wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor MYB93 (Myb-related protein 93) (AtMYB93) (Q9S9Z2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that acts as negative regulator of lateral root (LR) development. Required for normal auxin responses during LR development. May be part of a negative feedback loop stimulated specifically in the endodermis upon LR initiation to ensure that LRs are formed only in the correct place.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:24902892}. Cytoplasm {ECO:0000269|PubMed:24902892}.
Interaction partners:
- ARABIDILLO protein
- Cytochrome P450 86B1
- Glycerol-3-phosphate acyltransferase 5
- 3-ketoacyl-CoA synthase 20
- Cytochrome P450 86A1
Sequence:
MGRSPCCDENGLKKGPWTPEEDQKLIDYIHKHGHGSWRALPKLADLNRCGKSCRLRWTNYLRPDIKRGKFSAEEEQTILHLHSILGNKWSAIATHLQGRTDNEIKNFWNTHLKKKLIQMGIDPVTHQPRTDLFASLPQLIALANLKDLIEQTSQFSSMQGEAAQLANLQYLQRMFNSSASLTNNNGNNFSPSSILDIDQHHAMNLLNSMVSWNKDQNPAFDPVLELEANDQNQDLFPLGFIIDQPTQPLQQQKYHLNNSPSELPSQGDPLLDHVPFSLQTPLNSEDHFIDNLVKHPTDHEHEHDDNPSSWVLPSLIDNNPKTVTSSLPHNNPADASSSSSYGGCEAASFYWPDICFDESLMNVIS
Protein: NADH:quinone reductase (EC 1.6.5.9) (Q9I4V0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the NADH-dependent reduction of a broad spectrum of quinone substrates, generating the corresponding hydroquinones. Highly prefers NADH to NADPH as a reducing substrate. Also displays a small NADH oxidase activity. Does not exhibit nitronate monooxygenase activity; is inactive against propionate 3-nitronate, 3-nitropropionate, nitroethane, 1-nitropropane, 2-nitropropane, and the anionic forms ethylnitronate, propyl-1-nitronate, and propyl-2-nitronate. Has no azoreductase activity since it is not able to reduce the azo dye methyl red with NADH. May be required to maintain an appropriate [NAD(+)]/[NADH] ratio for the catabolism of fatty acids in P.aeruginosa PAO1.
Interaction partners:
- Probable acyl-CoA dehydrogenase
- Probable short-chain dehydrogenase
- Probable enoyl-CoA hydratase/isomerase
- Probable acyl-CoA dehydrogenase
- Probable major facilitator superfamily
- 3-alpha,7-alpha, 12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
- Thiolase C-terminal domain-containing protein
- Pimeloyl-CoA synthetase
Sequence:
MGVFRTRFTETFGVEHPIMQGGMQWVGRAEMAAAVANAGGLATLSALTQPSPEALAAEIARCRELTDRPFGVNLTLLPTQKPVPYAEYRAAIIEAGIRVVETAGNDPGEHIAEFRRHGVKVIHKCTAVRHALKAERLGVDAVSIDGFECAGHPGEDDIPGLVLLPAAANRLRVPIIASGGFADGRGLVAALALGADAINMGTRFLATRECPIHPAVKAAIRAADERSTDLIMRSLRNTARVARNAISQEVLAIEARGGAGYADIAALVSGQRGRQVYQQGDTDLGIWSAGMVQGLIDDEPACAELLRDIVEQARQLVRQRLEGMLAGV
Protein: Receptor expression-enhancing protein 6 (Polyposis locus protein 1-like 1) (Q96HR9)
Organism: Homo sapiens (Human)
Function: Required for correct function and survival of retinal photoreceptors. Required for retinal development (By similarity). In rod photoreceptors, facilitates stability and/or trafficking of guanylate cyclases and is required to maintain endoplasmic reticulum and mitochondrial homeostasis (By similarity). May play a role in clathrin-coated intracellular vesicle trafficking of proteins from the endoplasmic reticulum to the retinal rod plasma membrane (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24098485, ECO:0000269|PubMed:27889058}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q9JM62}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Receptor expression-enhancing protein 5
Sequence:
