wanglab/gogpt-training-data huggingface dataset:
Protein: C-X-C motif chemokine 3 (Cytokine-induced neutrophil chemoattractant 2) (CINC-2) (Macrophage inflammatory protein 2-alpha/beta) (MIP2-alpha/beta) (Q10746)
Organism: Rattus norvegicus (Rat)
Function: Ligand for CXCR2 (By similarity). Has chemotactic activity for neutrophils. May play a role in inflammation and exert its effects on endothelial cells in an autocrine fashion.
Subcellular location: Secreted.
Interaction partners:
- C-X-C chemokine receptor type 2
- C-X-C chemokine receptor type 1
- Growth-regulated alpha protein
- C-X-C motif chemokine 2
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor Jun
- Transcription factor p65
- Interleukin-1 beta
- C-X-C chemokine receptor type 5
- Interleukin-1 alpha
Sequence:
MAPPTRRLLNAALLLLLLLMATSHQPSGTVVARELRCQCLKTLPRVDFENIQSLTVTPPGPHCTQTEVIATLKDGQEVCLNPQAPRLQKIIQKLLKSDKSS
Protein: GH10911p (Q8SXB5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVASAQRGDRECHVVVLLEDDMVEWDEEFPPQMGEEYCQTVHSTAMHRFFKYIENRDVAKQVMKDRGLKKIRCGIEGYPTHKEKIRRRPGGRAEVIYSYVQRPFIHMSWEKEEAKSRHVDFQCVKSKSVTNLAEANADPPLELDASGNPIPPIAVANPHPNNAELAAGMAVAPAAIGVAGPAVVVAVDEAAGGVVMLNELDQAAIAVAVGIVDENM
Protein: Fibroblast growth factor 21 (FGF-21) (Q9JJN1)
Organism: Mus musculus (Mouse)
Function: Stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Activity probably requires the presence of KLB. Regulates systemic glucose homeostasis and insulin sensitivity.
Subcellular location: Secreted {ECO:0000269|PubMed:30605666}.
Interaction partners:
- Beta-klotho
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 4
- Fibroblast growth factor receptor 2
- Klotho
- Fibroblast growth factor receptor 3
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 3
- Insulin-like growth factor 1 receptor
- Platelet-derived growth factor receptor beta
Sequence:
MEWMRSRVGTLGLWVRLLLAVFLLGVYQAYPIPDSSPLLQFGGQVRQRYLYTDDDQDTEAHLEIREDGTVVGAAHRSPESLLELKALKPGVIQILGVKASRFLCQQPDGALYGSPHFDPEACSFRELLLEDGYNVYQSEAHGLPLRLPQKDSPNQDATSWGPVRFLPMPGLLHEPQDQAGFLPPEPPDVGSSDPLSMVEPLQGRSPSYAS
Protein: Neck protein (H9C199)
Organism: Pectobacterium phage ZF40 (Bacteriophage ZF40)
Interaction partners:
Sequence:
MKLNVETRGGNKIAQKLKEIQDRVMAKRRVLVGLPAGSGNYEDGAPIAVIGAVQEFGSADGRVPERSFLRVPIRQNQDSIKKAFRALTGAVARGEITAFQMLDQIGARAAGFCQEAIEAGIQPANADSTIKAKGSSTPLIVHGFLKGKITHVVED
Protein: Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10] (Q8IRY7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Effector of the programmed cell death (PCD) activators rpr, grim and hid. May play an apoptotic role in the germline as well as soma. Fadd interacts with Dredd to promote cleavage of Dredd and is necessary and sufficient for enhancing Dredd-induced apoptosis. Plays a role in the innate immune response. Required for resistance to Gram-negative bacterial infection. Diap2-mediated ubiquitination of Dredd is critical for processing of imd and rel and the subsequent expression of antimicrobial genes such as DptA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10934188, ECO:0000269|PubMed:9740659}.
