wanglab/gogpt-training-data huggingface dataset:
Protein: Regulator of G-protein signaling 3 (RGP3) (RGS3) (P49796)
Organism: Homo sapiens (Human)
Function: Down-regulates signaling from heterotrimeric G-proteins by increasing the GTPase activity of the alpha subunits, thereby driving them into their inactive GDP-bound form. Down-regulates G-protein-mediated release of inositol phosphates and activation of MAP kinases.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9858594}. Nucleus {ECO:0000269|PubMed:10749886}. Cell membrane {ECO:0000269|PubMed:9858594}; Peripheral membrane protein {ECO:0000269|PubMed:9858594}. Note=Long isoforms are cytoplasmic and associated with the plasma membrane (PubMed:9858594). Short isoforms are nuclear (PubMed:10749886).
Interaction partners:
- Ephrin-B2
- Ephrin-B1
- Ephrin-B3
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Regulator of G-protein signaling 12
Sequence:
MPVIPALWEVEMGRSQGQEIETILANRSHSDSTPLPNFLSGSHRPECCTCRLLTASGAQDSLPFGRRLYSGPWRSCEEVCHVSVLSVLSTSCGLSLSLPIFPGWMEWLSPDIALPRRDEWTQTSPARKRITHAKVQGAGQLRLSIDAQDRVLLLHIIEGKGLISKQPGTCDPYVKISLIPEDSRLRHQKTQTVPDCRDPAFHEHFFFPVQEEDDQKRLLVTVWNRASQSRQSGLIGCMSFGVKSLLTPDKEISGWYYLLGEHLGRTKHLKVARRRLRPLRDPLLRMPGGGDTENGKKLKITIPRGKDGFGFTICCDSPVRVQAVDSGGPAERAGLQQLDTVLQLNERPVEHWKCVELAHEIRSCPSEIILLVWRMVPQVKPGPDGGVLRRASCKSTHDLQSPPNKREKNCTHGVQARPEQRHSCHLVCDSSDGLLLGGWERYTEVAKRGGQHTLPALSRATAPTDPNYIILAPLNPGSQLLRPVYQEDTIPEESGSPSKGKSYTGLGKKSRLMKTVQTMKGHGNYQNCPVVRPHATHSSYGTYVTLAPKVLVFPVFVQPLDLCNPARTLLLSEELLLYEGRNKAAEVTLFAYSDLLLFTKEDEPGRCDVLRNPLYLQSVKLQEGSSEDLKFCVLYLAEKAECLFTLEAHSQEQKKRVCWCLSENIAKQQQLAASPPDSKMFETEADEKREMALEEGKGPGAEDSPPSKEPSPGQELPPGQDLPPNKDSPSGQEPAPSQEPLSSKDSATSEGSPPGPDAPPSKDVPPCQEPPPAQDLSPCQDLPAGQEPLPHQDPLLTKDLPAIQESPTRDLPPCQDLPPSQVSLPAKALTEDTMSSGDLLAATGDPPAAPRPAFVIPEVRLDSTYSQKAGAEQGCSGDEEDAEEAEEVEEGEEGEEDEDEDTSDDNYGERSEAKRSSMIETGQGAEGGLSLRVQNSLRRRTHSEGSLLQEPRGPCFASDTTLHCSDGEGAASTWGMPSPSTLKKELGRNGGSMHHLSLFFTGHRKMSGADTVGDDDEASRKRKSKNLAKDMKNKLGIFRRRNESPGAPPAGKADKMMKSFKPTSEEALKWGESLEKLLVHKYGLAVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMASKAKKIFAEYIAIQACKEVNLDSYTREHTKDNLQSVTRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDLINQKKMSPPL
Protein: ADP-ribosylation factor GTPase-activating protein 3 (ARF GAP 3) (Q9D8S3)
Organism: Mus musculus (Mouse)
Function: GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Also found on peripheral punctate structures likely to be endoplasmic reticulum-Golgi intermediate compartment. {ECO:0000250}.
