Details for: FERMT2
Associated with
Other Information
Genular Protein ID: 3632927190
Symbol: FERM2_HUMAN
Name: Fermitin family homolog 2
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 8175911
Title: Identification of serum-inducible genes: different patterns of gene regulation during G0->S and G1->S progression.
PubMed ID: 8175911
PubMed ID: 12697302
Title: URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas.
PubMed ID: 12697302
PubMed ID: 12679033
Title: Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation.
PubMed ID: 12679033
PubMed ID: 12508121
Title: The DNA sequence and analysis of human chromosome 14.
PubMed ID: 12508121
DOI: 10.1038/nature01348
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 18458155
Title: Kindlin-2 (Mig-2): a co-activator of beta3 integrins.
PubMed ID: 18458155
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21768292
Title: Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition.
PubMed ID: 21768292
PubMed ID: 21325030
Title: Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins.
PubMed ID: 21325030
DOI: 10.1242/jcs.076976
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22699938
Title: Kindlin 2 forms a transcriptional complex with beta-catenin and TCF4 to enhance Wnt signalling.
PubMed ID: 22699938
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 22030399
Title: Structural basis of phosphoinositide binding to kindlin-2 protein pleckstrin homology domain in regulating integrin activation.
PubMed ID: 22030399
PubMed ID: 22078565
Title: Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation.
PubMed ID: 22078565
PubMed ID: 22653426
Title: Crystal structure of kindlin-2 PH domain reveals a conformational transition for its membrane anchoring and regulation of integrin activation.
PubMed ID: 22653426
Sequence Information:
- Length: 680
- Mass: 77861
- Checksum: BAFF5AF2CD91C43C
- Sequence:
MALDGIRMPD GCYADGTWEL SVHVTDLNRD VTLRVTGEVH IGGVMLKLVE KLDVKKDWSD HALWWEKKRT WLLKTHWTLD KYGIQADAKL QFTPQHKLLR LQLPNMKYVK VKVNFSDRVF KAVSDICKTF NIRHPEELSL LKKPRDPTKK KKKKLDDQSE DEALELEGPL ITPGSGSIYS SPGLYSKTMT PTYDAHDGSP LSPTSAWFGD SALSEGNPGI LAVSQPITSP EILAKMFKPQ ALLDKAKINQ GWLDSSRSLM EQDVKENEAL LLRFKYYSFF DLNPKYDAIR INQLYEQAKW AILLEEIECT EEEMMMFAAL QYHINKLSIM TSENHLNNSD KEVDEVDAAL SDLEITLEGG KTSTILGDIT SIPELADYIK VFKPKKLTLK GYKQYWCTFK DTSISCYKSK EESSGTPAHQ MNLRGCEVTP DVNISGQKFN IKLLIPVAEG MNEIWLRCDN EKQYAHWMAA CRLASKGKTM ADSSYNLEVQ NILSFLKMQH LNPDPQLIPE QITTDITPEC LVSPRYLKKY KNKQITARIL EAHQNVAQMS LIEAKMRFIQ AWQSLPEFGI THFIARFQGG KKEELIGIAY NRLIRMDAST GDAIKTWRFS NMKQWNVNWE IKMVTVEFAD EVRLSFICTE VDCKVVHEFI GGYIFLSTRA KDQNESLDEE MFYKLTSGWV
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.