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 Q5AH02

Entry ID Method Resolution Chain Position Source
AF-Q5AH02-F1 Predicted AlphaFoldDB

No variants for Q5AH02

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5AH02

No associated diseases with Q5AH02

3 regional properties for Q5AH02

Type Name Position InterPro Accession
domain RasGAP protein, C-terminal 1413 - 1563 IPR000593
domain Calponin homology domain 184 - 291 IPR001715
domain Ras GTPase-activating domain 978 - 1193 IPR001936

Functions

Description
EC Number
Subcellular Localization
  • Bud neck
  • Forms a ring at the bud neck in a MLC1-dependent manner, which contracts at the end of cytokinesis
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cellular bud neck The constriction between the mother cell and daughter cell (bud) in an organism that reproduces by budding.
mitotic actomyosin contractile ring A cytoskeletal structure composed of actin filaments, myosin, and myosin-associated proteins that forms beneath the plasma membrane of many cells, including animal cells and yeast cells, in a plane perpendicular to the axis of the mitotic spindle, i.e. the cell division plane. Ring contraction is associated with centripetal growth of the membrane that divides the cytoplasm of the two future daughter cells. In animal cells, the mitotic contractile ring is located inside the plasma membrane at the location of the cleavage furrow. In budding fungal cells, e.g. mitotic S. cerevisiae cells, the mitotic contractile ring forms beneath the plasma membrane at the mother-bud neck before mitosis.

3 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.
calmodulin binding Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.
GTPase activator activity Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.

4 GO annotations of biological process

Name Definition
mitotic actomyosin contractile ring assembly actin filament organization Any actin filament organization that is involved in mitotic actomyosin contractile ring assembly.
regulation of actin cytoskeleton organization Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
regulation of GTPase activity Any process that modulates the rate of GTP hydrolysis by a GTPase.
signal transduction The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAIGNIAARY LSSLEETDTT ATTTTTTTSN VLQPSNRLNS PTKFNRKSLD NNSQDLDALA
70 80 90 100 110 120
RALNITPSKP ETPTSISKGS ATSLLRTKFE SPSATVSSFK STSSSNGVSP TKKNHFVEIT
130 140 150 160 170 180
SDETPSWANK NYKDILNKSP TKFNTQSNVH TPLKQLNQPI GTPSSSSLSP AKNASKSSPG
190 200 210 220 230 240
YEYLCRIEAI KQWLESVLQE QITQSASQLI SYIRNGIHLA KLANVVLPTS KPVFLNDSKL
250 260 270 280 290 300
QFKHTENINR FFQLLDFFNM PDLFRFELTD LYDAKNVPKV WFCLHALSYI LHKQDPSYPA
310 320 330 340 350 360
MNNLVGKVDF SADDIRTANR ALVNSPLPNF SSADTGEGKS DTSNNNSSTT SATAAFMDKV
370 380 390 400 410 420
TSPVKKTPSP LKRPQQLQKK QLELVEDNKP ELTQDSSGLS KISRDDPFTD RVDLAPPSTS
430 440 450 460 470 480
NAKLELHTPP SKSLEFKIKS PIIDLSHRDS DYYTPELESH LPNIIKFQSL ARGAVFRYLM
490 500 510 520 530 540
FVDRILLKSY QDEFTNLFAI IRGNKARRKT VHKHRDELRL YSFEIIELQS IIRKNFVINK
550 560 570 580 590 600
KPNFTSITND VETVELQSLI RGKLTRDWKK YVTNGLEKFT PQIIDFQSLV RMKSIYSKSN
610 620 630 640 650 660
KVISYKDEIL PSLIELQSIA RSQLYHRFSR SNAIDETEII KIQSIIRRNA VIEDLYTKLS
670 680 690 700 710 720
KVRSNKRRLI ELQSIARGGV ARTKLCNSVL VTLIYEDGIL NQLFAKIRGD NYRKKFNSQK
730 740 750 760 770 780
SELLKYEKSS IIPVQTLFRG VLSRYTKEVT LSDIFDQIDS VITLQSVARG KLMRGSIYEF
790 800 810 820 830 840
SDYYQKHIKQ VVKAQAILQR VFAQNAYKQL ITSKNPPLKV IRRFAPLLSN NDRDFQDEMT
850 860 870 880 890 900
LSDLKDLIIE KCKANEEYEN QIEQLDMKLG LLDKNKISIE EFLKPTKGKT FKPIVENVKN
910 920 930 940 950 960
LERLNKSLKK KIELWQTLFY FIQTNPIYLT KLFNSIPYTK NQTKSGQDLF QSVIQLFPVR
970 980 990 1000 1010 1020
DSSITYHSRE EYFLVKLMIQ LMQNDTANSN NLGDITKLHL TNWIDFFTNF NNHTFQRQHL
1030 1040 1050 1060 1070 1080
KALLGKFVIR IVDNEQVDFE SDPIRIYNQI IDHEMKVYGR SEKSRDISPQ AAIQLPEVSN
1090 1100 1110 1120 1130 1140
KFVGNLMSLR ETCSDLLSML QKNASGNKAL LQIPDHVKLI CRQGYLCAQR KFPDKSDQQH
1150 1160 1170 1180 1190 1200
LAVAGVIFVK HYLGSILQVP ENYGILTGNN DTQKAKSKDN LRYLYRVMLQ LFSMKPFNDN
1210 1220 1230 1240 1250 1260
FLKPLNEYIM ASTDTVKSII SQAIINVGEI ETVYELHDYD DLVTHQRPKL TISVNSLIQL
1270 1280 1290 1300 1310 1320
EKSILQNVDI ITTGNDDQLY KTCVEVEKLL ISPQDMLTLT DLSSVTLNLN PTTQEESIVD
1330 1340 1350 1360 1370 1380
SKTKTLFTQA KRCLLYIIRV QEEDDSDDLL ELLISGIKPS HEQRFKEIVQ YEKAEQDISL
1390 1400 1410 1420 1430 1440
NNSKSVTANT VNKKKSTRPY SGTSLGDLSN LTYHELKKMC LEIILKLESM GELTRKNSFQ
1450 1460 1470 1480 1490 1500
TLLNQIAMDI KTKDSQRQCR WQQLQVSQKT IKKLSEKENY LKTQLHNYKK HVESVLLELQ
1510 1520 1530 1540 1550 1560
SKSKSNDKNW KRRLFNIMVI PVFSKQYFYH RELRKHNRLP KFGSYKYSAK KLIDQKVLID
1570 1580 1590 1600 1610 1620
FSTANNVATA SKLDFMFSCH QVGKFTIEVA SGTVNIPGAT NTITLDELLA LQYENKTKFE
1630 1640
LFDGMATFDS NNFMGLIFRK FYDLKKE