Interaction partners:
- Coatomer subunit beta
- Coatomer subunit beta'
- ADP-ribosylation factor 1
- ADP-ribosylation factor GTPase-activating protein 1
- Coatomer subunit delta
- Coatomer subunit gamma-1
- Coatomer subunit gamma-2
- Coatomer subunit alpha
- ADP-ribosylation factor 4
- ADP-ribosylation factor 5
Sequence:
MGDPSKQDILAIFKRLRSVPTNKVCFDCGAKNPSWASISYGVFLCIDCSGSHRSLGVHLSFIRSTELDSNWSWFQLRCMQVGGNSNASSFFHQHGCATKDTNAKYNSRAAQLYREKIKTLATQATRRHGTDLWLDSCAAPPVSPPPKEEDFFASHASLEVSGAMQASAQPESASSTPWGLETTPEKHEGGPGQGPSVEGLNTPGKAAPEVSSIIKKKPNQAKKGLGAKKGSLGAQKLTNTSFTEIEKQAQAVDKRKEQEDLARGAPKEESIVSSLRLAYKDLEISRKKDERLNLSGQKKVEAERLGMGFGSCRSGISHSVTSDMQTIEQESPTLAKPRRKYQEDPEDSYFSSSSKWSEQSSRYFDDPMELRSSSFSSWDDGADSYWKKDSSRDPEPAMRSTGSSDRPSARRKPEYEPIGSTDEAQKKFGNVKAISSDMYFGIQAQTDFETRARLERLSTSSSISSADLFDEQRKQTAGNYNLSNVLPNAPDMAQFKQGVRSVAGKLSVFANGVMTSIQDRYGS
Protein: Isopenicillin N synthase (IPNS) (EC 1.21.3.1) (P05326)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Isopenicillin N synthase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. IpnA catalyzes the cyclization of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) to form isopenicillin N (IPN) that contains the beta-lactam nucleus. The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase penDE to yield penicillin in the peroxisomal matrix (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P08703}.
Interaction partners:
- N-
- Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 40 kDa form
- Acyl-CoA:6-aminopenicillanic-acid-acyltransferase, putative
Sequence:
MGSVSKANVPKIDVSPLFGDDQAAKMRVAQQIDAASRDTGFFYAVNHGINVQRLSQKTKEFHMSITPEEKWDLAIRAYNKEHQDQVRAGYYLSIPGKKAVESFCYLNPNFTPDHPRIQAKTPTHEVNVWPDETKHPGFQDFAEQYYWDVFGLSSALLKGYALALGKEENFFARHFKPDDTLASVVLIRYPYLDPYPEAAIKTAADGTKLSFEWHEDVSLITVLYQSNVQNLQVETAAGYQDIEADDTGYLINCGSYMAHLTNNYYKAPIHRVKWVNAERQSLPFFVNLGYDSVIDPFDPREPNGKSDREPLSYGDYLQNGLVSLINKNGQT
Protein: Solute carrier family 25 (Mitochondrial carrier dicarboxylate transporter), member 10, isoform CRA_a (Solute carrier family 25 member 10 isoform 1) (A0A0S2Z3G3)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAAEARVSRWYFGGLASCGAACCTHPLDLLKVHLQTQQEVKLRMTGMALRVVRTDGILALYSGLSASLCRQMTYSLTRFAIYETVRDRVAKGSQGPLPFHEKVLLGSVSGLAGGFVGTPADLVNVRMQNDVKLPQGQRRNYAHALDGLYRVAREEGLRRLFSGATMASSRGALVTVGQLSCYDQAKQLVLSTGYLSDNIFTHFVASFIAAAGDEPPPQGGCATFLCQPLDVLKTRLMNSKGEYQGVFHCAVETAKLGPLAFYKGLVPAGIRLIPHTVLTFVFLEQLRKNFGIKVPS
Protein: Protein kinase C delta (A0A494C1T7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVT
Protein: PR domain zinc finger protein 12 (EC 2.1.1.-) (PR domain-containing protein 12) (A2AJ77)
Organism: Mus musculus (Mouse)
Function: Involved in the positive regulation of histone H3-K9 dimethylation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H4Q4}.