Interaction partners:
- Fas-associated death domain protein
- Death-associated inhibitor of apoptosis 2
- Protein immune deficiency
- AT03047p
- Nuclear factor NF-kappa-B p110 subunit
- Apoptosome protein Dark
- BG1
- Cytochrome c-2
- Cytochrome c-1
- Caspase drICE
Sequence:
MAGSNLLIHLDTIDQNDLIYVERDMNFAQKVGLCFLLYGDDHSDATYILQKLLAMTRSDFPQSDLLIKFAKSRPETWRRHLVEALCIIGARKVLRRLGFCWQELRMHYLPHIAGITLHVHPLLKSLYRMCEELSLVQSGRLLLDVREKVESQQAGDPLRFYDPAYLEIFLLDWLTRRSIKLGDINAAGSDVQLLVGHLKSNGLQAQANLLKDTIISNAPEPDAAGTAAMAVKQEIESDNQQSYCSTQIDALKLTRENAGIALIINQQKFHRNVSRDNMKFLSPDPLRRRDGTDVDKERLIEVFSSMGYNVEAYDNVDHMGIIERIRSACDRSLVRDSLVVFILSHGFEEAVYASNSIAMKITDIEDLLCSYDTLYYKPKLLIIQACQEKLVHKKKPNELFRIDVTTVSPDQHIDMLRAMSTVNGYAALRHTQTGSWFIGSLCDAIDRRSASEHIADILTIVTNEVSKKRGSNDESMVPNVKSTFRQHVYFPPRL
Protein: Protein argonaute MEL1 (Protein MEIOSIS ARRESTED AT LEPTOTENE 1) (OsMEL1) (Q851R2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Essential for the progression of premeiotic mitosis and meiosis during sporogenesis. Regulates the cell division of premeiotic germ cells, the proper modification of meiotic chromosomes, and the faithful progression of meiosis, probably via small RNA-mediated gene silencing. May be involved in histone H3 'Lys-9' demethylation in the pericentromeric region.
Subcellular location: Nucleus, nucleolus {ECO:0000305}.
Interaction partners:
- Os02g0152700 protein
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase subunit
- Endoribonuclease Dicer homolog 4
- Endoribonuclease Dicer homolog 3b
- Endoribonuclease Dicer homolog 1
- Endoribonuclease Dicer homolog 3a
- Endoribonuclease Dicer homolog 2a
- Endoribonuclease Dicer homolog 2b
- Os03g0121901 protein
Sequence:
MAYRGGGRGGRGGEQRPPYSGRGDVPGRGGGGGGGGAPPYRPASGFVWPPPGMTPRPGPPQPQYPRPGPPAVVYGAPMPAAHHQGAYQPGGVYRAPSPGVPVIGGYARSTPVTIRAPPPSHSSAPAPYQPAAAAPAPSSSSTAPSATALAKEFEQKLFVSETALAPPAAVASAAAAPAGEASVESDKDLAPVSKKGLAHPARPGFGAAGKKVMIRANHFLVNVADNNLFHYDVSINPESKSRATNREVLNELIKLHGKTSLGGKLPAYDGRKSLYTAGSLPFESEEFVVKLIDPEKKDKERAEREYKITIRIAGRTDLYHLQQFLLGRQRDMPQETIQVLDVVLRESPSWNYVTVSRSFFSTQFGHRGDIGEGLECWRGYYQSLRPTQMGLSLNIDISATSFFKPVTVIQFVEEFLNIRDTSRPLSDRDRVKIKKALRGVRIETNHQEDQIRRYKITGITPIPMSQLIFPVDDNGTRKTVVQYFWDRYNYRLKYASWPCLQSGSDSRPVYLPMEVCKIVEGQRYSKKLNDKQVTNILRATCQRPQQREQSIHEMVLHNKYTEDRFAQEFGIKVCNDLVSVPARVLPPPMLKYHDSGREKTCAPSVGQWNMINKKMINGGTVDNWTCLSFSRMRPEEVQRFCGDLIQMCNATGMSFNPRPVVDVRSTNPNNIENALRDVHRRTSELLAREGKGGLQLLIVILPEVSGSYGKIKRVCETDLGIVSQCCLPRHASRPNKQYLENVALKINVKVGGRNTVLERAFIRNGIPFVSEVPTIIFGADVTHPPPGEDSASSIAAVVASMDWPEITKYRGLVSAQPHRQEIIEDLFSVGKDPVKVVNGGMIRELLIAFRKKTGRRPERIIFYRDGVSEGQFSHVLLHEMDAIRKACASLEEGYLPPVTFVVVQKRHHTRLFPEVHGRRDMTDKSGNILPGTVVDRQICHPTEFDFYLCSHAGIQGTSRPTHYHVLYDENHFTADALQSLTNNLCYTYARCTRAVSVVPPAYYAHLAAFRARYYVEGESSDGGSTPGSSGQAVAREGPVEVRQLPKIKENVKDVMFYC
