wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon gamma (IFN-gamma) (P01580)
Organism: Mus musculus (Mouse)
Function: Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation. Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation. Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription. Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits. In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading. Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference. Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (By similarity). Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01579}.
Interaction partners:
- Ifngr2 protein
- Interferon gamma receptor 1
- Tyrosine-protein kinase JAK2
- Interleukin-1 beta
- Granulocyte-macrophage colony-stimulating factor
- Granulocyte colony-stimulating factor
- Interferon alpha/beta receptor 1
- Interleukin-10
- Interleukin-3
- Interleukin-1 alpha
Sequence:
MNATHCILALQLFLMAVSGCYCHGTVIESLESLNNYFNSSGIDVEEKSLFLDIWRNWQKDGDMKILQSQIISFYLRLFEVLKDNQAISNNISVIESHLITTFFSNSKAKKDAFMSIAKFEVNNPQVQRQAFNELIRVVHQLLPESSLRKRKRSRC
Protein: Lymphotactin (C motif chemokine 1) (Cytokine SCM-1) (Lymphotaxin) (Small-inducible cytokine C1) (P47993)
Organism: Mus musculus (Mouse)
Function: Chemotactic activity for lymphocytes but not for monocytes or neutrophils. In thymus, mediates medullary accumulation of thymic dendritic cells and contributes to regulatoy T cell development, playing a role in self-tolerance establishment.
Subcellular location: Secreted.
Interaction partners:
- Chemokine XC receptor 1
- C-C motif chemokine 5
- C-X-C motif chemokine 10
- C-X-C motif chemokine 9
- C-C chemokine receptor type 7
- C-C chemokine receptor type 5
- C-C motif chemokine 28
- Stromal cell-derived factor 1
- CX3C chemokine receptor 1
- C-C chemokine receptor type 1
Sequence:
MRLLLLTFLGVCCLTPWVVEGVGTEVLEESSCVNLQTQRLPVQKIKTYIIWEGAMRAVIFVTKRGLKICADPEAKWVKAAIKTVDGRASTRKNMAETVPTGAQRSTSTAITLTG
Protein: Spliced leader RNA PSE-promoter transcription factor, putative (Q57WR3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRSSANFFLANSSSGGLSKYRPRFRPRRLVLPVNPSDVHSISRANNPMYAKYQEGIRLRRRAERRGVIALSFVPSERSVGDAFRIMVEVCEKEGFFESKSSTPNYLRKVRELIKRAETELGTGERVKNTSANPSFYDIGLSEARDLSRNADKSRHAEGNIETREIDSLWSLLNATPLDSPVHGILALRGKALLESIIANTVQQQYPRLRSKHLQEIIHECCSLLACGRAAFRLGFADVCGINGEINMWRELNVLTERFNTARHKAAAHLQRVEKGVTQQRRWYWRGVLRSSSKRLKQFPVRQGDLLPRMEWIRESVYAFVAFVDLAEKSGDNVRVVPLIENLFCGQISSFVSTNQTLKKAHRMVDMLSKARIECDATTEKEKIQQLESLSTDIENELAALEQFTDDELGVMSRVVHPLNARSDNRKEQFSSSGGAHAVQSLRDDIFDDYRVTRHNKEAPPMVINCMRPQNALKEAQIILRYDPNVSETLSSSPIDVDQVIRRVTEVHETNSYATLYNFQQFRQVEYTVCRLYAGKRCIGQGKGETLMEAVNEAAQHTLLNYYLKDVSNANSREKEEDAVTEAFSATPPELTEVRVKEATEEEVIF
Protein: Terminal nucleotidyltransferase 5C (EC 2.7.7.19) (Q5SSF7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of one adenosine molecule from an ATP to an mRNA poly(A) tail bearing a 3'-OH terminal group and enhances mRNA stability and gene expression. Can also elongate RNA oligos ending with uridine molecule, provided that the sequence is adenosine-rich (By similarity). Mainly targets mRNAs encoding endoplasmic reticulum-targeted protein.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5VWP2}. Cytoplasm {ECO:0000269|PubMed:28931820}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5VWP2}. Note=Recruited into the centrosome through its interaction with PLK4. {ECO:0000250|UniProtKB:Q5VWP2}.