MDGLRQRVEHFLEQRNLVTEVLGALEAKTGVEKRYLAAGAVTLLSLYLLFGYGASLLCNLIGFVYPAYASIKAIESPSKDDDTVWLTYWVVYALFGLAEFFSDLLLSWFPFYYVGKCAFLLFCMAPRPWNGALMLYQRVVRPLFLRHHGAVDRIMNDLSGRALDAAAGITRNVLQVLARSRAGITPVAVAGPSTPLEADLKPSQTPQPKDK
Protein: tRNA splicing endonuclease subunit 34 (tRNA-splicing endonuclease subunit Sen34) (B0V3J0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLVVEVANGRSLVWGAEAVQALRERLGVGGRTVGALPRGPRQNSRLGLPLLLMPEEARLLAEIGAVTLVSAPRPDSRHHSLALTSFKRQQEESFQEQSALAAEARETRRQELLEKITEGQAAKKQKLEQASGASSSQEAGSSQAAKEDETSDGQASGEQEEAGPSSSQAGPSNGVAPLPRSALLVQLATARPRPVKARPLDWRVQSKDWPHAGRPAHELRYSIYRDLWERGFFLSAAGKFGG
Protein: Probable inactive receptor kinase At5g58300 (Q9LVM0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- FAM10 family protein At4g22670
- 26S proteasome regulatory subunit 6B homolog
- Camphor resistance CrcB family protein
- U-box domain-containing protein 41
- Uncharacterized protein At3g28850
- ABC transporter G family member 3
Sequence:
MMQFHFQFYVGPVFTLRPSKGFLSTCLVSFLFVTTTFCSYAIADLNSDRQALLAFAASVPHLRRLNWNSTNHICKSWVGVTCTSDGTSVHALRLPGIGLLGPIPPNTLGKLESLRILSLRSNLLSGNLPPDIHSLPSLDYIYLQHNNFSGEVPSFVSRQLNILDLSFNSFTGKIPATFQNLKQLTGLSLQNNKLSGPVPNLDTVSLRRLNLSNNHLNGSIPSALGGFPSSSFSGNTLLCGLPLQPCATSSPPPSLTPHISTPPLPPFPHKEGSKRKLHVSTIIPIAAGGAALLLLITVIILCCCIKKKDKREDSIVKVKTLTEKAKQEFGSGVQEPEKNKLVFFNGCSYNFDLEDLLRASAEVLGKGSYGTAYKAVLEESTTVVVKRLKEVAAGKREFEQQMEIISRVGNHPSVVPLRAYYYSKDEKLMVCDYYPAGNLSSLLHGNRGSEKTPLDWDSRVKITLSAAKGIAHLHAAGGPKFSHGNIKSSNVIMKQESDACISDFGLTPLMAVPIAPMRGAGYRAPEVMETRKHTHKSDVYSFGVLILEMLTGKSPVQSPSRDDMVDLPRWVQSVVREEWTSEVFDIELMRFQNIEEEMVQMLQIAMACVAQVPEVRPTMDDVVRMIEEIRVSDSETTRPSSDDNSKPKDSNVQV
Protein: Vacuolar protein sorting-associated protein 35 (Maternal-embryonic 3) (Vesicle protein sorting 35) (Q9EQH3)
Organism: Mus musculus (Mouse)
Function: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Required for endosomal localization of WASHC2 and mediates the association of the CSC with the WASH complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome {ECO:0000250|UniProtKB:Q96QK1}. Early endosome {ECO:0000305}. Late endosome {ECO:0000305}.
Interaction partners:
- Sorting nexin-1
- Vacuolar protein sorting-associated protein 26A
- Vacuolar protein sorting-associated protein 26B
- Sorting nexin-2
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-3
- Sorting nexin-5
- Sorting nexin-27
- Sorting nexin-6
- TBC1 domain family member 5
Sequence:
MPTTQQSPQDEQEKLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYMAISDELHYLEVYLTDEFAKGRKVADLYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPTDEETTGDISDSMDFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILEQVVNCRDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLALFAHREDGPGIPAEIKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDYVDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNILTVLKLKHFHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQDQPDQPVEDPDPEDFADEQSLVGRFIHLLRSDDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLAFRYKENSQMDDKWEKKCQKIFSFAHQTISALIKAELAELPLRLFLQGALAAGEIGFENHETVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMKCFSEENHEPLRTQCALAASKLLKKPDQGRAVSTCAHLFWSGRNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQLFIEILNRYIYFYEKENDAVTIQVLNQLIQKIREDLPNLESSEETEQINKHFHNTLEHLRSRRESPESEGPIYEGLIL
Protein: Replication factor A protein 3 (Single-stranded DNA-binding protein P12 subunit) (Q92374)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism.