Protein: Zinc finger C-x8-C-x5-C-x3-H type family protein (F4K9A6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSKPEETSDPNPTGPDPSRSSSDEVTVTVADRAPSDLNHVSEELSDQLRNVGLDDSAKELSVPISVPQGNVETDSRALFGSDQKEEEEGSEKRMMMVYPVRPDSEDCSFYMRTGSCKYGSSCKFNHPVRRKLQDLKFLGSMRTRNGKEYIGRERVRERDEDVENPKLMECKYYFRTGGCKYGESCRFSHMKEHNSPASVPELNFLGLPIRPGEKECPFYMRNGSCKFGSDCKFNHPDPTAIGGVDSPLYRGNNGGSFSPKAPSQASSTSWSSTRHMNGTGTAPFIPSMFPHSRGVTPQASDWNGYQASSAYPPERSPLAPSSYQVNNSLAETSSFSQYQHQMSVEEFPERPDQPECTYYLKTGDCKFKYKCKYHHPKNRLPKQAAFSFNDKGLPLRPDQSMCTHYSRYGICKFGPACRFDHSIPPTFSPSSSQTVEARQVGANGNEDDSWH
Protein: Serine protease hepsin (EC 3.4.21.106) (Transmembrane protease serine 1) [Cleaved into: Serine protease hepsin non-catalytic chain; Serine protease hepsin catalytic chain] (P05981)
Organism: Homo sapiens (Human)
Function: Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2. Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1885621}; Single-pass type II membrane protein {ECO:0000269|PubMed:1885621}. Apical cell membrane {ECO:0000269|PubMed:26673890}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Immunoglobulin lambda-like polypeptide 5
- Kunitz-type protease inhibitor 1
- Hepatocyte growth factor-like protein
- Hepatocyte growth factor
- Alpha-methylacyl-CoA racemase
Sequence:
MAQKEGGRTVPCCSRPKVAALTAGTLLLLTAIGAASWAIVAVLLRSDQEPLYPVQVSSADARLMVFDKTEGTWRLLCSSRSNARVAGLSCEEMGFLRALTHSELDVRTAGANGTSGFFCVDEGRLPHTQRLLEVISVCDCPRGRFLAAICQDCGRRKLPVDRIVGGRDTSLGRWPWQVSLRYDGAHLCGGSLLSGDWVLTAAHCFPERNRVLSRWRVFAGAVAQASPHGLQLGVQAVVYHGGYLPFRDPNSEENSNDIALVHLSSPLPLTEYIQPVCLPAAGQALVDGKICTVTGWGNTQYYGQQAGVLQEARVPIISNDVCNGADFYGNQIKPKMFCAGYPEGGIDACQGDSGGPFVCEDSISRTPRWRLCGIVSWGTGCALAQKPGVYTKVSDFREWIFQAIKTHSEASGMVTQL
Protein: Chitinase ChiA (EC 3.2.1.14) (A5FB63)
Organism: Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae)
Function: Major extracellular chitinase, which is essential for chitin utilization.
Subcellular location: Secreted {ECO:0000269|PubMed:24363341}. Note=Translocated across the cytoplasmic membrane via the Sec system, and across the outer membrane via the type IX secretion system (T9SS).