Interaction partners:
- Exosome complex exonuclease RRP44
Sequence:
MAEEGSSTKDSESFSVLNWDQVSRLHEVLTEVVPIHGRGNFPTLEITLKDIVQTVRGRLEEAGINVQDVRLNGSAAGHVLVKDNGLGCKDLDLIFHVALPTEAEFQLVRDVVLCSLLNFLPEGVNKLKISPVTLKEAYVQKLVKVCTDTDRWSLISLSNKNGRNVELKFVDSIRRQFEFSVDSFQIILDSLLFFYDCSGNPISEHFHPTVIGESMYGDFEEAFDHLQNRLIATKNPEEIRGGGLLKYSNLLVRDFRPADQEEIKTLERYMCSRFFIDFPDILEQQRKLETYLQNHFSDEERSKYDYLMILRRVVNESTVCLMGHERRQTLNLISLLALRVLAEQNIIPSATNVTCYYQPAPYVSDGNFNNYYIAHPPITYSQPYPTWLPCN
Protein: Leukocyte surface antigen CD47 (Antigenic surface determinant protein OA3) (Integrin-associated protein) (IAP) (Protein MER6) (CD antigen CD47) (Q08722)
Organism: Homo sapiens (Human)
Function: Adhesive protein that mediates cell-to-cell interactions. Acts as receptor for thrombospondin THBS1 and as modulator of integrin signaling through the activation of heterotrimeric G proteins. Involved in signal transduction, cardiovascular homeostasis, inflammation, apoptosis, angiogenesis, cellular self-renewal, and immunoregulation. Plays a role in modulating pulmonary endothelin EDN1 signaling. Modulates nitrous oxide (NO) signaling, in response to THBS1, hence playing a role as a pressor agent, supporting blood pressure (By similarity). Plays an important role in memory formation and synaptic plasticity in the hippocampus (By similarity). Receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation. Positively modulates FAS-dependent apoptosis in T-cells, perhaps by enhancing FAS clustering (By similarity). Plays a role in suppressing angiogenesis and may be involved in metabolic dysregulation during normal aging. In response to THBS1, negatively modulates wound healing (By similarity). Inhibits stem cell self-renewal, in response to THBS1, probably by regulation of the stem cell transcription factors POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 (By similarity). May play a role in membrane transport and/or integrin dependent signal transduction. May prevent premature elimination of red blood cells (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:39121194, ECO:0000269|PubMed:7691831}; Multi-pass membrane protein {ECO:0000269|PubMed:7691831}.
Interaction partners:
- Signal-regulatory protein gamma
- Thrombospondin-1
- Tyrosine-protein phosphatase non-receptor type substrate 1
- Lysosome membrane protein 2
- Platelet glycoprotein 4
- Scavenger receptor class B member 1
- Signal-regulatory protein beta-1
- Ammonium transporter Rh type A
- Glycophorin-B
- Cell surface glycoprotein CD200 receptor 1
Sequence:
MWPLVAALLLGSACCGSAQLLFNKTKSVEFTFCNDTVVIPCFVTNMEAQNTTEVYVKWKFKGRDIYTFDGALNKSTVPTDFSSAKIEVSQLLKGDASLKMDKSDAVSHTGNYTCEVTELTREGETIIELKYRVVSWFSPNENILIVIFPIFAILLFWGQFGIKTLKYRSGGMDEKTIALLVAGLVITVIVIVGAILFVPGEYSLKNATGLGLIVTSTGILILLHYYVFSTAIGLTSFVIAILVIQVIAYILAVVGLSLCIAACIPMHGPLLISGLSILALAQLLGLVYMKFVASNQKTIQPPRKAVEEPLNAFKESKGMMNDE
Protein: Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein) (P97260)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum. Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway. Binds cholesterol via its SSD domain.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10896675}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:10896675}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:15899885}; Multi-pass membrane protein {ECO:0000255}. Note=Moves from the endoplasmic reticulum to the Golgi in the absence of sterols (PubMed:10896675). Requires the presence of SPRING for proper localization to endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q12770, ECO:0000269|PubMed:10896675}.