Interaction partners:
Sequence:
MMGSVLPAEALVLKTGLKAPGLALAEVITSDILHSFLYGRWRNVLGEQLLEDKSHHASPKTAFTAEVLAQSFSGEVQKLSSLVLPVEVIIAQSSIPGEGLGIFSKTWIKAGTEMGPFTGRVIAPEHVDICKNNNLMWEVFNEDGTVRYFIDASQEDHRSWMTYIKCARNEQEQNLEVVQIGTSIFYKAIEMIPPDQELLVWYGNSHNTFLGIPGVPGLEEEQKKNKHEDFHPADSATGTAGRMRCVICHRGFNSRSNLRSHMRIHTLDKPFVCRFCNRRFSQSSTLRNHVRLHTGERPYKCQVCQSAYSQLAGLRAHQKSARHRPPSTALQAHSPALPAPHAHAPALAAAAAAAAAAHHLPAMVL
Protein: Nucleus accumbens-associated protein 1 (NAC-1) (BTB/POZ domain-containing protein 14B) (Q7TSZ8)
Organism: Mus musculus (Mouse)
Function: Functions as a transcriptional repressor. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines. Involved in the acute behavioral and neurological responses to cocaine and amphetamines.
Subcellular location: Nucleus. Cytoplasm. Note=Distribution in the cytoplasm is dependent on phosphorylation. {ECO:0000250}.
Interaction partners:
- Homeobox protein NANOG
- POU domain, class 5, transcription factor 1
- Sal-like protein 4
- Transcription factor SOX-2
- Zinc finger protein 281
- Nuclear receptor subfamily 0 group B member 1
Sequence:
MAQTLQMEIPNFGNSILECLNEQRLQGLYCDVSVVVKGHAFKAHRAVLAASSSYFRDLFNSSRSAVVELPAAVQPQSFQQILTFCYTGRLSMNMGDQFLLIYTAGFLQIQEIMEKGTEFFLKVSSPSCDSQGLHPEEAPSSEPQSPVAQTLGWPACSTPLPLVSRVKTEQELDSVQCTPMAKRLWDSSQKEAGGSGGNNGSRKMAKFSTPDLALNRMPQPLSMATATAAVAVVAVGGCVSGPSMSERTSPGTSSAYTSDSPSSYHNEEDEEEDAGEEGTDEQYRQICNMYTMYSMLNVGQTAEKVEALPEQVVLESRSRIRVRQDLASLPAELINQIGNRCHPKLYDEGDPSEKLELVTGTNVYITRAQLMNCHVSAGTRHKVLLRRLLASFFDRNTLANSCGTGIRSSTNDPRRKPLDSRVLHAVKYYCQNFAPNFKESEMNAIAADMCTNARRVVRKSWLPKTKPLHLVEGDNYSSFISDTCKIEPDMMSMEHSFETASHDGEAGPSAEVLQ
Protein: Glutamate-1-semialdehyde 2,1-aminomutase (GSA) (EC 5.4.3.8) (Glutamate-1-semialdehyde aminotransferase) (GSA-AT) (P23893)
Organism: Escherichia coli (strain K12)
Function: Aminomutase that catalyzes the transfer of the amine group on carbon 2 of glutamate 1-semialdehyde to the adjacent carbon 1 to form 5-aminolevulinate.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Glutamyl-tRNA reductase
- Delta-aminolevulinic acid dehydratase
- Porphobilinogen deaminase
- Enterobactin synthase component F
- Uroporphyrinogen decarboxylase
- Uroporphyrinogen-III synthase
- Ferrochelatase
- Malonyl CoA-acyl carrier protein transacylase
- Siroheme synthase
- Oxygen-dependent coproporphyrinogen-III oxidase
Sequence:
MSKSENLYSAARELIPGGVNSPVRAFTGVGGTPLFIEKADGAYLYDVDGKAYIDYVGSWGPMVLGHNHPAIRNAVIEAAERGLSFGAPTEMEVKMAQLVTELVPTMDMVRMVNSGTEATMSAIRLARGFTGRDKIIKFEGCYHGHADCLLVKAGSGALTLGQPNSPGVPADFAKYTLTCTYNDLASVRAAFEQYPQEIACIIVEPVAGNMNCVPPLPEFLPGLRALCDEFGALLIIDEVMTGFRVALAGAQDYYGVVPDLTCLGKIIGGGMPVGAFGGRRDVMDALAPTGPVYQAGTLSGNPIAMAAGFACLNEVAQPGVHETLDELTTRLAEGLLEAAEEAGIPLVVNHVGGMFGIFFTDAESVTCYQDVMACDVERFKRFFHMMLDEGVYLAPSAFEAGFMSVAHSMEDINNTIDAARRVFAKL