Subcellular location: Nucleus.
Interaction partners:
- Replication factor A protein 1
- Replication factor A protein 2
- DNA polymerase delta subunit 4
- DNA polymerase subunit delta-2
- DNA polymerase delta subunit 3
- DNA polymerase delta catalytic subunit
- Replication factor C subunit 3
- ATP-dependent DNA helicase pfh1
- Flap endonuclease 1
- Inner kinetochore subunit mhf2
Sequence:
MERPTPRVTKDMLPECSGKTVRIVGKANQVEGETAKVDSNGSFDMHLTVDNTLEPNHFYEFVVSVKPDSSVQLLTCVDFGTDIDMEVYQKLVLFSHKYNSLFFE
Protein: Tail sheath protein (Q37916)
Organism: Listeria phage A511 (Bacteriophage A511)
Interaction partners:
Sequence:
MAIEIYPRKPVSRPHTEISVDTSGIGGSSSGSEKILCLVGSATGGKPNAVYKVRNYSQAKSVFRSGELLDAIERAWNPGEGTGAGDILAMRVEEAKEATFEAEGVKVSSTIYGADANDIQVALEDNTITGTKRLSIVFAKERVNQVYDNLGSIFSIKYKGTEASATFTVAVDPVTFKATKLTLKAGDKTVKEYDLGSGAYAETNVLISDINNLPDFEAKFFPIGDKNLTTDNFDAQIDVDIKTKEAYVKAVGGDIEKQTAYNGYVEFEFDRSKEIANFPLTKLTGGDNGTIPESWADKFSYFANEGGYYLVPLTSKQAVHAEALQFVRDCSYNGNPMRVFVGGGIGESMEQLFTRAIGLQNERAGLIGFSGTVKMDDGRSLKMPGYMFAAQVAGLTCGLEIGEAITFKNIAIETLDTIYEGSQLDQLNESGIITAEFVRNRAVTNFRIVDDVTTFNDKTDPVKSEIGVGEANDFLVSELKISLDNEYIGTKIIDTSASLVKNFVQSFLDRKKLAKEIQDYSPEEVQVVIEGDIARISLTVFPIRSMKKIEVSLVYRQQILTA
Protein: Serine carboxypeptidase-like 49 (EC 3.4.16.-) (P32826)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable carboxypeptidase.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- TRF-like 3
Sequence:
MEKLTFLSLLLHFVVFIASTIPSSSFLLNDRTFERSNLPSTRAEKLIRELNLFPQQDLNVIDVADLPLTAAEGPGIVERKFVFPNILADGGPTVDDLGHHAGYYKLPKSRGASMFYFFFESRNKKDAPVVIWLTGGPGCSSELAVFYENGPFKITSNMSLAWNEYGWDQVSNLLYVDQPVGTGFSYTTDKSDIRHDETGVSNDLYDFLQAFFAEHPKLAKNDFYITGESYAGHYIPAFASRVHKGNKANEGVHINLKGFAIGNGLTDPALQYPAYPDYALEMGLITQKEHDRLEKIVPLCELSIKLCGTDGTTSCLASYLVCNSLFSGVMSHAGGVNYYDIRKKCVGSLCYDFSNMEKFLNLQSVRKSLGVGDIDFVSCSTSVYQAMLVDWMRNLEVGIPTLLEDGISLLVYAGEYDLICNWLGNSRWVNAMEWSGKTNFGAAKEVPFIVDGKEAGLLKTYEQLSFLKVRDAGHMVPMDQPKAALKMLKRWMENSLIEDATVTVAAQGGEELVAQM
Protein: Mitochondrial escape protein 2 (Protein RNA12) (P32843)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:8649384}; Single-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:8649384}.