Interaction partners:
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- Beta-N-acetylglucosaminidase-like protein Glycoside hydrolase family 20
- chitinase
- Peptidase family M4, thermolysin
Sequence:
MKHYYRLLFLLLFPLLASAQPAHGKKVVGYYAQWSIYARDFNVPKIDGSKLTHLNYSFYGTTYDPAHPENTKLKCLDTYADFEHMEGGIPWDAPVKGNFYDLMKLKQKYPHLKILISVGGWTKGQDLSPIAASPVARAALAADMANFIVTYPFIDGFDIDWEYPLSGGTDGTEIVNGMPVPPQKYSPDDNKNLVLLLKAMRQAMPNKLVTIAAGNNVRNVSKQYLGPNNRAQYGMTEDISTYCDYITYFGYDFGGNWYDKTCYNAPLYASGNPNDPLYGATQSESLDELTNQYLNVIGFPANKLIMGLPFYGKKFDNVAANSTNGLFVAAPRYIVPGCTNPQNPTGTWDGSGACEKSGSIEICDLVGNPVTNSHAYLDPNTMMVTPSAASAGWVRYFDNTTKVPYLYNSTLKQFISYEDKQSMDLKVQYIKSRNLAGGMIWELSQDTRGSIPNSLLNQVDTSFGSVVPGTVSISGSVKNGSALVTDVTVELRNASNAVIQTVVSANGNFAFNNLTSGQNYSLTALKATYTFTPVTLVNVTVNQTAVVINGTQPTYTVSGTVLDGSTPVSGVTVTAVSGSTTLTAVSNASGVYSIAGLTAGLNFTVTAAKSGFSYAPASTVYNAIDSNKTLNFTQGAPVVNYTVSGTVLNSTTPVSGVTVTASFTGGSYAAVTNASGTYSLSLPSGGNYTVTAALTGQTFTPASTVYSNLNANKTLNFTQDVVVSTSKISGTVKNGTNPVAGAKVELVLPWTDNTHNWKSVIATTDAQGKYSFDNSVVDGYTQVLSLKLNSWQNGEVAYYPNNLANFAVPANPTVYNFNTSSTAKSALAAAANLISGTVKNGTTPVAGAKVEIVLPWTDNTHNWKSVLATTDASGNYSFDNSVVAGYTQILSLKLNGWENGDVTYYPNNLANFAVPTTPTIYNFNRQAVVATKPVVTITAPTASAIAINLGSAINFVASVGLSAVDATTISSVVFSLDGQSLSTANSSGTYTAAWTPAANQFSLSHTLTVTATASNGTTDSKTYSFTLTCSGANCPNALPVITWNSPSNTTVYQNTFQVVPISVTAVDSDGTVSGVTITINGGTFNMTAGTNNTYTYNFTPSAYQDYPVVIKATDNKSGVTTLNNTIKIATVSTNRFIPLPSKIILGYAHSWENAGAPFLYFSQMVGSKFNVVDYSFVETVNRDGYTPILTTNDTRYLTNGVFNKQLLKNDIKSLRDSGVPVIVSIGGQNGHVVLDNVTQKNIFVNGLKAIIDEYQFDGVDIDFEGGSMNFNAGGLRDISYAGISAYPRLKNVVDAFKELKAYYGPGFLLTAAPETQYVQGGYTTYTDTFGSFLPIIQNLRNELDLLAVQLYNTGGENGLDGQYYGTAKKSNMVTALTDMVIKGYNIASTGMRFDGLPASKVLIALPACPSAAGSGYLTPTEGINAMHYLRTGTTFSGRTYTMQPGGPYPSLRGLMTWSVNWDASSCGNSSELSKAYAAYFASQTAAKTLVLDDISAKSNATIAYFKNNALSVTNENEDIAQVDVFNVLGQNLVSHRNVQNNKEVLLHNQSFSSKQLFLVVVTDKAGNKKSFKVMNFLN
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (Q63745)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEQVEILRRFIQRVQAMKSPDHNGEDNFARDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPRAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQLYEIHGAQKITDGNEISTGNMVSSIDSEKQDSPPPKPPRTRSCLVEGDAKEEILQPPEPHPVPPILTPSPPSAFPTLHCVARQ
Protein: Noxa (Phorbol-12-myristate-13-acetate-induced protein 1) (Q0GKC8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Bcl-2-like protein 1
- Apoptosis regulator Bcl-2
- Apoptosis regulator Bcl-2
- BCL2-interacting killer
- BCL2-binding component 3
Sequence:
MAKKEQTAVVECAQQLRNIGDLLNWKYKLLELIVTLQKIQMEGKR
Protein: Anoctamin-9 (Transmembrane protein 16J) (P86044)
Organism: Mus musculus (Mouse)
Function: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide. Does not exhibit calcium-activated chloride channel (CaCC) activity (By similarity). Can inhibit the activity of ANO1 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:29604966, ECO:0000269|PubMed:36330924}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:36330924}. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane. {ECO:0000250|UniProtKB:A1A5B4}.