Protein: Fasciclin-like arabinogalactan protein 4 (A9XTK9)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MASSSPLSPILLSLFLVFICGVSAQTAPAPAPSGPLNFTGILDKNGQYTYFLQLLAQTQVGSQVQTQLKTTTEGFTVFAPTDNAFNNLKPGTVNNLDPQQKVQLVLYHVIPKYYSLNDLQFVSNPVRTQAGEDFGLNVTGLNNQVNVSSGVVETQINNALYQKKPLAIYQADKVLLPEEFFEAKSPAAAPSPATKKSSTGSKSNSRASATADEPASADNSGSTGRNMGLGFVVGLALACIGFLS
Protein: HERV-H LTR-associating protein 2 (Human endogenous retrovirus-H long terminal repeat-associating protein 2) (Q9UM44)
Organism: Homo sapiens (Human)
Function: Through interaction with TMIGD2, costimulates T-cells in the context of TCR-mediated activation. Enhances T-cell proliferation and cytokine production via an AKT-dependent signaling cascade.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Putative uncharacterized protein ANKRD13C-DT
- Transmembrane and immunoglobulin domain-containing protein 2
- Killer cell immunoglobulin-like receptor 3DL3
- Cytotoxic T-lymphocyte protein 4
Sequence:
MKAQTALSFFLILITSLSGSQGIFPLAFFIYVPMNEQIVIGRLDEDIILPSSFERGSEVVIHWKYQDSYKVHSYYKGSDHLESQDPRYANRTSLFYNEIQNGNASLFFRRVSLLDEGIYTCYVGTAIQVITNKVVLKVGVFLTPVMKYEKRNTNSFLICSVLSVYPRPIITWKMDNTPISENNMEETGSLDSFSINSPLNITGSNSSYECTIENSLLKQTWTGRWTMKDGLHKMQSEHVSLSCQPVNDYFSPNQDFKVTWSRMKSGTFSVLAYYLSSSQNTIINESRFSWNKELINQSDFSMNLMDLNLSDSGEYLCNISSDEYTLLTIHTVHVEPSQETASHNKGLWILVPSAILAAFLLIWSVKCCRAQLEARRSRHPADGAQQERCCVPPGERCPSAPDNGEENVPLSGKV
Protein: Guanine nucleotide-binding protein-like 1 (GTP-binding protein HSR1) (P36915)
Organism: Homo sapiens (Human)
Function: Possible regulatory or functional link with the histocompatibility cluster.
Interaction partners:
- Elongation factor 1-alpha 1
- 60S ribosomal export protein NMD3
- Proliferation-associated protein 2G4
- GTP-binding protein 4
- Ribosome biogenesis protein BOP1
- Eukaryotic translation initiation factor 6
- Large ribosomal subunit protein uL18
- Pescadillo homolog
- Nucleolar complex protein 2 homolog
- Heat shock factor protein 1
Sequence:
MPRKKPFSVKQKKKQLQDKRERKRGLQDGLRSSSNSRSGSRERREEQTDTSDGESVTHHIRRLNQQPSQGLGPRGYDPNRYRLHFERDSREEVERRKRAAREQVLQPVSAELLELDIREVYQPGSVLDFPRRPPWSYEMSKEQLMSQEERSFQDYLGKIHGAYSSEKLSYFEHNLETWRQLWRVLEMSDIVLLITDIRHPVVNFPPALYEYVTGELGLALVLVLNKVDLAPPALVVAWKHYFHQHYPQLHVVLFTSFPRDPRTPQDPSSVLKKSRRRGRGWTRALGPEQLLRACEAITVGKVDLSSWREKIARDVAGATWGNGSGEEEEEEDGPAVLVEQQTDSAMEPTGPTQERYKDGVVTIGCVGFPNVGKSSLINGLVGRKVVSVSRTPGHTRYFQTYFLTPSVKLCDCPGLIFPSLLPRQLQVLAGIYPIAQIQEPYTAVGYLASRIPVQALLHLRHPEAEDPSAEHPWCAWDICEAWAEKRGYKTAKAARNDVYRAANSLLRLAVDGRLSLCFHPPGYSEQKGTWESHPETTELVVLQGRVGPAGDEEEEEEEELSSSCEEEGEEDRDADEEGEGDEETPTSAPGSSLAGRNPYALLGEDEC
Protein: Homeobox protein Hox-A7 (Homeobox protein Hox-1.1) (Homeobox protein M6-12) (M6) (P02830)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Meis1
- Homeobox protein Hox-A9
- Homeobox protein Hox-B7
- Homeobox protein Hox-C6