Interaction partners:
- Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1
- Pre-mRNA-splicing factor 6
- Oligoribonuclease, mitochondrial
Sequence:
MLLVRTTSLNVSRMPVPCLARGIGILKGKYRLANLMNAQPSVRHVSSEIQQKDQQAGESNTATDTGVIHKSDEETLIYFDNVYARTTSVWNPTLWYNLLLRNQSRDAVREKIRNLASPPNNPIYGLELKSTIPVKRDGGVFATFVVPPKYTKAQVNSLIQQNTARESSKNLLSYFTRASAFPVKGSPWIEDLRRLPSTTIVIKFQGPALTEEEIYSLFRRYGTIIDIFPPTAANNNVAKVRYRSFRGAISAKNCVSGIEIHNTVLHIQYENIRRGHLVSNFFTNHTRIAIPVLFALLSIFAVLVFDPIREFSIEQKITHKYSLSWDNKFWKQLKTLTSSTMTSIKYYWGGPDDNHQRKHLWEERIEKVNDLKMWLEENNNTFVVIRGPRGSGKHDLVMQHTLQNRANVLYLDCDKLIKSRTDPMFLKNAASQLGYFPIFPWIDSVTGVLDLTVQGLTGQKTGLSETKESRFRNMLTTSLMSIRRIALKNYKAFVSTGDGTVNVKEEDYLQQHPEAKPVIVIDRFEGKSEINGFVYKELSDWAAMLVQMNIAHVIFLTETVASNQRLSESLPNQVFKNLILSDASKENSRNYVLSQLEDYLYYNKKSKGENVKEPESEKETAENNDSDSEADTSVKKAEVILNEKELQEIDASLEPLGGRMLDLQAFVRRVKSGEEPSEAVDKMIEQASEQITQMFLSDKIDSNKSAQAWELIELLSANPVIPFHEIVNKPLFKAAPETGIMELENNGLITVSRDRGVLQEIRPAKPLYRAAFTYLINDPELAKVLKTRYLLKVVGFETGRIKKWEEELKPLGKVPDQKLFKTRLDYLSGKINASNAVITKCEEEIKNLSK
Protein: Probable histone chaperone asf-1-like protein (Anti-silencing function protein 1-like) (Q17603)
Organism: Caenorhabditis elegans
Function: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase tousled-like 1
- WD_REPEATS_REGION domain-containing protein
- Protein HIRA
- Chromatin assembly factor 1 subunit A dimerization domain-containing protein
- DNA replication licensing factor MCM2
- Tetratricopeptide SHNi-TPR domain-containing protein
- Probable histone-binding protein rba-1
- Protein NASP homolog 1
- Histone acetyltransferase type B catalytic subunit
- Small nuclear ribonucleoprotein associated homolog 13
Sequence:
MASRVNIVQVQILDNPAMFVDKFKMEITFEVFEHLPHDLEWELVYVGSGTSRDFDQVLDSALVGPIPEGRHKFVFDAEHPDISKIPVEDIVGVSVLLLRCKYNDQEFINMGWFVANEYTDEELKENPPAKPLIEKLSRKIETEDLRVTTFPIRWTDEDPVAEPVDEEANKVFDEDDLMPLHDDGQDDDEEEEDDDETGPNTEEVDLNESFNERMANAHDGTEQKNGEESMEHDGASGDVEMGDKH
Protein: Ragulator complex protein LAMTOR3 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3) (MEK-binding partner 1) (Mp1) (Mitogen-activated protein kinase kinase 1-interacting protein 1) (Mitogen-activated protein kinase scaffold protein 1) (O88653)
Organism: Mus musculus (Mouse)
Function: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:19177150}; Peripheral membrane protein {ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:19177150}; Cytoplasmic side {ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:19177150}. Note=Recruited to lysosome and endosome membranes by LAMTOR1. {ECO:0000269|PubMed:19177150}.