Interaction partners:
Sequence:
MQDDESSQIFMGPEGDQLPLVEMGSCKPEASDQWDCVLVADLQTLKIQKHAQKQLQFLENLESNGFHFKMLKDQKKVFFGIRADSDVIDKYRTLLMNPEDSGSRDEQSFNIATTRIRIVSFVVNNKLKPGDTFEDLVKDGVFETMFLLHKGEQNLKNIWARWRNMFEPQPIDEIREYFGEKVALYFTWLGWYTYMLVPAAVVGLIVFLSGFALFDSSQISKEICSANDIFMCPLGDHSHRYLRLSEMCTFAKLTHLFDNEGTVLFAIFMALWATVFLEIWKRKRAHEVQSWKLYEWDEEEEEMALELINSPHYKLKDHRHSYLSSTIILILSLFMICLMIGMAHVLVVYRVLAGALFSSLVKQQVTTAVVVTGAVVHYIIIVIMTKVNKYVALKLCKFEESGTFSEQERKFTVKFFILQFFAHFSSLIYIAFILGRINGHPGKSTRLAGLWKLEECHLSGCMMDLFIQMAIIMGLKQTLSNCVEYLCPLLAHKWRLMWASKHGHMSKDPELKEWQRNYYMNPINTFSLFDEFMEMMIQYGFTTIFVAAFPLAPLLALFSNLVEIRLDAIKMVRLQRRLVPRKAKDIGTWLQVLETIGVLAVIANGMVIAFTSEFIPRVVYKYHYGPCRTNRTFTDDCLTNYVNHSLSVFYTKHFNDHSRMEGQENVTVCRYRDYRNEHDYNLSEQFWFILAIRLTFVILFEHFALCIKLIAAWFVPDVPQKVKNEVLQEKYDRIRHRMRFSSRSTDV
Protein: Multiple epidermal growth factor-like domains protein 9 (Multiple EGF-like domains protein 9) (Epidermal growth factor-like protein 5) (EGF-like protein 5) (Q8BH27)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MNGGAERAMRSLPSLGGLALLCCAAAAAASTASAGNVTGGGGAEGQVVPSPSPGLRDQASSPFPKTAAPTAQAPRTGPPRTTVRKTGATTPSAGSPEIIPPLRTSAQPAATPFPALDLSPATPSEDGHTPTTESPPSRPAPTTLASTVGQPPTTSVVTTAQASSTPGTPTAESPDRSSNSSGVPPTAPVTEAPTSPPPEHMCNCSEVGSLDVKRCNQTTGQCDCHVGYQGLHCDTCKEGFYLNHTVGLCLPCHCSPHGAVSILCNSSGNCQCKVGVTGSMCDKCQDGHYGFGKTGCLPCQCNNRSDSCDVHTGACLNCQENSKGEHCEECKEGFYPSPDAAKQCHRCPCSAVTSTGNCTIESGELEPTCDQCKDGYTGQNCNKCENGYYNSDSICTQCECHGHVDPIKTPKICKPESGECINCLHNTTGFWCEKCLEGYVRDLQRNCIKQEVIVPTPEGSTILVSNASLTTSVPTPVINSTFAPTTLQTIFAVSSSENSTSALADVSWTQFNIIILTVIIIVVVLLMGFVGAVYMYREYQNRKLNAPFWTIELKEDNISFSSYHDSIPNADVSGLLEDDANEVAPNGQLTLTTPIHNYKA
Protein: Leucine carboxyl methyltransferase 1 (EC 2.1.1.233) (A2RTH5)
Organism: Mus musculus (Mouse)
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Protein phosphatase methylesterase 1
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
Sequence:
MASSSRESSFSSCSSSCDLDDEGVRGTCEDASLCKRFAVSIGYWHDPYIEHLVRQSKERKAPEINRGYFARVHGVSQLIKAFLRKTECHCQILNLGAGMDTTFWKLKDEGLLPNKYFEVDFPMIVTRKLLTIKSKPLLFRPIMELHPEDTLQMDSHMLDSKRYAIIGADLRDLSELEEKLKKCNMNTQLPTLLITECVLVYMTPEQSANLLKWAASSFETAMFINYEQVNMDDRFGQIMIENLRRRSCDLAGVETCKSLESQKERLLLNGWETASAVNMMELYSGLPRAEVNRIESLEFLDEMELLEQLMRHYCLCWATRGGQELGLKEITY
Protein: V-type proton ATPase subunit G (A0A0G2KAG3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
IRGKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLTQLLGMVCDVRPQVHPNYRITV
Protein: Probable C-terminal domain small phosphatase (EC 3.1.3.16) (Developmental gene 1148 protein) (Q9XYL0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May function as a phosphatase involved in the regulation of cell growth and differentiation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit pprA
- Mitochondrial import inner membrane translocase subunit tim17
- Transmembrane protein
- 2-
Sequence:
MNSSPITQVSNPNDSLNHSSTNLIPSSHNSLNNYPQKSVKGNRKKKGSIINKLFCCFVPSNDQNNGNNINTDNGASNNDKLQQQKQYNQQQQQQYNQHQQQQQQQQQQQQYINKDSSQQNGEIPLMVPMIPRHVGLKTLVLDLDETLVHSSFKPVHNPDFIVPVEIEGTIHQVYVVKRPFVDDFLRAIAEKFEIVVFTASLAKYADPVLDFLDTGRVIHYRLFRESCHNHKGNYVKDLSRLGRDLKSTIIVDNSPSSYLFHPENAIPIDSWFDDKDDRELLDLLPLLDDLIKVEDVRLVLDESRNN
Protein: E3 ubiquitin-protein ligase ZNRF3 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase ZNRF3) (Zinc/RING finger protein 3) (Q5SSZ7)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that acts as a negative regulator of the Wnt signaling pathway by mediating the ubiquitination and subsequent degradation of Wnt receptor complex components Frizzled and LRP6. Acts on both canonical and non-canonical Wnt signaling pathway. Acts as a tumor suppressor in the intestinal stem cell zone by inhibiting the Wnt signaling pathway, thereby resticting the size of the intestinal stem cell zone. Along with RSPO2 and RNF43, constitutes a master switch that governs limb specification (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9ULT6}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- R-spondin-2
- R-spondin-1
- Leucine-rich repeat-containing G-protein coupled receptor 4
- Leucine-rich repeat-containing G-protein coupled receptor 5
- R-spondin-4
- R-spondin-3
- Frizzled-8
- Frizzled-1
- Frizzled-4
- Frizzled-5
Sequence:
MRPRSGGRPGAPGRRRRRLRRGPRGRRLPPPPPLPLLLGLLLAAAGPGAARAKETAFVEVVLFESSPSGDYTTHTTGLTGRFSRAGAMLSAEGEIVQMHPLGLCNNNDEEDLYEYGWVGVVKLEQPELDPKPCLTVLGKAKRAVQRGATAVIFDVSENPEAIDQLNQGSEDPLKRPVVYVKGADAIKLMNIVNKQKVARARIQHLPPRQPTEYFDMGIFLAFFVVVSLVCLILLVKIKLKQRRSQNSMNRLAVQALEKMETRKFNSKSKGRREGSCGALDTLSSGSTSDCAICLEKYIDGEELRVIPCTHRFHRKCVDPWLLQHHTCPHCRHNIIEQKGNPGAVCVETSNLTRGRQPRVTLPVHYPGRVHRTNAIPAYPTRTSMDSHGNPVTLLTMDRHGEQNLYSPQTPTYVRGYPPLHLDHTLAPHRCSLEHRAYSPAHPFRRPKFSSRSFSKAACFSQYETMYQHYYFQGLSYPEQEGQTIPSVTPRGQSRAFPPSGASSLLFPTMVHVAPPTHVESGSTSSFSCYHGHRSVCSGYLADCPGSDSSSNSSGQCRCSSSDSVVDCTEVSNQGVYGSCSTFRSSLSSDYDPFIYRSRGPAVHLEGSPPPEELPAGHSQSAGRGEPWLGPASPSGDQLSTCSLEMNYSSNSSLEPRGPNSSTSEVGLEVSPGAALDLRRTWKGGPEGPSCACCFEPQPFPPGSGIETSAGGSSLFLGPRLLEDCNPPSGEPQLGSSQGLYGLHSDHYPRTDGVKYEGLPCCFYEEKQVAHSAGRGNGCYTEDYSVSVQYTLTEEPPPSCYAGPRDLSQRIPIIPEDVDCDLGLPQDCHGMHNHSPWGGALSLDVPRLHWSLGTTREEEQAPCYQAEVQPGCSPEEAGASRASLSSAPQDTQESHALAAEASGPGSGPGIGTGA
Protein: pH-response transcription factor pacC/RIM101 (Q4WY67)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including pacC itself) and represses transcription of acid-expressed genes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q00202}. Nucleus {ECO:0000250|UniProtKB:Q00202}. Note=Cytoplasmic at acidic ambient pH, and nuclear in its processed form at alkaline ambient pH. {ECO:0000250|UniProtKB:Q00202}.
Interaction partners:
- Probable DNA-binding protein creA
- Secondary metabolism regulator laeA
- PH response protein PalF
- Calpain-like protease PalBory
- Developmental and secondary metabolism regulator veA
- PH signal transduction protein PalA, putative
- Vacuolar protein-sorting protein bro1
- C2H2 finger domain transcription factor crzA
- C2H2 type master regulator of conidiophore development brlA
- Xylanolytic transcriptional activator xlnR
Sequence:
MSEHQDTATNNNTTASPSATAAPMPAPISQEQPSSQPAATTPAPVSTSTPPASVTATAAAATAAVSAPQANGTPPSDEQLSCLWQGCSEKCPSAEALYDHICERHVGRKSTNNLNLTCQWGSCRTTTVKRDHITSHIRVHVPLKPHKCEFCGKAFKRPQDLKKHVKTHADDSVLVRSPEPGARNPDMMFHGAGKGYAAAAHYFEPSLNAVPSQGYAHGAPQYYSSHPPHQPSNPSYGNVYYALNHGHDGHASYESKKRGYDALNEFFGDLKRRQFDLHSYAAVGQRLLGLQNLSLPILTGGPLPEYQPMPAPVAVGGGYGPGGHGAPVYHLPPMSNIRTKNDLINIDQFLQQMQDTIYENDDHVAAAGVAQPGAHYVHGGMSYRTTHSPPTQLPPSHAVATTSASTSMSNPATHSPPTGTPALTPPSSAQSYTSARSPISISSAHRVSPPHHDGGSGMYPRLPSTTMADSLAGGYPTASSAAPPSTLSGIFDDDRRRYTGGTLQRARPEERRPSIQMDTSHDGKEDGERTPTGKARSSGSDSPVRISANLIDPALHSSSPSDAEAALRTAQAATEVADRADSQWVEKVRLLEYLRSYIASRLERGEYDSDSDDHASAAASPVIKHDGHMDGVESSHKPITAEETSAPPAAKAESNHGVMYPTLHGLDGDEDTKMHH
Protein: Small ribosomal subunit protein uS9m (28S ribosomal protein S9, mitochondrial) (MRP-S9) (S9mt) (P82933)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379}.
