Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q2TCH4

Entry ID Method Resolution Chain Position Source
AF-Q2TCH4-F1 Predicted AlphaFoldDB

No variants for Q2TCH4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2TCH4

No associated diseases with Q2TCH4

5 regional properties for Q2TCH4

Type Name Position InterPro Accession
domain Zinc finger, LIM-type 271 - 330 IPR001781-1
domain Zinc finger, LIM-type 331 - 388 IPR001781-2
domain Zinc finger, LIM-type 389 - 448 IPR001781-3
domain Zinc finger, LIM-type 449 - 506 IPR001781-4
domain Paxillin/TGFB1I1, LIM domain 1 273 - 325 IPR047075

Functions

Description
EC Number
Subcellular Localization
  • Cell junction, focal adhesion
  • Nucleus matrix
  • Cytoplasm, cytoskeleton
  • Associated with the actin cytoskeleton; colocalizes with stress fibers
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
focal adhesion A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).
nuclear matrix The dense fibrillar network lying on the inner side of the nuclear membrane.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
transcription coactivator activity A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator.

2 GO annotations of biological process

Name Definition
cell differentiation The process in which relatively unspecialized cells, e.g. embryonic or regenerative cells, acquire specialized structural and/or functional features that characterize the cells, tissues, or organs of the mature organism or some other relatively stable phase of the organism's life history. Differentiation includes the processes involved in commitment of a cell to a specific fate and its subsequent development to the mature state.
Wnt signaling pathway The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell and ending with a change in cell state.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEDLDALLAD LQITTPPRCP VLLTDSPEKP QPTETRPPPP PYDPKTAMSN KTSDHETFPV
70 80 90 100 110 120
DKDHLYSTVQ KYPLPSVSPA LGGGLCELDR LLNELNATQF NITDEIMSQF PTRDPSEQKA
130 140 150 160 170 180
EAQKEAEKRA LSASSATLEL DRLMASLSDF HKQNTVSQEV EAPGAYKGSE EVSRPGDTED
190 200 210 220 230 240
LSSPRSTACV PKDLEDAPTP KSFKVVSAPG HLEVKTNQVN SDEVTASRVP DSVSGSKVPE
250 260 270 280 290 300
ATSVPRSDLD SMLVKLQSGL KQQGIETYSK GLCESCQRPI AGQVVTALGH TWHPEHFVCA
310 320 330 340 350 360
HCHTLIGTSN FFEKDGRPYC EKDYFMLYAP RCALCELPIV QNMVTALGCT WHPEHFCCKV
370 380 390 400 410 420
CKKPIGEEGF HEKDGEQYCS DDYFRLFGAV CAGCTEAVKE SYISALGGLW HPQCFVCHVC
430 440 450 460 470 480
HTPFINGSFF EHEGLPLCET HYHSRRGSLC AGCEQPITGR CVTAMGKKFH PQHLNCTFCL
490 500
RQLNKGTFRE HDEKPYCQAC YARLYG