Interaction partners:
Sequence:
MTLTERLREKISQAFYNHGLLCASYPIPIILFTGLCILACCYPLLKLPLPGTGPVEFSTPVKDYSPPPVDSDHKQGEPSEQPEWYVGAPVAYIQQIFVKSSVSPWHKNLLAVDVFRLPLSRAFQLVEEIRNHVLRDSSGTKSLEEVCLQVTDLLPGLRKLRNLLPEHGCLLLSPGNFWQNDWERFHADPDIIGTIHQHEPKTLQTSATLKDLLFGVPGKYSGVSLYTRKRTVSYTITLVFQRYHAKFLSSLRARLMLLHPSPNCSLRAENLVHVHFKEEIGIAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNVATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMFFFTTVLSIDIRRMELADLNKRLPPESCLPSAKPVGRPARYERQLAVRPAMPHTITLQPSSFRNLRLPKRLRVIYFLARTRLAQRLIMAGTVVWIGILVYTDPAGLRTYLAAQVTEQSPLGEGSLGPMPVPSGVLPASRPDPAFSIFPPDAPKLPENQTVPGELPEHAAPAEGVHDSRAPEVTWGPEDEELWRRLSFRHWPTLFNYYNITLAKRYISLLPVIPVTLRLNPQEALEGRQPQDGRSAWAPPESLPAGLWEAGPKGPGGTQAHGDITLYKVAALGLAAGIVLVLLLLCLYRVLCPRNYGQPGGGAGRRRRGELPCDDYGYAPPETEIVPLVLRGHLMDIECLASDGMLLVSCCLAGQVCVWDAQTGDCLTRIPRPGSRRDSCGGGAFETQENWERLSDGGKTSPEEPGESPPLRHRPRGPPQPALFGDQPDLTCLIDTNFSVQLPPEPTQPEPRHRAGCGRARDSGYDFSRLVQRVYQEEGLAAVRMPALRPPSPGSPLPQASQEDGAAPEKGSPPLAWAPSTAGSIWSLELQGNLIVVGRSSGRLEVWDAIEGVLCCSNDEVSSGITALVFLDRRIVAARLNGSLDFFSLETHTSLSPLQFRGTPGRGSSPSSSVYSSSNTVACHLTHTVPCAHQKPITALRAAAGRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTVYIDQTMVLASGGQDGAICLWDVLTGSRVSHTFAHRGDVTSLTCTTSCVISSGLDDLINIWDRSTGIKLYSIQQDLGCGASLGVISDNLLVTGGQGCVSFWDLNYGDLLQTVYLGKNSEAQPARQILVLDNAAIVCNFGSELSLVYVPSVLEKLD
Protein: SCP domain-containing protein (A1Z959)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Peptidase S1 domain-containing protein
- Intrepid
Sequence:
MLYLLSVLIIVLISQEALSTDYCNKDLCLPEITHIACRNYGDFDESCGSEAIIMKFPMHMRAHLLAVLNDFRNTVAKGQYPHLRPASRMATLRWHEELAGLAKFALRRCDYIDDYCSNTDEFSYVSYIYGSTKWLQLEKDPISVLDFVLQFWMDDVKGCTMAHINAEKPAKDGQCRGYFTQLVQDLAAHVGCAMMLRKGQTSGLYQYGVLCHFSRGKIANELVYRASAHPGSRCYAGTHSIYEGLCSPEEHVNPNALQLGELN
Protein: Protein FMP23, mitochondrial (P38231)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in mitochondrial iron or copper homeostatis.