Interaction partners:
- Ragulator complex protein LAMTOR1
- Ragulator complex protein LAMTOR5
- Ragulator complex protein LAMTOR2
- Neutral amino acid transporter 9
- Ras-related GTP-binding protein C
- Ragulator complex protein LAMTOR4
- Regulatory-associated protein of mTOR
- Ras-related GTP-binding protein D
- Ras-related GTP-binding protein A
- Dual specificity mitogen-activated protein kinase kinase 1
Sequence:
MADDLKRFLYKKLPSVEGLHAIVVSDRDGVPVIKVANDSAPEHALRPGFLSTFALATDQGSKLGLSKNKSIICYYNTYQVVQFNRLPLVVSFIASSSANTGLIVSLEKELAPLFEELIKVVEVS
Protein: Rifin (Q8IBE2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLTYLNILSCYIILNILLLSSQINIQWNLYNTTQIQKTKLTITNTRLLCECDLYTPSNYDDDQEMKELMQQFEDRTSQRFHKYEERMKTTRQKCREQCDKDIKKIILNYKIEKELSQKLVTLETNIDTTDISTCVCEKSLSDKLEKTCLRCGGVFGGGVMPGFGAIGGTALYALNQLKPTAIATAIEEAIKAGASNISAAAFKASEAAGLAKVITELKALSVEKLIPGILNSIFSETHYTNATKIAEIILTKKSVTCGLSSPGNPICHEFGINFNIIDPGNGFFFPDKTGITQKVTEVVEGAKGAAANASKVASERVTAAIKAHETNVINATYAGYEITIIASIIAILIIVLIMVIIYLILRYQRKKKMKKKLQYIKLLKE
Protein: DNA repair and recombination protein RAD54-like (Protein okra) (Q93781)
Organism: Caenorhabditis elegans
Interaction partners:
- XPC
- WD_REPEATS_REGION domain-containing protein
- XPA C-terminal domain-containing protein
- XPG
- DNA-directed RNA polymerase II subunit rpb-9
- DNA repair endonuclease XPF
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB1
- RNA polymerase Rpb4/RPC9 core domain-containing protein
- UV-stimulated scaffold protein A homolog
Sequence:
MSTKPEPENPDSGTPKTLSVDDDDIVVIEDQNTPKYREAALRRSNSSSSDFDEKWEPELDEEDFCENDADVLAEPISSKSRKKSRRSDSSEFVPSEESDDDEEYEVLEKSRKKGRKSGSSSRSSSDDFIESDDNEDYKSAGLLDDNDSKNFKARIDKLKPEATSELVDTRMVTSEEYGKSSKPWKVNAGVWNKLHKFQQEGVEWLQKKTDHRSGGILADEMGLGKTIQSVVFLRSIQETARTHYKTTGLDTALIVCHVSIIAQWIKELNQWFPKARVFLLHSHCSTGRQEDYVGSIFRKLQRRRKEYPDGAIILTTYSLFTKLKKPIVKHLWQVVILDEGHYIRNENTKCSIAMRKLMTTQRFILTGTPFQNRLSEFWKLVDFVHPGRLSDSATFHRNFTHIINAGANLNCSPEAAAKAYECLVALHIAVKPLILRRLQEDHKEVLQLPEKQEIVLSCELSKRQRRLYMEYGNSHQVNEIIERRLKAFVGINHLTNICNHPGIYRSLSPASPKFGSIKDSGKVEMTFKLFDDWFKSPTNRVILFTQRRTVITMMEYFLAEKGIKCVSLTGADSAAARPKIIKKFEDDVSIKVFLMTTRAGGLGLNLTCANKVIIFDPDWNPQADNQAKNRIYRMGQTNDVAIYRLVSNGTIEDLKFFKQVQKENLAARLLHNAEIDQFVPNNTLADLFRLKPKGLEGSEIGVYLDGEIAREGSKKQKRDKVEKKAAKKRMKNKLAGFEDKKLLLSLFDDDKLVAMREHSISLQNSSSMNRIEKMKMRKSIDDAVGSLLHTEGRLAHTWKQVFHKQLRKTLKKSINGDYFVEEEQLDSYWNTVHSGFRANDDQRELDRLVKLATDMLQFFNGVPGAKEDSIHRIFVKDSDRKDPTQMFFIQEIISTLAKYDDASDTWILRDKYRSADVLSPVKKKNKRRSDDNDEVDAKRARKSREWSDSSGPSTSRM
Protein: Inositol-3-phosphate synthase (MIP synthase) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase) (IPS) (MI-1-P synthase) (P42800)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11986}.
