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

0 structures for Q6XD99

Entry ID Method Resolution Chain Position Source

No variants for Q6XD99

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6XD99

No associated diseases with Q6XD99

34 regional properties for Q6XD99

Type Name Position InterPro Accession
conserved_site Actinin-type actin-binding domain, conserved site 56 - 65 IPR001589-1
conserved_site Actinin-type actin-binding domain, conserved site 130 - 154 IPR001589-2
domain Pleckstrin homology domain, spectrin-type 2194 - 2213 IPR001605-1
domain Pleckstrin homology domain, spectrin-type 2214 - 2235 IPR001605-2
domain Pleckstrin homology domain, spectrin-type 2256 - 2273 IPR001605-3
domain Pleckstrin homology domain, spectrin-type 2276 - 2294 IPR001605-4
domain Calponin homology domain 54 - 158 IPR001715-1
domain Calponin homology domain 173 - 278 IPR001715-2
domain Pleckstrin homology domain 2191 - 2303 IPR001849
repeat Spectrin repeat 303 - 411 IPR002017-1
repeat Spectrin repeat 423 - 525 IPR002017-2
repeat Spectrin repeat 530 - 636 IPR002017-3
repeat Spectrin repeat 639 - 742 IPR002017-4
repeat Spectrin repeat 745 - 847 IPR002017-5
repeat Spectrin repeat 850 - 952 IPR002017-6
repeat Spectrin repeat 957 - 1060 IPR002017-7
repeat Spectrin repeat 1063 - 1166 IPR002017-8
repeat Spectrin repeat 1170 - 1259 IPR002017-9
repeat Spectrin repeat 1276 - 1376 IPR002017-10
repeat Spectrin repeat 1481 - 1585 IPR002017-11
repeat Spectrin repeat 1587 - 1691 IPR002017-12
repeat Spectrin repeat 1693 - 1796 IPR002017-13
repeat Spectrin repeat 1800 - 1902 IPR002017-14
repeat Spectrin repeat 1909 - 2009 IPR002017-15
repeat Spectrin repeat 2013 - 2092 IPR002017-16
repeat Spectrin/alpha-actinin 305 - 411 IPR018159-1
repeat Spectrin/alpha-actinin 425 - 525 IPR018159-2
repeat Spectrin/alpha-actinin 530 - 849 IPR018159-3
repeat Spectrin/alpha-actinin 851 - 1169 IPR018159-4
repeat Spectrin/alpha-actinin 1171 - 1587 IPR018159-5
repeat Spectrin/alpha-actinin 1588 - 1800 IPR018159-6
repeat Spectrin/alpha-actinin 1801 - 2022 IPR018159-7
repeat Spectrin/alpha-actinin 2015 - 2157 IPR018159-8
domain Pleckstrin homology domain 9 2195 - 2296 IPR041681

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

19 GO annotations of cellular component

Name Definition
actin cytoskeleton of dendritic spine The actin cytoskeleton that is part of a dendritic spine.
axolemma The portion of the plasma membrane surrounding an axon; it is a specialized trilaminar random mosaic of protein molecules floating within a fluid matrix of highly mobile phospholipid molecules, 7-8 nm in thickness.
cell junction A cellular component that forms a specialized region of connection between two or more cells, or between a cell and the extracellular matrix, or between two membrane-bound components of a cell, such as flagella.
cell projection A prolongation or process extending from a cell, e.g. a flagellum or axon.
cortical actin cytoskeleton The portion of the actin cytoskeleton, comprising filamentous actin and associated proteins, that lies just beneath the plasma membrane.
cortical cytoskeleton The portion of the cytoskeleton that lies just beneath the plasma membrane.
cuticular plate A dense network of actin filaments found beneath the apical cell surface of hair cells, and into which stereocilia are inserted.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
glutamatergic synapse A synapse that uses glutamate as a neurotransmitter.
M band The midline of aligned thick filaments in a sarcomere; location of specific proteins that link thick filaments. Depending on muscle type the M band consists of different numbers of M lines.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
postsynapse The part of a synapse that is part of the post-synaptic cell.
postsynaptic density An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
spectrin Membrane associated dimeric protein (240 and 220 kDa) of erythrocytes. Forms a complex with ankyrin, actin and probably other components of the membrane cytoskeleton, so that there is a mesh of proteins underlying the plasma membrane, potentially restricting the lateral mobility of integral proteins.

6 GO annotations of molecular function

Name Definition
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
ankyrin binding Binding to ankyrin, a 200 kDa cytoskeletal protein that attaches other cytoskeletal proteins to integral membrane proteins.
GTPase binding Binding to a GTPase, any enzyme that catalyzes the hydrolysis of GTP.
phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.
protein-containing complex binding Binding to a macromolecular complex.
structural constituent of cytoskeleton The action of a molecule that contributes to the structural integrity of a cytoskeletal structure.