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
Sequence:
MLINHLSKIRTVRHFSNIKPVLSKEVSRRVIVAPASHFKTSSPNVKSNIPIHEYKQLPEDSNYIEKHYKELQVFLNEFLIKKLNKTYADFEGDPDELVFQLEKFIELEVTPRYTNHSAPDGCEERFKSIGDRIVVDRYLDFVKDVRLTLLLNGGHSFIFDVMLQAKEVFDKMQKE
Protein: Polyprotein P1234 (Non-structural polyprotein) (A3RMR8)
Organism: Chikungunya virus (CHIKV)
Subcellular location: Host cell membrane {ECO:0000256|ARBA:ARBA00004112}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004112}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004112}. Host cell projection, host filopodium {ECO:0000256|ARBA:ARBA00004490}. Host cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004615}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004615}. Host cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004350}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004350}. Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
Interaction partners:
Sequence:
MDSVYVDIDADSAFLKALQRAYPMFEVEPRQVTSNDHANARAFSHLAIKLIEQEIDPDSTILDIGSAPARRMMSDRKYHCVCPMRSAEDPERLANYARKLASAAGKVLDRNISGKIGDLQAVMAVPDTETPTFCLHTDVSCRQRADVAIYQDVYAVHAPTSLYHQAIKGVRVAYWVGFDTTPFMYNAMAGAYPSYSTNWADEQVLKAKNIGLCSTDLTEGRRGKLSIMRGKKLKPCDRVLFSVGSTLYPESRTLLKSWHLPSVFHLKGKLSFTCRCDTVVSCEGYVVKRITMSPGLYGKTIGYAVTHHADGFLMCKTTDTVDGERVSFSVCTYVPATICDQMTGILATEVTPEDAQKLLVGLNQRIVVNGRTQRNTNTMKNYLLPVVAQAFSKWAKECRKDMEDEKLLGVRERTLTCCCLWAFKKQKTHTVYKRPDTQSIQKVQAEFDSFVVPGLWSSGLSIPLRTRIKWLLRKVPKTDLIPYSGNAQEAQDAEKEAEEEREAELTHEALPPLQAAQEDVQVEIDVEQLEDRAGAGIIETPRGAIKVTAQLTDHVVGEYLVLSPQTVLRSQKLSLIHALAEQVKTCTHSGRAGRYAVEAYDGRVLVPSGYAISPEDFQSLSESATMVYNEREFVNRKLHHIAMHGPALNTDEESYELVRAERTEHEYVYDVDQRRCCKKEEAAGLVLVGDLTNPPYHEFAYEGLKIRPACPYKIAVIGVFGVPGSGKSAIIKNLVTRQDLVTSGKKENCQEISTDVMRQRGLEISARTVDSLLLNGCNRPVDVLYVDEAFACHSGTLLALIALVRPRQKVVLCGDPKQCGFFNMMQMKVNYNHNICTQVYHKSISRRCTLPVTAIVSSLHYEGKMRTTNEYNMPIVVDTTGSTKPDPGDLVLTCFRGWVKQLQIDYRGHEVMTAAASQGLTRKGVYAVRQKVNENPLYASTSEHVNVLLTRTEGKLVWKTLSGDPWIKTLQNPPKGNFKATIKEWEVEHASIMAGICSHQVTFDTFQNKANVCWAKSLVPILETAGIKLNDRQWSQIIQAFKEDKAYSPEVALNEICTRMYGVDLDSGLFSKPLVSVYYADNHWDNRPGGKMFGFNPEAASILERKYPFTKGKWNINKQICVTTRRIEDFNPTTNIIPVNRRLPHSLVAEHRPVKGERMEWLVNKINGHHVLLVSGYNLALPTKRVTWVAPLGVRGADYTYNLELGLPATLGRYDLVVINIHTPFRIHHYQQCVDHAMKLQMLGGDSLRLLKPGGSLLIRAYGYADRTSERVICVLGRKFRSSRALKPPCVTSNTEMFFLFSNFDNGRRNFTTHVMNNQLNAAFVGQATRAGCAPSYRVKRMDIAKNDEECVVNAANPRGLPGDGVCKAVYKKWPESFKNSATPVGTAKTVMCGTYPVIHAVGPNFSNYSESEGDRELAAAYREVAKEVTRLGVNSVAIPLLSTGVYSGGKDRLTQSLNHLFTAMDSTDADVVIYCRDKEWEKKISEAIQMRTQVELLDEHISIDCDVIRVHPDSSLAGRKGYSTTEGALYSYLEGTRFHQTAVDMAEIYTMWPKQTEANEQVCLYALGESIESIRQKCPVDDADASSPPKTVPCLCRYAMTPERVTRLRMNHVTNIIVCSSFPLPKYKIEGVQKVKCSKVMLFDHNVPSRVSPREYRSSQESVQEVSTTTSLTHSQFDLSADGETLPVPSDLDADAPALEPALDDGAVHTLPTIIGNLAAVSDWVMSTVPVAPPRRRRGRNLTVTCDEREGNITPMASVRFFRAELCPAVQETAETRDTAISLQAPPSTTMELSHPPISFGAPSETFPITFGDFDEGEIESLSSELLTFGDFLPGEVDDLTDSDWSTCPDTDDELXLDRAGGYIFSSDTGPGHLQQKSVRQSVLPVNTLEEVHEEKCYPPKLDELKEQLLLKKLQESASMANRSRYQSRKVENMKATIIQRLKRGCKLYLMAETPKVPTYRTIYPAPVYSPPINVRLSNPESAVAACNEFLARNYPTVSSYQITDEYDAYLDMVDGSESCLDRATFNPSKLRSYPKQHAYHAPSIRSAVPSPFQNTLQNVLAAATKRNCNVTQMRELPTLDSAVFNVECFKKFACNREYWEEFAASPIRITTENLTTYVTKLKGPKAAALFAKTHNLLPLQDVPMDRFTVDMKRDVKVTPGTKHTEERPKVQVIQAAEPLATAYLCGIHRELVRRLNAVLLPNVHTLFDMSAEDFDAIIAAHFKPGDAVLETDIASFDKSQDDSLALTALMLLEDLGVDHSLLDLIEAAFGEISSCHLPTGTRFKFGAMMKSGMFLTLFVNTLLNITIASRVLEDRLTKSACAAFIGDDNIIHGVVSDELMAARCATWMNMEVKIIDAVVSQKAPYFCGGFILHDTVTGTACRVADPLKRLFKLGKPLAAGDEQDEDRRRALADEVIRWQRTGLIDELEKAVYSRYEVQGISVAVMSMATFASSRSNFEKLRGPVITLYGGPK
Protein: Inositol-3-phosphate synthase (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase) (IPS) (MI-1-P synthase) (MIP synthase) (Q54N49)
Organism: Dictyostelium discoideum (Social amoeba)
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:
- Inositol monophosphatase
- 3'
- 3'
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Multiple inositol polyphosphate phosphatase 1
- Prolyl endopeptidase
- Uncharacterized protein
- Delta 9 fatty acid desaturase
- Delta 9 fatty acid desaturase
- Inositol-tetrakisphosphate 1-kinase
Sequence:
MSAQMFESFKVNSPNVKYTDEHIISDYTYQTTKVQNVNGELIVEPVDQKYIFKTERKVPRMGVMIVGLCGNNGTTVVGGVIANREGLCWNTKQGLQTPNYFGSVVMSSTIRMGMDENGCDAYIPLKNLIPMVHPNDIVFGGWDINNANLADAMQRAQVFDYDLQVQLIPHMKNITPLPSIYFPDFIAANQKDRANNVLTGTKKEQMEQIRKDIRDFKESNKLDTVVVMWSANTERFSSLVPGVNDTIENLMAAIDRSEEEISPSTLFAVASILENTTYINGSPQNTFVPAVVDLAIQHNVSIGGDDFKTGQTKIKSVLTDYLVSAGIKPVSIVSYNHLGNNDGKNLSAPQQFRSKEITKSNVVDDMIASNNILYKQGEHPDHVIVIKYVPYVGDSKRAMDEYTSQIFMGGHNTIVLHNTCEDSLLAAPIILDLVILAEVTSRITMKKQDDDQFATFHPVLSLLSYLLKAPIVPKHATVVNALFKQRACIENIFKACVGIAPDNNMLLEQRL
Protein: GSKIP domain-containing protein (D9PTP0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSLHKVSSINRSAGTNPASRGGESSLELEAIAAVHELSFAVQSISVSEMLPRTPDLIFVNVTTLEAQPYCLELTLKGWRITSLRSDCMVGDFTRLELFTKYYDSLYLLMDDISPGYRERFSEKLVQRLKLIEAGEEDQVAPCASLQSPSLSTDSSSKESQYSSTESLPIVTPVSTPAIDPDFKPKFK
