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 Q08EC4

Entry ID Method Resolution Chain Position Source
AF-Q08EC4-F1 Predicted AlphaFoldDB

67 variants for Q08EC4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs27615088 4 T>I No EVA
rs248248899 5 S>N No EVA
rs3388614811 13 T>S No EVA
rs3388617906 24 A>V No EVA
rs3388612818 40 I>V No EVA
rs3388605110 91 L>I No EVA
rs224420857 92 T>A No EVA
rs33722333 96 A>E No EVA
rs33722333 96 A>V No EVA
rs3388614837 108 P>S No EVA
rs226664150 124 S>P No EVA
rs3388607098 150 F>L No EVA
rs3388607083 164 A>S No EVA
rs3388607083 164 A>T No EVA
rs3388619285 179 Q>E No EVA
rs27614974 191 K>Q No EVA
rs3388615873 204 A>G No EVA
rs27614973 206 L>R No EVA
rs3388614813 215 D>E No EVA
rs3388618715 244 D>G No EVA
rs256751392 255 R>K No EVA
rs3388613233 262 F>V No EVA
rs3388617038 262 F>Y No EVA
rs3388615912 287 Q>H No EVA
rs27614962 291 T>I No EVA
rs3388618658 292 V>M No EVA
rs3388614855 301 E>K No EVA
rs3388619224 322 K>T No EVA
rs3388618655 323 V>A No EVA
rs1133984175 350 G>S No EVA
rs243087656 354 N>D No EVA
rs3388614981 364 L>Q No EVA
rs3388617005 373 R>* No EVA
rs3388600517 378 N>I No EVA
rs3388609865 379 S>F No EVA
rs3388600463 384 G>R No EVA
rs3388617882 394 D>G No EVA
rs3388611671 408 V>M No EVA
rs1134772445 428 V>I No EVA
rs3388607099 432 W>* No EVA
rs27614960 444 S>T No EVA
rs27614959 463 T>S No EVA
rs3388614784 476 R>* No EVA
rs3388612842 479 R>M No EVA
rs259148918 482 D>H No EVA
rs864266671 482 D>V No EVA
rs229376617 529 L>V No EVA
rs27614958 534 S>N No EVA
rs3388607087 536 D>V No EVA
rs258159462 537 R>H No EVA
rs3388611634 570 D>N No EVA
rs3388613284 586 F>L No EVA
rs27614956 589 N>S No EVA
rs3388618686 596 D>N No EVA
rs235627573 603 I>T No EVA
rs236139535 623 P>L No EVA
rs252614435 630 E>K No EVA
rs27614953 633 R>K No EVA
rs3388615861 635 N>S No EVA
rs3388613760 647 L>Q No EVA
rs264944577 654 T>P No EVA
rs256509694 679 S>T No EVA
rs3388615053 712 S>I No EVA
rs3388611592 787 S>L No EVA
rs1134436378 795 H>Y No EVA
rs3388615021 797 R>W No EVA
rs3388615859 801 D>V No EVA

No associated diseases with Q08EC4

4 regional properties for Q08EC4

Type Name Position InterPro Accession
domain SH3 domain 11 - 73 IPR001452
domain Serine rich protein interaction domain 433 - 589 IPR014928
domain CAS family, C-terminal 607 - 803 IPR021901
domain Cas scaffolding protein family member 4, SH3 domain 14 - 70 IPR035744

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton
  • Cell junction, focal adhesion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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).

1 GO annotations of molecular function

Name Definition
protein tyrosine kinase binding Binding to protein tyrosine kinase.

8 GO annotations of biological process

Name Definition
actin filament reorganization A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of actin filaments.
cell adhesion The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules.
cell migration The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms.
positive regulation of cell migration Any process that activates or increases the frequency, rate or extent of cell migration.
positive regulation of protein kinase B signaling Any process that activates or increases the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
positive regulation of protein tyrosine kinase activity Any process that increases the rate, frequency, or extent of protein tyrosine kinase activity.
positive regulation of substrate adhesion-dependent cell spreading Any process that activates or increases the frequency, rate or extent of substrate adhesion-dependent cell spreading.
transmembrane receptor protein tyrosine kinase signaling pathway The series of molecular signals initiated by an extracellular ligand binding to a receptor on the surface of the target cell where the receptor possesses tyrosine kinase activity, and ending with the regulation of a downstream cellular process, e.g. transcription.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9NQ75 CASS4 Cas scaffolding protein family member 4 Homo sapiens (Human) PR
10 20 30 40 50 60
MRGTSIREGA PKTLLARALY DNHADCSDEL AFSRGDILTI VEQNVPESEG WWRCLLHGRQ
70 80 90 100 110 120
GLAPANRLQV LRETPADRPC PLLPRGPDTD LTSSGAPYQV QDLISPPPQG PVYEPMRSWV
130 140 150 160 170 180
EGPSPATAQV YELPESPSSA RIICEKTLSF PKQALSVLPR PTRASLPTLP SQVYDVPVQR
190 200 210 220 230 240
QGFSTLERLE KQQFYDIPTS SQKALLHSST SQGRDVTLAP TMAFRQGGGY NPLSSPQKSE
250 260 270 280 290 300
RIHDTPVLLE KADVRNVSMT SFTKDSGSRA IPGSSAVHTG AVALSPQLGN TVQRKNSLPE
310 320 330 340 350 360
EPTYAFPTSR DPLPSDAGGS YKVPSRFLIP RVEQQNTMPN IYDTPKAMQG VSHNAPKAMQ
370 380 390 400 410 420
GVSLAGKELE RGREAPENSP WISGQTSFLS PDSDRLSVAS SDSRASVVSS CSSISMDSSS
430 440 450 460 470 480
GSSSEDSVKE LWMDVDFAKE TAVSLQHKVA SSAAGLLLFV SRTWRFKDSL ETNIHRIRRA
490 500 510 520 530 540
ADHVEESVRE FLDFAQGVGG TACNLTDSYL QARIRDQLQT ISSSYQTLLD AKGSLDRCNW
550 560 570 580 590 600
SLEVLVTDKV QNSLDDLERF VATARIVPED VKRFTSIVIA NGKLLFKQNC EKGEMDLKCE
610 620 630 640 650 660
RCIRPPQRET ESYQESSPFD RQPTTEHSFE LARKNRVNVC WQQSPNLQEK GKPTMEGKSN
670 680 690 700 710 720
RNPDFHGMSP PPLTSPSPSG QNTERKIHLS KHSRLYFGAL FKAISVFASS LSNGQPPEVF
730 740 750 760 770 780
ITQSKLVITV GQKLVDTLCS ETQEKDERNE ILCGSSHLCG LLKDLALATK SAVIQYPSPS
790 800
ALSLLQSEVE RLEHHSRKFR DTLE