- Homeobox protein Hox-B5
- Homeobox protein Hox-B6
- Pre-B-cell leukemia transcription factor 1
- Homeobox protein Hox-A6
Sequence:
MSSSYYVNALFSKYTAGASLFQNAEPTSCSFAPNSQRSGYGPGAGAFASTVPGLYNVNSPLYQSPFASGYGLGADAYNLPCASYDQNIPGLCSDLAKGACDKADEGVLHGPAEASFRIYPWMRSSGPDRKRGRQTYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKEHKDESQAPTAAPEDAVPSVSTAADKADEEEEEEEEEEEEEEE
Protein: C-X-C chemokine receptor type 2 (High affinity interleukin-8 receptor B) (C9J1J7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MEDFNMESDSFEDFWKGEDLSNYSYSSTLPPFLLDAAPCEPESLEINKYFVVIIYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRYLVKFICLSIWGL
Protein: Phosphatidylinositol-3-phosphatase SAC1 (EC 3.1.3.64) (Phosphatidylinositol-4-phosphate phosphatase) (Suppressor of actin mutations 1-like protein) (Q9NTJ5)
Organism: Homo sapiens (Human)
Function: Phosphoinositide phosphatase which catalyzes the hydrolysis of phosphatidylinositol 4-phosphate (PtdIns(4)P). Can also catalyze the hydrolysis of phosphatidylinositol 3-phosphate (PtdIns(3)P) and has low activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) (By similarity). Shows a very robust PtdIns(4)P phosphatase activity when it binds PtdIns(4)P in a 'cis' configuration in the cellular environment, with much less activity seen when it binds PtdIns(4)P in 'trans' configuration. PtdIns(4)P phosphatase activity (when it binds PtdIns(4)P in 'trans' configuration) is enhanced in the presence of PLEKHA3.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27044890, ECO:0000269|PubMed:29461204, ECO:0000269|PubMed:31806350}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:29461204, ECO:0000269|PubMed:31806350}. Note=Trafficking between the ER and Golgi is regulated by nutrient status and by TMEM39A (PubMed:31806350). Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS) in the presence of phosphatidylinositol-4,5-bisphosphate (PubMed:27044890). {ECO:0000269|PubMed:27044890, ECO:0000269|PubMed:31806350}.
Interaction partners:
Sequence:
MATAAYEQLKLHITPEKFYVEACDDGADDVLTIDRVSTEVTLAVKKDVPPSAVTRPIFGILGTIHLVAGNYLIVITKKIKVGEFFSHVVWKATDFDVLSYKKTMLHLTDIQLQDNKTFLAMLNHVLNVDGFYFSTTYDLTHTLQRLSNTSPEFQEMSLLERADQRFVWNGHLLRELSAQPEVHRFALPVLHGFITMHSCSINGKYFDWILISRRSCFRAGVRYYVRGIDSEGHAANFVETEQIVHYNGSKASFVQTRGSIPVFWSQRPNLKYKPLPQISKVANHMDGFQRHFDSQVIIYGKQVIINLINQKGSEKPLEQTFATMVSSLGSGMMRYIAFDFHKECKNMRWDRLSILLDQVAEMQDELSYFLVDSAGQVVANQEGVFRSNCMDCLDRTNVIQSLLARRSLQAQLQRLGVLHVGQKLEEQDEFEKIYKNAWADNANACAKQYAGTGALKTDFTRTGKRTHLGLIMDGWNSMIRYYKNNFSDGFRQDSIDLFLGNYSVDELESHSPLSVPRDWKFLALPIIMVVAFSMCIICLLMAGDTWTETLAYVLFWGVASIGTFFIILYNGKDFVDAPRLVQKEKID
Protein: Factor arrest protein 11 (P53917)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Participates in the control of the reentry into the cell cycle following pheromone treatment.