Protein: Coiled-coil domain containing 141 (J3QN68)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XEGQVQGADVLAVNGTREDGLPMDLRRTSSDKEDSAQGLILPEDTLSGEESECISSDDISLPPLPVSPESPLAPSDMEVEELTSSSALALHISGYRMHPGTGSRRARNCVQMDTYRSCTRTQSIRCSFRRYVRQMLASMWLKPKTLVAPCLPKPSSM
Protein: Phosphoinositide phosphatase SAC4 (AtSAC4) (EC 3.1.3.-) (Phosphatidylinositol 3,5-bisphosphate 5-phosphatase SAC4) (Protein SUPPRESSOR OF ACTIN 4) (SAC domain protein 4) (Q7XZU1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Subcellular location: Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Protein VAC14 homolog
- 1-phosphatidylinositol-3-phosphate 5-kinase FAB1A
- 1-phosphatidylinositol-3-phosphate 5-kinase FAB1B
- Putative 1-phosphatidylinositol-3-phosphate 5-kinase FAB1C
- Putative 1-phosphatidylinositol-3-phosphate 5-kinase FAB1D
- Phosphatidylinositol 3-kinase VPS34
- Phosphatidylinositol-3-phosphatase myotubularin-1
- Phosphatidylinositol-3-phosphatase myotubularin-2
- Phosphoinositide phosphatase SAC3
- Phosphoinositide phosphatase SAC5
Sequence:
MTSSPSVENGGSGSSGSSALLGCMQQFKLFETQANFYMIGWNGSGVYRILKIDRLEASELNLREDSTAYTKKECYELLKRIHEGNKATGGLKLVTVCYGIIGFIKFLGPYYMLLITERREIGEICGHIVYEVSKSDMIALQHSSVLCNTANLRDENRYKRLLCMVDLTKDFFFSYSYNIMRSFQKNICDHESGGTLYKKMFVWNEFLTRGTRHHLRNTLWTVALVYGFFKQTILSEAGRNFKLTLIARRSRHNAGTRYLKRGINESGNVANDVETEQIVSEDVPVDRPMQISSVVQNRGSIPLFWSQETSRMKVKPDIVLSKRDLNYEATRVHFENLVERYGVPIIILNLIKTNERKPRESILRAEFANAIDFINKDLPEENRLRFLHWDLHKHFHSKTENVLALLGKVAACALMLTGFFYYQLTPAMKLEGYMSLSSSDADTSPHNSSDDDSRDYDSLEKNCRPSKNVANGDYDVKPSRLQSGVLRTNCIDCLDRTNVAQYAYGWAALGQQLHALGIRDAPTIELDDPLSSTLMGLYERMGDTLAYQYGGSAAHNKVFSERRGQWRAATQSQEFLRTLQRYYNNAYMDADKQDAINIFLGTFRPEQGSQAVWELRSDSHSNGRSGEISMGEDEKFLVKRCLSDGNILHESHTPMSAMSRKNESISHRGFVSSHQVTRTHIISESSPDMPAAGDVTLSRCTPSMPSTHFFGDVQKVQHNGSSSIYLSEQEDMSSVSNFVDIEWLSSSENLCENDHLSRPSALTIYSTAETSSSENIITEVKQLTPAMRESGSSSRKGKEPVETELSVHTKIRDDFPDSFKQWVAYGEALCH
Protein: Protein EFR3 homolog A (Protein EFR3-like) (Q8BG67)
Organism: Mus musculus (Mouse)
Function: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. In the complex, EFR3A probably acts as the membrane-anchoring component. Also involved in responsiveness to G-protein-coupled receptors; it is however unclear whether this role is direct or indirect.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15363888}; Lipid-anchor {ECO:0000250|UniProtKB:Q14156}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q14156}. Note=Palmitoylation anchors the protein to the plasma membrane. A small amount is observed in the cytosol. {ECO:0000250|UniProtKB:Q14156}.
