE QLEEGGPRPL
ERRSSWYVDA SDVLTTEDPQ CPQPLEGAWP VTLGDAQALK PLKFSSNQPP AAGSSRQDAK
DPTSLLGVLQ AEADSTSEGL EDAVHSRGAR PPAAGPGGDE DEDEEDTAPE SALDTSLDKS
FSEDAVTDSS GSGTLPRARG RASKGTGKRR KKRPSRSQEE VPPDSDDNKT KKLCVIQ
//