Interaction partners:
- Myo-inositol transporter 1
- Kinase
- Transcriptional regulator
Sequence:
MSTPIEFKSSNSVTKDDHLYTKFTYENSVVEKDANGKFIVTPTASDYEFKVDLKVPKVGLLLVGIGGNNGTTLLGATLANKHNISFENKEGVVKPNYYGSVTQASTVKIGVDKETGEDVYVPFNSIVPMVNPNDLVVDGWDISGLPLDQAMKRAKVLDVTLQKQLYPYLENKKPLESIYYPDFIALNQSERANNVFNQVNGEVKTDNKWADVEKIRKDIRDFKAKNELDKVIILWTANTERYADVLPNVNDTADNLIKSIKESHEEIAPSTVFAVASILEKVPYINGSPQNTFVPGVIELAEKYDSFIGGDDFKSGQTKIKSVLAQFLVDAGIKPLSIASYNHLGNNDGYNLSSPKQFRSKEISKQSVVDDIIESNELLYNKESGDKVDHCIVIKYLPAVGDSKVAMDEYYSELMLGGHNKISIHNVCEDSLLATPLIIDLVVATEFATRVQVKGPGKSDYDELYPVASLLSYWLKAPLARPGFKPINGLNKQRQQLVNLLSVLVGLPIDNELRFERILK
Protein: BclA protein (Q6I1X8)
Organism: Bacillus anthracis
Interaction partners:
Sequence:
MSNNNYSNGLNPDESLSASAFDPNLVGPTLPPIPPFTLPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGDTGTTGPTGPTGPTGPTGPTGPTGPTGATGLTGPTGPTGPSGLGLPAGLYAFNSGGISLDLGINDPVPFNTVGSQFGTAISQLDADTFVISETGFYKITVIANTATASVLGGLTIQVNGVPVPGTGSSLISLGAPIVIQAITQITTTPSLVEVIVTGLGLSLALGTSASIIIEKVA
Protein: Follicle-stimulating hormone receptor (FSH-R) (Follitropin receptor) (P35378)
Organism: Mus musculus (Mouse)
Function: G protein-coupled receptor for follitropin, the follicle-stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P23945}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23945}.
Interaction partners:
- Follitropin subunit beta
- Glycoprotein hormones alpha chain
- Pro-opiomelanocortin
- Pituitary adenylate cyclase-activating polypeptide
- Pro-glucagon
- Natriuretic peptides A
- VIP peptides
- Gastric inhibitory polypeptide
- Thyrotropin subunit beta
- Steroid 17-alpha-hydroxylase/17,20 lyase
Sequence:
MALLLVSLLAFLGSGSGCHHWLCHCSNRVFLCQDSKVTEIPPDLPRNAIELRFVLTKLRVIPKGSFSGFGDLEKIEISQNDVLEVIEADVFSNLPNLHEIRIEKANNLLYINPEAFQNLPSLRYLLISNTGIKHLPAFHKIQSLQKVLLDIQDNINIHIIARNSFMGLSFESVILWLNKNGIQEIHNCAFNGTQLDELNLSDNNNLEELPDDVFQGASGPVVLDISRTKVYSLPNHGLENLKKLRARSTYRLKKLPSLDKFVMLIEASLTYPSHCCAFANWRRQTSELHPICNKSISRQDIDDMTQPGDQRVSLVDDEPSYGKGSDMLYSEFDYDLCNEFVDVTCSPKPDAFNPCEDIMGYNILRVLIWFISILAITGNTTVLVVLTTSQYKLTVPRFLMCNLAFADLCIGIYLLLIASVDIHTKSQYHNYAIDWQTGAGCDAAGFFTVFASELSVYTLAAITLERWHTITHAMQLECKVQLCHAASIMVLGWAFAFAAALFPIFGISSYMKVSICLPMDIDSPLSQLYVMALLVLNALAFVVICGCYTHIYLTVRNPNIVSSSRDTKIAKRMATLIFTDFLCMAPILFFAISASLKVPLITVSKAKILLVLFYPINSCANPFLYAIFTKNFRRDFFVLMSKFGCYEVQAQIYKTETSSITHNFHSRKNPCSSAPRVTNSYVLVPLNHSVQN
Protein: Rho-related protein racA (P34147)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- GTPase activating protein homolog 1
- Cofilin-1A
Sequence:
