O13818

PR
Gene name
SPAC19A8.02
Protein name
Uncharacterized PH domain-containing protein C19A8.02
Names
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPAC19A8.02
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

363-500 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for O13818

Entry ID Method Resolution Chain Position Source
AF-O13818-F1 Predicted AlphaFoldDB

13 variants for O13818

Variant ID(s) Position Change Description Diseaes Association Provenance
I_2488780_C_A 53 C>F No Jeffares_SNPs
I_2487671_T_A 423 N>Y No Jeffares_SNPs
I_2487629_G_A 437 R>C No Jeffares_SNPs
I_2487607_C_T 444 G>E No Jeffares_SNPs
I_2487017_C_T 641 A>T No Jeffares_SNPs
I_2486875_C_T 688 S>N No Jeffares_SNPs
I_2486830_A_G 703 V>A No Jeffares_SNPs
I_2486408_C_T 844 E>K No Jeffares_SNPs
I_2486284_T_C 885 K>R No Jeffares_SNPs
I_2486146_T_C 931 K>R No Jeffares_SNPs
I_2486108_T_C 944 T>A No Jeffares_SNPs
I_2485766_C_G 1058 V>L No Jeffares_SNPs
I_2485460_C_T 1127 R>K No Jeffares_SNPs

No associated diseases with O13818

2 regional properties for O13818

Type Name Position InterPro Accession
domain Kazal domain 450 - 507 IPR002350
domain Major facilitator superfamily domain 30 - 646 IPR020846

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Nucleus membrane ; Multi-pass membrane protein
  • Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cortical endoplasmic reticulum A cortical network of highly dynamic tubules that are juxtaposed to the plasma membrane and undergo ring closure and tubule-branching movements.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
nuclear membrane Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
spindle pole body The microtubule organizing center in fungi; functionally homologous to the animal cell centrosome.

1 GO annotations of molecular function

Name Definition
lipid binding Binding to a lipid.

1 GO annotations of biological process

Name Definition
endoplasmic reticulum-plasma membrane tethering The attachment of an endoplasmic reticulum membrane to the plasma membrane via molecular tethers.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAAPANASSK KDHVIPVLLN ECSIDSPSFR ASMYYLGNQI KAFNEWSHDF LCCCNKFIES
70 80 90 100 110 120
IMAIEPIVAS MSLNAMPSNV ASGFFDPDYA TTALLHGQDL FRSSYMVQLQ QAKNLRKFIV
130 140 150 160 170 180
APLDLFRDSK VKPLLQLNDR FKAEQAKYDA EVLRYSSLGH SKDLSQMRDE AKSLYEARKS
190 200 210 220 230 240
YFTVALQYVV RVTSFRSSID FIVIESICKF SIETFRLTDR LHESNRHIND QLIRLLSYET
250 260 270 280 290 300
KLKESYPSLK RIVSNVFDRI EKEILKRVQP PTNLDAYRFD PQQICQTNAT KRQGWLLRNI
310 320 330 340 350 360
SSSKADNKAI WRKYWFFVDN GYVGYLINDA NGGVFESEKI GVLLCKFSVL PSNHRKFCFQ
370 380 390 400 410 420
IKTKSVSYIL QAETHMEMLE WGSVINNARE HCINSGISAN RILSPTLPSF SAKATSIINP
430 440 450 460 470 480
QVNGRSNSTG KIGKNYRPRR TYSGRLLCGP NNYEVSTIMR SPTISTVPPP KYLSNSINGA
490 500 510 520 530 540
KFLNPLAPWT LVNAPLITNL THETITSLLD QEAFFHGNSP CALLANFWGS VNYGHVLERQ
550 560 570 580 590 600
NVYIEDLSNP SYKRLAREIH IEKLPSELKL RNAEFRGIFG ESEASTVLFV CRVCSKREDQ
610 620 630 640 650 660
IRMPGRMYCT MKGIYIYYNI NGLVLIEHFP ISSILNVKQF ASTKCDYFYM NIQNIGTVRF
670 680 690 700 710 720
RLYLDSSKAL TDRLNVLLCN YIADKPNSSI QLLSCIKRLN DDVKRFERGG DDNALKSYGV
730 740 750 760 770 780
QPSQEDLLIR RGRSSRALTN LINKNESNDS FMEDLRDFKI AMLPKETVQV VRSHHLDDIV
790 800 810 820 830 840
FDRVYNVSTK ALFHIVFGDR STVLSGAYNL HGVDDVEFLP WGKDPKTNLS RRYINYKVYN
850 860 870 880 890 900
YDQEGQCQSY HYEDCQIMDV RNDYHLYIMT WLHHSWTLPY RDYFKIVTKT SISHLRREKS
910 920 930 940 950 960
RLLISVGLEW IVKPFAISKV IEAECRKLAI KYIKTEVNFL EKATRRARNQ PLIAIINQYG
970 980 990 1000 1010 1020
RVGDYNESMV YRRKIPFNCE LKNLSIIDII RNNWWLFLQG LAIDLLKLPW AVFHIFLRYL
1030 1040 1050 1060 1070 1080
FSHSFLVIIF ACSVILNLSL MFCFGAKYWD ERQNNKFVGQ VFDEFKNIET SARYVYMKDV
1090 1100 1110 1120 1130 1140
DDLLVGLPTY LHPNVTYPSE CLQSFALKSS PQKSHWLRKR NYIAEKRKKI LENLASLNYY
1150 1160 1170 1180 1190 1200
EYIIHEDAVY QYIQQELLGC DKAREFDLYP PSMQRYCDSC TQDWRNRTLF FGKDTLATRL
1210
LTLETVENAD YAA