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Details on Person UniProt:P26039 Tln1

Class:IdReferenceGeneProduct:103521
_chainChangeLogchain:1-2541 added on Sat February 7 2015
_displayNameUniProt:P26039 Tln1
_timestamp2024-11-03 19:43:52
chainchain:1-2541
checksum78832388E2392B8E
commentFUNCTION High molecular weight cytoskeletal protein concentrated at regions of cell-matrix and cell-cell contacts. Involved in connections of major cytoskeletal structures to the plasma membrane. With KANK1 co-organize the assembly of cortical microtubule stabilizing complexes (CMSCs) positioned to control microtubule-actin crosstalk at focal adhesions (FAs) rims.SUBUNIT Part of a complex composed of THSD1, PTK2/FAK1, TLN1 and VCL (By similarity). Interacts with THSD1; this promotes interaction with PTK2/FAK1 and VCL (By similarity). Interacts with NRAP and LAYN (By similarity). Interacts with SYNM (By similarity). Interacts with ITGB1; the interaction is prevented by competitive binding of ITGB1BP1 (By similarity). Binds with high affinity to VCL and with low affinity to integrins (PubMed:15272303, PubMed:15642262, PubMed:20610383, PubMed:23389036). Interacts with APBB1IP; this inhibits VCL binding (PubMed:23389036). Interacts with PTK2/FAK1 (PubMed:7622520). Interacts with PIP5K1C (PubMed:15623515). Interacts with F-actin (PubMed:20610383). Interacts with SVEP1 (PubMed:36792666). Interacts (via R7 domain) with KANK1 or KANK2 (via KN motif); this interaction likely initiates the assembly of cortical microtubule stabilization complexes (CMSCs) at the vicinity of focal adhesions.INTERACTION Colocalizes with LAYN at the membrane ruffles (By similarity). Localized preferentially in focal adhesions than fibrillar adhesions.DOMAIN Consists of an N-terminal FERM domain linked via a short unstructured region to a large flexible C-terminal rod which contains 13 amphipathic helical bundles (R1-R13). The rod begins with a five-helix bundle (R1) followed by three four-helix bundles (R2-R4). These are followed by a series of eight five-helix bundles (R5-R7 and R9-R13) in which the N- and C-termini are positioned at opposite ends of the bundle, creating a linear chain. The four-helix bundle R8 does not disrupt the chain because it is inserted into a loop in the R7 five-helix bundle. The uneven distribution of four- and five-helix bundles creates two distinctly different zones: a compact N-terminal region sensitive to stretch and a linear C-terminal region that is optimal for force transmission.
descriptionrecommendedName: Talin-1
geneNameTln1
Tln
identifierP26039
isSequenceChangedFALSE
keyword3D-structure
Acetylation
Cell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Phosphoprotein
Reference proteome
modified[InstanceEdit:143527] Schmidt, EE, 2004-11-12 07:45:10
[InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53
[InstanceEdit:354386] Schmidt, EE, 2008-06-18 04:45:12
[InstanceEdit:384350] Kanapin, AA, 2008-11-26 14:00:39
[InstanceEdit:392885] Kanapin, AA, 2009-03-09 12:07:18
[InstanceEdit:400710] Schmidt, EE, 2009-03-25 05:33:35
[InstanceEdit:423310] Kanapin, AA
[InstanceEdit:435478] Kanapin, AA
[InstanceEdit:435871] Kanapin, AA
[InstanceEdit:447347] Kanapin, AA
[InstanceEdit:525883] Kanapin, AA
[InstanceEdit:613449] Kanapin, AA
[InstanceEdit:797602] Kanapin, AA
[InstanceEdit:937368] Yung, CK
[InstanceEdit:1042053] Yung, CK
[InstanceEdit:1220657] Yung, CK
[InstanceEdit:1300696] Yung, CK
[InstanceEdit:1301627] Yung, CK
[InstanceEdit:1551960] Weiser, JD
[InstanceEdit:1995863] Weiser, JD
[InstanceEdit:2132304] Weiser, JD
[InstanceEdit:2265580] Weiser, JD
[InstanceEdit:3445779] Weiser, JD
[InstanceEdit:4341137] Weiser, JD
[InstanceEdit:5433710] Weiser, JD
[InstanceEdit:5618415] Weiser, JD
[InstanceEdit:5634237] Weiser, JD
[InstanceEdit:5673015] Weiser, JD
[InstanceEdit:9027688] Weiser, JD
[InstanceEdit:9037114] Weiser, JD
[InstanceEdit:9637257] Weiser, JD
[InstanceEdit:9676415] Weiser, JD
[InstanceEdit:9706439] Weiser, JD
[InstanceEdit:9715482] Weiser, JD
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
[InstanceEdit:9862192] Weiser, Joel, 2024-02-26
[InstanceEdit:9917590] Weiser, Joel, 2024-08-09
[InstanceEdit:9926675] Weiser, Joel, 2024-11-03
nameTln1
referenceDatabase[ReferenceDatabase:2] UniProt
secondaryIdentifierTLN1_MOUSE
A2AIM8
Q8VEF0
sequenceLength2541
species[Species:48892] Mus musculus
(referenceEntity)[EntityWithAccessionedSequence:9855035] Tln1 [cytosol] [Mus musculus]
[EntityWithAccessionedSequence:9855103] Tln1(1-432) [cytosol] [Mus musculus]
[EntityWithAccessionedSequence:9855172] Tln1(433-2541) [cytosol] [Mus musculus]
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No pathways have been reviewed or authored by UniProt:P26039 Tln1 (103521)