Interaction partners:
- Factor arrest protein 8
- Factor arrest protein 3
- Vacuolar protein sorting-associated protein 64
- Factor arrest protein 10
- Protein phosphatase PP2A regulatory subunit A
- Factor arrest protein 7
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-like PPG1
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Serine/threonine-protein kinase KIC1
Sequence:
MNASGRSHSKGPIIRSVSLEDLKRNSSFKGNLKYKDEVTSHKEPQVGTLSNEELLKDLDNMLRGKLNMGRNSFHADKRNKSDGNISALTFKARSGLEGDIRTIDIQQDSSDENDNFKFSDDGVNKDRNNEKDNNTDNAVEFQDDAEEAEEENEDESFANVDELDGFDLNKVSDGKHVPINEKGEVDYNMPVDKEFQKSLDQCAASLEERSSAPYALQRAVDWELKMFYSLEDELSEWFCSSDYMHFGQTQTLFKQKITQPQLFFDDENYAASVVECLIEDIPNSLASNLLALSYISMGCFAFTNSKSEHTKIIRRNNLMLVPHIQEIVHAFKKIAISCRDDNRNLKKQTILLFHSSTILYFICSICIEGRGENPEAVNVVIDAFEKTDLLEFLTKYIENWRWNSRLAMRIRNMISLLFKLIVLQFGDSSVYKQTKSSIYNLHGLTYPSKHPEKLSISPLHYQAFREDITSRFPDYNMPSSGLPKDVDKSESLSQFLEIPRPKSKNPLNMALIVPEKHIATPAPSPPSSPQLMHLGEGPRPRKSFQTNMAYPCLYPSDNEGSEDDTLEDRIDLNIERKPDNDIVIPFSTEEAARILSESLEIKLSTKQLWYERDLFMITERGWKQQLENEPYDYAALNHDANSSKEEKSAICIMQRIDKYYKSCLSSFNSLVFVLLQTMESSLTNNFHRKSEVSDKNLLNMLTPQLEIVRAKELSLKSAAGILHALLKWFKLSHILKFEHLAVVIHDSRYINTCASILSKYSEVYPERVFNKYVQTPNSFWKECSLSNESYRESYSVDDSGEVDTEIMPSFAYLLRILRKVTGNKTQRLKELPLSIGILFKRYYRLFNLDMYHPILKITRELTPFKNKRWKSEHMELISGVYLYEKLELTDNWVTGKDISGELSDACGQEIALRALLQFYNFQHYEISMEDLGYGHRNSSSQDLLNKESEYLNI
Protein: HTH-type transcriptional regulator IscR (Q667Y0)
Organism: Yersinia pseudotuberculosis serotype I (strain IP32953)
Function: Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins.
Interaction partners:
Sequence:
MRLTSKGRYAVTAMLDVALHSQDGPVPLADISERQGISLSYLEQLFSRLRKNGLVASVRGPGGGYLLGKDASAIAVGAVITAVDESVDATRCQGKEGCQGGNRCLTHTLWRDLSERISSFLNNITLAELVNNQDILEVADRQNNDTRRTANGRPQETINVNLRA
Protein: BK channel (H8ESE4)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGEIYSPSQSKGFNQPYGYPMNCNLSRVFMEMTEEDRKCLEERKYWCFLLSSITTFCASMILVVIWRVVTHLCCQRREKEFVEPIPAPEAVQINMNGSKHAPSETDPFLKQQEEKHLGWMTEAKDWAGELISGQSLTGRFLVLLVFILSIGSLIIYFYDASFQNFQVETCIPWQDSPSQQIDLGFNIFFLVYFFIRFIAASDKVWFLLEMYSWIDFFTIPPSFVAIYLQRNWLGFRFLRALRLMTVPDILQYLNILKTSSSIRLTQLVTIFVAVCLTGAGLVHLLENSGDFFKGFINPHRITYADSVYFVLVTMSTVGYGDIYCTTLCGRLFMIFFILFGLAMFASYVPEIADLIGNRQKYGGEYKGEHGKKHIVVCGHITYDSVSHFLQDFLHEDRDDVDVEVVFLHRVVPDLELEGLFKRHFTKVEFFTGTVMDSLDLSRVKIGDADACLVLANKYSTNPDAEDAANIMRVISIKNYSSDIRVIVQLMQYHNKAYLLNIPSWDWKRGDDVICLAELKLGFIAQSCLAPGFSTMMANLFAMRSFKTSPHTPLWLNDYLRGAGMEMYTESLSPSFANMSFPEAANLLFNRLGLLLLAIELKDEENKECNIAINPGPHIVIQPQTQGFFIAQSADEVKRAFFWCKQCHDDIKDVSLIKKCKCKNLALFRRNTKHSTAAREKNAKISDYSDFDALFYQNDARATDVLQQFQPQAPAGPMGHLGQQVQLRMINQQRPSSGGRRNSMSIPPDGRGVDFSKDFEQQFQDMKYDSTGMFHWCPSRNLEDCVLERHQAAMTVLNGHVVVCLFADQDSPLIGLRNFIMPLRSSNFHYHELKHVVIVGDLEYLRKEWKTLYNLPKISILNGSPLSRADLRAVNINLCDMCVIISARVPNTEDTTLADKEAILASLNIKAMQFDDTLGFFPMRHQTGDRSPLGSPISMQKKGAKFGTNVPMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAISVLDSLMSTTYFNDSALTLIRTLVTGGATPELELILAEGAGLRGGYSTPETLSNRDRCRIAQISLQDNPYDGVVHNTTYGAMFTIALRRYGQLCIGLYRLHDQDNPDSMKRYVITNPPAELRIKNTDYVYVLEQFDPGLEYEPGKRHF
Protein: 3 beta-hydroxysteroid dehydrogenase type 7 (3 beta-hydroxysteroid dehydrogenase type VII) (3-beta-HSD VII) (3-beta-hydroxy-Delta(5)-C27 steroid oxidoreductase) (C(27) 3-beta-HSD) (EC 1.1.1.-) (Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase) (EC 1.1.1.181) (Confluent 3Y1 cell-associated 2) (O35048)
Organism: Rattus norvegicus (Rat)
Function: The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. HSD VII is active against four 7-alpha-hydroxylated sterols. Does not metabolize several different C(19/21) steroids as substrates. Involved in bile acid synthesis. Plays a key role in cell positioning and movement in lymphoid tissues by mediating degradation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC): 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- 25-hydroxycholesterol 7-alpha-hydroxylase
- Aldo-keto reductase family 1 member D1
- Cytochrome P450 7A1
- Cytochrome P450 family 8 subfamily B member 1
- Cytochrome P450, family 39, subfamily a, polypeptide 1
- Cholesterol 25-hydroxylase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Methylsterol monooxygenase 1
- Squalene monooxygenase
- Lanosterol synthase
Sequence:
MADSAQVPALVYLVTGGCGFLGEHIVRMLLEWEPRLRELRVFDLHLSSWLEELKTGPVQVTAIQGDVTQAHEVAAAMAGSHVVIHTAGLVDVFGKASPETIHKVNVQGTQNVIDACVQTGTRLLVYTSSMEVVGPNVKGHPFYRGNEDTPYEAIHRHPYPCSKALAEQLVLEANGRKGLRFGGRLFRAIPASVEHGRVYVGNVAWMHILVARELEQRAALMGGQVYFCYDKSPYKSYEDFNMEFLSPCGLRLIGTHPLLPYWLLVLLTALNALLQWLLRPLVLYTPLLNPYTLAVANTTFTVSTNKAQRHFGYKPLFSWEESRARTIHWVQAMEGSAW