MQAIKLVVVGDGAVGKSCLLIAYTTNAFPGEYVPTVFDNYSANVMIDGKPFNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSIVSRASFENIRAKWYPEILHHAPNIPIVLVGTKNDLRGHHDLKRPEVSAAEANNLVRELGFSGYVETSALLQTNLRELFSLAIRTATSPKSASAKKKGGFFSSSSSSSSSSSSKSSEKSVPIPPVMPPAGKAPWIDIITSSYDKEMRETLNSESFSDVKFTFFEERPVYAHRVILCSASEFFRRVFGYTLSSDQAEFKLDDLNEGKVKNIRSVTIKPNEKNDDGTKSSGEFVEISIDSSINRRVFNRFIEFLYTGVLNYLDKNDQLQETIALAESVGFKYLASACKNVLGGNEDLNPSIGTFLNDQLGETSKELFFTKKILSDIQFIVEGRSIFAHKALIFSRSNVVNALIGRNFIEREGKVEMSDDVTFDSFMAILEYLYTAHAPIEEGDSVGILVLGNRFDLRRLVSLCELYISKEIERATTIGIFRSELDIIGLLICAQRHNAPQLEKFCLHFISSNYQPMRRRKEFALLDDKTKKHIEDNQWPPIHYLRAVEDYEKEMEKLKSSSKGWFKK
Protein: Melanoma-associated antigen 12 (Cancer/testis antigen 1.12) (CT1.12) (MAGE-12 antigen) (MAGE12F antigen) (P43365)
Organism: Homo sapiens (Human)
Function: Not known, though may play a role tumor transformation or progression. In vitro promotes cell viability in melanoma cell lines.
Interaction partners:
- Melanoma-associated antigen 6
- Chondrosarcoma-associated gene 1 protein
- Melanoma-associated antigen 3
- Melanoma-associated antigen 1
- Cancer/testis antigen 1
Sequence:
MPLEQRSQHCKPEEGLEAQGEALGLVGAQAPATEEQETASSSSTLVEVTLREVPAAESPSPPHSPQGASTLPTTINYTLWSQSDEGSSNEEQEGPSTFPDLETSFQVALSRKMAELVHFLLLKYRAREPFTKAEMLGSVIRNFQDFFPVIFSKASEYLQLVFGIEVVEVVRIGHLYILVTCLGLSYDGLLGDNQIVPKTGLLIIVLAIIAKEGDCAPEEKIWEELSVLEASDGREDSVFAHPRKLLTQDLVQENYLEYRQVPGSDPACYEFLWGPRALVETSYVKVLHHLLKISGGPHISYPPLHEWAFREGEE
Protein: Cathepsin 7 (EC 3.4.22.-) (Cathepsin 1) (Q91ZF2)
Organism: Mus musculus (Mouse)
Function: Involved in trophoblast cell proliferation and differentiation probably by affecting mitotic cell cycle progression. Proteolytic activity and nuclear localization are essential for its role in cell cycle progression.
Subcellular location: Endosome {ECO:0000269|PubMed:18776147, ECO:0000305}. Lysosome {ECO:0000269|PubMed:18776147, ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18776147}. Golgi apparatus {ECO:0000269|PubMed:18776147, ECO:0000305}. Nucleus {ECO:0000269|PubMed:18776147}. Secreted, extracellular space {ECO:0000269|PubMed:18776147}.
Interaction partners:
Sequence:
MTPTVFLSILCLGVALAAPAPDYNLDAEWEEWKRSNDRTYSPEEEKQRRAVWEGNVKWIKQHIMENGLWMNNFTIEMNEFGDMTGEEMKMLTESSSYPLRNGKHIQKRNPKIPPTLDWRKEGYVTPVRRQGSCGACWAFSVTACIEGQLFKKTGKLIPLSVQNLMDCSVSYGTKGCDGGRPYDAFQYVKNNGGLEAEATYPYEAKAKHCRYRPERSVVKVNRFFVVPRNEEALLQALVTHGPIAVAIDGSHASFHSYRGGIYHEPKCRKDTLDHGLLLVGYGYEGHESENRKYWLLKNSHGERWGENGYMKLPRGQNNYCGIASYAMYPAL
Protein: Ino4p (A0A1D8PH18)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Transcriptional regulator
- Ino2p
Sequence:
MSSDSSSPETTTISEQNTTTNETGTGKQGRKKTKSSVLSDEQKKAHHIASEQKRRENIRAEFDKIVSLTPNLNESENRSELNILTKSADYIDELRAENIKLIEICRQKGISIPPELIYSGPKNDGSDIAK