Interaction partners:
- Tetratricopeptide repeat protein 7A
- Phosphatidylinositol 4-kinase alpha
- Tetratricopeptide repeat protein 7B
- Hyccin
- Hyccin 2
Sequence:
MPTRVCCCCSALRPRYKRLVDNIFPEDPKDGLVKADMEKLTFYAVSAPEKLDRIGAYLAERLSRDVVRHRSGYVLIAMEALDQLLMACHSQSIKPFVESFLHMVAKLLESGEPKLQVLGTNSFVKFANIEEDTPSYHRRYDFFVSRFSAMCHSCHSDPEIRTEIRIAGIRGIQGVVRKTVNDELRATIWEPQHMDKIVPSLLFNMQKIEEVDSRLGPPSSPSAADKEENPAVLAESCFRELLGRATFGNMNNAVRPVFAHLDHHKLWDPNEFAVHCFKIIMYSIQAQYSHHVIQEILGHLDARRKDSPRVRAGIIQVLLEAVAIAAKGSIGPTVLEVFNTLLKHLRLSVELEANDSQKGSVGSVTVSSKDNDEKIVQNAVIQTIGFFGSNLPDYQRSEIMMFIMGKVPVFGTSTHTLDISQLGDLGTRRIQIMLLRSLLMVTSGYKAKTIVTALPGSFLDPLLSPSLMEDYELRQLVLEVMHNLMDRHDNRAKLRGIRIIPDVADLKIKREKICRQDTSFMKKNGQQLYRHIYLGCKEEDNVQKNYELLYTSLALITIELANEEVVIDLIRLAIALQDSAIINEDNLSMFHRCGIMALVAAYLNFVSQMIAVPAFCQHVSKVIETRTMEAPYFLPEHIFRDKCMLPKSLEKHDKNLYFLTNKIAESLGGSGYSVERLTVPYVPQVTDEDRLSRRKSIVDTVSIQVDILSNSVPSDDVVSNTEEITFEALKKAIDTNGMEEQEKEKRRLVIEKFQKAPFEEIAAQCESKANLLHDRLAQILELTIRPPPSPSGTLTVTSGHTQYQSVPVYEMKFPDLCVY
Protein: Clathrin light chain (Q8MN58)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:16734666, ECO:0000305}; Peripheral membrane protein {ECO:0000269|PubMed:16734666}; Cytoplasmic side {ECO:0000269|PubMed:16734666}. Membrane, coated pit {ECO:0000269|PubMed:16734666, ECO:0000305}; Peripheral membrane protein {ECO:0000269|PubMed:16734666}; Cytoplasmic side {ECO:0000269|PubMed:16734666}. Note=Cytoplasmic face of coated pits and vesicles. Localized to punctae scattered within the cytoplasm, along the plasma membrane and concentrated in the perinuclear region. {ECO:0000269|PubMed:16734666, ECO:0000305}.
Interaction partners:
- Clathrin heavy chain
- I/LWEQ domain-containing protein
- Epidermal growth factor receptor substrate 15 homolog
- AP-2 complex subunit alpha-2
- AP-2 complex subunit mu
- AP-1 complex subunit beta
- AP-2 complex subunit sigma
- ANTH domain-containing protein
- AP-1 complex subunit gamma
- Epsin
Sequence:
MSDPFGEENVEITEEFVEGDINENDLIDGNVEYVDGNGISFETTTFDNSNNNNNNNNHNNNSYNSGFDGDLSSVDGDMKPKETAPAMREYLEKHEKEMQEKKKKSEEKRQKKIAEAKQSLDNFYSEREAKKKTALKNNRDHNKSLETDSTSGNTTHTWESVVSMIDLQAKPNPANKDTSRMREILIRLKNQPIV
Protein: SIGNR7 protein (Q14FK5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAGEPEFHQPKNHEEEVTSGEQGFAEHDPEGLVCSSKSLQGHLTQVPWLLLLLISLGLFLLMLATLVQVSRIRAYSQGQTQDQQGSSSLDKVAVPREQTHSGLEQIQQIQQQLTQFNASLAGLCRPCPWDWELFQGSCYLFSRTLGSWETSASSCEDLGAHLVIVNSVSEQQFLKYWHIRKNQLTWIGLSDHRSEGSWQWVDDTPLKLSFWKEGEPNNEGDEDCVVMAEDKWNDSRCTANNFWVCEQPSAPCPGY