Protein: Liver X nuclear receptor alpha variant 1 (F1D8N1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MSLWLGAPVPDIPPDSAVELWKPGAQDASSQAQGGSSCILREEARMPHSAGGTAGVGLEAAEPTALLTRAEPPSEPTEIRPQKRKKGPAPKMLGNELCSVCGDKASGFHYNVLSCEGCKGFFRRSVIKGAHYICHSGGHCPMDTYMRRKCQECRLRKCRQAGMREECVLSEEQIRLKKLKRQEEEQAHATSLPPRASSPPQILPQLSPEQLGMIEKLVAAQQQCNRRSFSDRLRVTPWPMAPDPHSREARQQRFAHFTELAIVSVQEIVDFAKQLPGFLQLSREDQIALLKTSAIEVMLLETSRRYNPGSESITFLKDFSYNREDFAKAGLQVEFINPIFEFSRAMNELQLNDAEFALLIAISIFSADRPNVQDQLQVERLQHTYVEALHAYVSIHHPHDRLMFPRMLMKLVSLRTLSSVHSEQVFALRLQDKKLPPLLSEIWDVHE
Protein: Synemin (G3V9G5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLSWRLQTSSEKAELQELNARLYEYVCRVRELERENLLLEEELRSRLSREDRWAEDQALYAEEARSLRQQLDELSWSTALAEGERDALRRELLDLQREGLEASTARGRLDAELEAQRRELEEALGARAALEALLGRLEAERRDLDAAHERQVRELRARASSLTMHFRARATGPAAPPPRLRDVHDSYALLVAESWRESMQLYEDEVRELEQALRRGQESRLQAEDEARLCAQEADALRNQALELEQLRARLEDELLRMREEYGMQAEERQRVIDSLEDEKDALTLAMADRLREYQELLQVKTGLSLEVATYRALLEGESNPEILIWTENIENVPRESRNTSYRYTDSVLQRKNEKNLFPRRKTPWAAVNHSSTLYSNGPGHLDSQTTTAVGNAARRGFLTSCYSSSATTSQQKPLEKTVSSQASLRPVIPTHGFLRNTDAQVKTFSHGPKAEGMGDTLTRRATESVITRESYRGHQGNVAAGAVNSTQSNERTVILGKKLETQATKEQERDRSGVVKLKPEEKMFDSKEKASEERNLRWEELTKLDARERESQHLRNEAKGKETLTGRSRKEREVPISLEVSRGSKSEVSTIHLQSSGRKDSANSREREVKTKETKFHLDGKDTAGSLQSDSTTETIAENIVTTILKQFTQSPGAEENVSSLPDTKVTYLDRKEFPGDRKTKTEIVMESKLTEDVDVSDEAGLDYLLSKDVKEVGLKGKSTETVIGEMINLGLKGREGRAKVVNVEIVEEPMSYVGGGKVEFSTPFQVEEVDDVSPSPKGFIEEEEGEGETHMAFSMHQRQRTNQPQVNVPHVEEVTEAGDSEGEQSYFVSTPDEYPGGHDREDDGSVYGQIHIEEESTIRYSWQDEIAQGTWRRKARGDTGEEKHMKVLEVPSASLGGAFGSAHVKEEASGELHAEPTIIEKEIKIPHEFHTSIKGVFSSEPRHQLVEVIGQLEETLPERMKEELSALTRQSQGEPGSVSVDVKKVQSSAGGSVTLMAEVNLSQTVDADQLDLEELSRDEAGEIEKAVESVVRESLTKRSSPVPRSPDREDGEEAPAGGFLFKRWATRELYSPSGEKDDTDRVFHSSDQRVTQGPVSATVEVTSPTGFVQSHVLEDVSQSVRHVKLGPTEMWRTEQVSYGGPTSPVVEVSEDFSEAVSSEGASRSVRHVTLGPRQNRVSTEVIFRGSVPTGQETGDTGEPDPAALSVEADISGSGRMPGSQQAHNEKETPFPGPISGAAQVGSNFSTEGSVGTQTFVRHLQLGSREGFREEIQFIAPIPDRAEWGEEDSGYTRVSLGRSTSIQHIDIVPQRYQASKQVAPQTLGFRDSEGVVLVERSAGMTQATHNFTSDREILKKEENTFQRVISGSPPDSVGDTGAEVTENISRSFRHIQIGPTEEDPSEYIVTSGPLSKTFVLDSSVASPGPGGGADGSSTPCHIALGPKETSFTFQMGVSDTRAIRSWTRDTGSEVEAHSVSHHGGWRVAHSRDEQSASTSSQASAGDAHQARGEKGTEQAGFDKTVQLQRMVDQRSVASDEKKVALLYLDNEEEEEGEGWF