Interaction partners:
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS10m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS35
- Large ribosomal subunit protein bL20m
Sequence:
MAAPCVSYGGAVSYRLLLWGRGSLARKQGLWKTAAPELQTNVRSQILRLRHTAFVIPKKNVPTSKRETYTEDFIKKQIEEFNIGKRHLANMMGEDPETFTQEDIDRAIAYLFPSGLFEKRARPVMKHPEQIFPRQRAIQWGEDGRPFHYLFYTGKQSYYSLMHDVYGMLLNLEKHQSHLQAKSLLPEKTVTRDVIGSRWLIKEELEEMLVEKLSDLDYMQFIRLLEKLLTSQCGAAEEEFVQRFRRSVTLESKKQLIEPVQYDEQGMAFSKSEGKRKTAKAEAIVYKHGSGRIKVNGIDYQLYFPITQDREQLMFPFHFVDRLGKHDVTCTVSGGGRSAQAGAIRLAMAKALCSFVTEDEVEWMRQAGLLTTDPRVRERKKPGQEGARRKFTWKKR
Protein: NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 4L) (NADH-plastoquinone oxidoreductase subunit 4L) (Q6ENA5)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01456}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01456}.
Interaction partners:
- NAD
- NAD
- NAD
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase chain 4
- Photosystem I iron-sulfur center
- NAD
- NAD
- NADH:quinone oxidoreductase/Mrp antiporter transmembrane domain-containing protein
- NAD
Sequence:
MMFEHVLFLSVYLFSIGIYGLITSRNMVRALICLELILNSINLNLVTFSDLFDSRQLKGDIFAIFVIALAAAEAAIGLSILSSIHRNRKSTRINQSNFLNN
Protein: Evasin P1127 (A0A0K8RJ67)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5 and CXCL8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MEAKTFAFLEIAMFIALGIQTFVAVTDAAGKDDEHFSVDYCGMNCTQQEDGSWTACSGRNGECRCYHESGKRSGLCLSTTYIDFSEYGNLSDSDIAAASPRLSMKESH
Protein: Fms related receptor tyrosine kinase 3 ligand (A0A1W2Q636)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTVLAPAWSPNSSLLLLLLLLSPCLRGTPDCYFSHSPISSNFHMRISELTDYLLKDYPVTVAINLQDEKHCKALWSLFLAHRWIEQLKTVAGSKMQKLLEDVNTEIHFVTSCTFQPLPECLRFVQTNISHLLQDTCSQLLALKPCIGKACQNFSRCLETPPPCFPQRVLEP
Protein: Lipopolysaccharide assembly protein B (Lipopolysaccharide regulatory protein) (P0AB58)
Organism: Escherichia coli (strain K12)
Function: Modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis. May act by modulating the proteolytic activity of FtsH towards LpxC. May also coordinate assembly of proteins involved in LPS synthesis at the plasma membrane.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00994, ECO:0000269|PubMed:24187084, ECO:0000269|PubMed:24722986}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00994, ECO:0000269|PubMed:24187084}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00994, ECO:0000269|PubMed:24187084}.
Interaction partners:
- Lipopolysaccharide assembly protein A
- Inner membrane protein YejM
- UDP-3-O-acyl-N-acetylglucosamine deacetylase
- ATP-dependent zinc metalloprotease FtsH
- Lipid A biosynthesis myristoyltransferase
- Orotidine 5'-phosphate decarboxylase
- UDP-2,3-diacylglucosamine hydrolase
- Outer membrane protein TolC
- Z-ring associated protein G
- Phosphatidylglycerophosphatase B
Sequence:
MLELLFLLLPVAAAYGWYMGRRSAQQNKQDEANRLSRDYVAGVNFLLSNQQDKAVDLFLDMLKEDTGTVEAHLTLGNLFRSRGEVDRAIRIHQTLMESASLTYEQRLLAIQQLGRDYMAAGLYDRAEDMFNQLTDETDFRIGALQQLLQIYQATSEWQKAIDVAERLVKLGKDKQRVEIAHFYCELALQHMASDDLDRAMTLLKKGAAADKNSARVSIMMGRVFMAKGEYAKAVESLQRVISQDRELVSETLEMLQTCYQQLGKTAEWAEFLQRAVEENTGADAELMLADIIEARDGSEAAQVYITRQLQRHPTMRVFHKLMDYHLNEAEEGRAKESLMVLRDMVGEKVRSKPRYRCQKCGFTAYTLYWHCPSCRAWSTIKPIRGLDGL