Protein: MGT2 magnesium transporter (Q4Q9Y4)
Organism: Leishmania major
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- MGT1 magnesium transporter
- Protein kinase domain-containing protein
Sequence:
MMHSKLDGVTPGVAEAHQLSPLVARQRYLTVNRSGGSSWFVRKDVMLKNLQVSQDSTLWLDVEGETPEERRAILNDLPWRVNIPSAVLDAVARPTESDVVELQPSLAQYAHGVLSCAINPLYDTTDETATVDEDNFSGEAFDAARGFVWCSVLITDTLIVTMHDKRFLGLEEVVRALEMRMNPMDTTSLGNSVLTPSIVFATLVAYSSEMMLPDPTTLLSEVDCIDEMVLLIAPGVRDQPDLLRRIALLRRRISSFRGLLYMKEKLLRELVTPSMRGSFVACDMVHVVPIYKEALDKNTKMADRLDDARDILNQANLNFVTGVSMRMSQSSANMDFKMQILSQVAVICLPLNLLASIFGMNCEVAWQADSHPNLKAFWGIVALMVAWVLVCSIPTIRHVLHGNAAKAIVPTDS
Protein: BZIP domain-containing protein (Q65CL5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQQNIQYTYSSDPRSGGNQNQQLHGISQFQQNSYQPTTYSNSNANNFHSSNSATFIPNSVTQTPQRRMGEEKSLVNMLDAYFIDSTTPSTSTSWNNQQPVQMSSIQQSVGSYNQQIPQLKDLQVEGMNVKLSSSPDKGEKDRVKKARQAEAARMRYHRLSNEEKRELNLKRTLAQKRKRQREKEMEELESILRETNDIQEDPDITEQLREKRMRAKWAEAARTRYARMTPEERRAHNTRRRMRQMQNAMSAIKACGMATGDPQKDDEAVRLHIKTQNAKKAEAARQRYHRMNDDEKRVYNQRRTEAFRRRRMEEEMLLAMPIGRINGEALDRAQQIVVRNAKRAEAARLRYQRMTPDQRKVAKQEPKEESWPSHEQSDTQIDHDLDLGDSYNQKRYTPKRRRNEMDDMISAGQMAVGSSGTITMGTGTPAKKDDMDALSSLERDVVKRTQHAQQILLRQRANQSSGTPRSVTPPPQAYIISNGQQQHQQLVGNQGNNGIGQHQVLHQGHMQQQQIQVSHQQSSQSIPQNIYTSGMIIQNQGQQQQGQQQQQGQSQQILNNPYRT
Protein: Acyl-coenzyme A thioesterase PaaI (EC 3.1.2.-) (Phenylacetic acid degradation protein PaaI) (P76084)
Organism: Escherichia coli (strain K12)
Function: Thioesterase with a preference for ring-hydroxylated phenylacetyl-CoA esters. Hydrolyzes 3,4-dihydroxyphenylacetyl-CoA, 3-hydroxyphenylacetyl-CoA and 4-hydroxyphenylacetyl-CoA. Inactive towards 4-hydroxybenzoyl-CoA and 4-hydroxyphenacyl-CoA.
Interaction partners:
- 1,2-phenylacetyl-CoA epoxidase, subunit B
- 1,2-phenylacetyl-CoA epoxidase, subunit A
- Putative 1,2-phenylacetyl-CoA epoxidase, subunit D
- Phenylacetate-coenzyme A ligase
- 1,2-phenylacetyl-CoA epoxidase, subunit C
- 1,2-phenylacetyl-CoA epoxidase, subunit E
- 3-hydroxyadipyl-CoA dehydrogenase
- 1,2-epoxyphenylacetyl-CoA isomerase
- Bifunctional protein PaaZ
- 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase
Sequence:
MSHKAWQNAHAMYENDACAKALGIDIISMDEGFAVVTMTVTAQMLNGHQSCHGGQLFSLADTAFAYACNSQGLAAVASACTIDFLRPGFAGDTLTATAQVRHQGKQTGVYDIEIVNQQQKTVALFRGKSHRIGGTITGEA