14 GO annotations of biological process

Name Definition
actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
actin filament capping The binding of a protein or protein complex to the end of an actin filament, thus preventing the addition, exchange or removal of further actin subunits.
central nervous system development The process whose specific outcome is the progression of the central nervous system over time, from its formation to the mature structure. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain and spinal cord. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
central nervous system formation The process that gives rise to the central nervous system. This process pertains to the initial formation of a structure from unspecified parts. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain, spinal cord and spinal nerves. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
common-partner SMAD protein phosphorylation The process of introducing a phosphate group on to a common-partner SMAD protein. A common partner SMAD protein binds to pathway-restricted SMAD proteins forming a complex that translocates to the nucleus.
Golgi to plasma membrane protein transport The directed movement of proteins from the Golgi to the plasma membrane in transport vesicles that move from the trans-Golgi network to the plasma membrane.
membrane assembly The aggregation, arrangement and bonding together of a set of components to form a membrane.
mitotic cytokinesis A cell cycle process that results in the division of the cytoplasm of a cell after mitosis, resulting in the separation of the original cell into two daughter cells.
plasma membrane organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the plasma membrane.
positive regulation of interleukin-2 production Any process that activates or increases the frequency, rate, or extent of interleukin-2 production.
positive regulation of protein localization to plasma membrane Any process that activates or increases the frequency, rate or extent of protein localization to plasma membrane.
protein localization to plasma membrane A process in which a protein is transported to, or maintained in, a specific location in the plasma membrane.
regulation of protein localization to plasma membrane Any process that modulates the frequency, rate or extent of protein localization to plasma membrane.
regulation of SMAD protein signal transduction Any process that modulates the rate, frequency or extent of SMAD protein signal transduction. Pathway-restricted SMAD proteins and common-partner SMAD proteins are involved in the transforming growth factor beta receptor signaling pathways.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF
70 80 90 100 110 120
TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL
130 140 150 160 170 180
QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL
190 200 210 220 230 240
LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL
250 260 270 280 290 300
AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET
310 320 330 340 350 360
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG
370 380 390 400 410 420
NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL
430 440 450 460 470 480
EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA
490 500 510 520 530 540
VVAVARELEA ESYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI
550 560 570 580 590 600
MDWMDEMKVL LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ AERVRGVNAS AQKFATDGEG
610 620 630 640 650 660
YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI
670 680 690 700 710 720
LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERIS
730 740 750 760 770 780
YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSN DVGHDEYSTQ
790 800 810 820 830 840
SLVKKHKDVA EEISNYRPTI DTLHEQAGAL PQAHAESPDV KGRLAGIEER YKEVAELTRL
850 860 870 880 890 900
RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
910 920 930 940 950 960
QASRVAVVNQ IARQLMHSGH PSEKEIRAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY
970 980 990 1000 1010 1020
HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE
1030 1040 1050 1060 1070 1080
KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR
1090 1100 1110 1120 1130 1140
TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL
1150 1160 1170 1180 1190 1200
RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT
1210 1220 1230 1240 1250 1260
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN
1270 1280 1290 1300 1310 1320
REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM
1330 1340 1350 1360 1370 1380
AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN
1390 1400 1410 1420 1430 1440
KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTTSAQNKV LDGASVFLLM YSCPPRCWRI
1450 1460 1470 1480 1490 1500
RWKRGRAQMR VDSKRLTVQT KFMELLEPLN ERKHNLLASK EIHQFNRDVE DEILWVGERM
1510 1520 1530 1540 1550 1560
PLATSTDHGH NLQTVQLLIK KNQTLQKEIQ GHQPRIDDIF ERSQNIITDS SSLNAEAIRQ
1570 1580 1590 1600 1610 1620
RLADLKQLWG LLIEETEKRH RRLEEAHKAQ QYYFDAAEAE AWMSEQELYM MSEEKAKDEQ
1630 1640 1650 1660 1670 1680
SAVSMLKKHQ ILEQAVEDYA ETVHQLSKTS RALVADSHPE SERISMRQSK VDKLYAGLKD
1690 1700 1710 1720 1730 1740
LAEERRGKLD ERHRLFQLNR EVDDLEQWIA EREVVAGSHE LGQDYEHVTM LQERFREFAR
1750 1760 1770 1780 1790 1800
DTGNIGQERV DTVNHMADDL INSGHSDAAT IAEWKDGLNE AWADLLELID TRTQILAASY
1810 1820 1830 1840 1850 1860
ELHKFYHDAK EIFGRIQDKH KKLPEELGRD QNTVETLQRM HTTFEHDIQA LGTQVRQLQE
1870 1880 1890 1900 1910 1920
DAARLQAAYA GDKADDIQKR ENEVLEAWKS LLDACEGRRV RLVDTGDKFR FFSMVRDLML
1930 1940 1950 1960 1970 1980
WMEDVIRQIE AQEKPRDVSS VELLMNNHQG IKAEIDARND SFTACIELGK ALLARKHYAS
1990 2000 2010 2020 2030 2040
EEIKEKLLQL TEKRKEMIDK WEDRWEWLRL ILEVHQFSRD ASVAEAWLLG QEPYLSSREI
2050 2060 2070 2080 2090 2100
GQSVDEVEKL IKRHEAFEKS AATWDERFSA LERLTTLELL EVRRQQEEEE RKRRPPSPEP
2110 2120 2130 2140 2150 2160
SAKVSEEAES QQWDTSKGDQ VSQNGLPAEQ GSPRMAGTME TSEMVNGAAE QRTSSKESSP
2170 2180 2190 2200 2210 2220
VPSPTSDRKA KSALPAQSAA TLPARTLETP AAQMEGFLNR KHEWEAHNKK ASSRSWHNVY
2230 2240 2250 2260 2270 2280
CVINNQEMGF YKDAKSAASG VPYHSEVPVS LKEAICEVAL DYKKKKHVFK LRLSDGNEYL
2290 2300 2310 2320 2330 2340
FQAKDDDEMN TWIQAITSAI SSDKHDTSAS TQSTPASSRA QTLPTSVVTI TSESSPGKRE
2350
KDKEKDKEKR FSLFGKKK