wanglab/gogpt-training-data huggingface dataset:
Protein: Protein unc-13 homolog 4B (Protein Staccato) (Q9VBY8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for tracheal development in embryos. Functions with the GTPase Rab39 and downstream of dnd, to regulate lumen fusion between previously separate tracheal branches (anastomosis). Essential component of secretory lysosome-related organelles (SLs) that are present in the tracheal fusion tip cells (FCs). Mediates intracellular fusion of the extending tracheal stalk cell lumen in the FCs by recruiting the SNARE complex component Syx1A to the SLs, this may then enable the SLs to interact with complementary SNAREs (such as Syb) present in the apical membrane of the FC-FC interface and the membranes of the separate tracheal stalk cells. May also function in the maturation and exocytosis of the SLs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27323327}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27323327}. Cell projection, filopodium {ECO:0000269|PubMed:27323327}. Late endosome {ECO:0000269|PubMed:27323327}. Lysosome {ECO:0000269|PubMed:27323327}. Note=Expressed throughout the cytoplasm of embryonic tracheal cells, except in the tracheal fusion cells (FCs) where it localizes to discrete intracellular vesicles. These vesicles also accumulate Rab39 and display late-endosomal, lysosomal, and SNARE components (Syx1A), characteristics of lysosome-related organelles. Prior to contact between FCs the vesicles localize to the presumed fusion point and sometimes to the filopodia. On contact between FCs, the lysosomes accumulate and move along the cytoskeleton track in a dynein-dependent manner between the two apical domains, becoming densely packed around the interface between the fusion cells. Some of the puncta remain associated with the primary apical FC membrane. {ECO:0000269|PubMed:27323327}.
Interaction partners:
- Stac-like, isoform J
Sequence:
MDEEQMWKGFFFKLQELKMNPPTEHEHQLQDGDDGFFEKFGSLLRQKSQIDEGVLKSSLAPLEENGSGGEEDSDESPDGTLQLSQDSECTSIDTFATESTLASSSDKDISTSVLDSAPVMNVTDLYEEILFEIFNNIGCENNEECTNSLVEFVQDAFKIPNATHEEIYEAARLKEPPNVRLNVEIIKAENLMSKDSNGLSDPFVTLYLESNGSHRYNSSVKPATLNPIWEEHFSLPITENARDEVLIVEVWDFDAAETVKEKVNKILDVKGVKGLSKLMKEIAVTASSGKHDNELIGRAAITLKSIPVSGLTVWYNLEKGSKGRSRGSLLVNLALSAEKNKSVAVQEHKNLLKLLLMYELETSQVANYWWSGKFSPNAELIRSQHAAQSGLTPFDCALSQWHAYSTIHETHKLNFTLFNSILDVVVPVITYMQNDSEDVKTFWDGVKRLLPSCFAVLRKLRSKNTSDKNIIRALNEVLDILKKIKELEVPESVDIFPKSVYGWLHTNDTDETCNIDTAIEDAINTGTREWLEHIVEGSRQSKNTETDDEKLQYVIKLIQMVRSDLQRAMEYFDKIFYHKIQLNYSAVLYLFYDSKLAEICKSIIIEVCNNIKRLDVPDDQFEYLPNLENVNMGTTLFEVYLILKRYVQLGESLCSEPLELSNFYPWFERGVTHWLDISIIKALSRIQKAIDLDQLKAVDETVKYSSSAVDTLSIFYQIKIFWQQLDWPEVEGSYIFVAKIVNDLCRCCIFYAQQMSRRVENIFIADDNNKNFILSEEWCIAINNMDYIRQSLPSFIKELSIDDIIKRLGEYRTNLEAERCASTIKTVIENALDTERNQIVELIEIVARKMAPPIRRYLAEGAEVLAKDSNSMDQLMMYLESSLATLYDTLNEINFQRILDGIWSELSIIMYDLIQSNLDKRRPPAFFQNLNNTLQTMMDCFKMGNLQTSDIKILSSIQSRLRLYSLETSDLIHQYYLERLENQKSQESSPYGQLTITAQLTDTGLLLNILNARNLLPMDSNGSVDSFVKASFMPTSRFNDVPTVKTNVHNKSCFPLYDQEFRINLSDHQRSEKNSLIVFSIKDKDLFGMSSQYIAESYISFADLEATPPGEQIMMNLSRPEYTDSESLRALEYRLGDKQAKDFLKKLKNRSFS
Protein: Malonate--CoA ligase ACSF3, mitochondrial (EC 6.2.1.76) (Acyl-CoA synthetase family member 3) (Q3URE1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q4G176}.
Interaction partners:
- Fatty acid synthase
- Malonyl-CoA decarboxylase, mitochondrial
- Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
- Acetyl-CoA carboxylase 1
- Acetyl-CoA carboxylase 2
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase X, mitochondrial
- Aldehyde dehydrogenase, mitochondrial
- Alpha-aminoadipic semialdehyde dehydrogenase
Sequence:
MPPHLALPFRRLFWSLASSQLIPRRHRGHSLLPTTPEAHTDGSVPVFIRALAFGDRIALIDKYGHHTYRELYDRSLCLAQEICRLQGCKVGDLQEERVSFLCSNDVSYVVAQWASWMSGGVAVPLYWKHPEAQLEYFIQDSRSSLVVVGQEYLERLSPLAQRLGVPLLPLTPAVYHGATEKPTEQPVEESGWRDRGAMIFYTSGTTGRPKGALSTHRNLAAVVTGLVHSWAWTKNDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQQVWEKFLSSEAPQITVFMAVPTVYSKLLDYYDKHFTQPHVQDFVRAVCKERIRLMVSGSAALPVPLLEKWRSATGHTLLERYGMTEIGMALSNPLTEARVPGSVGTPLPGVEVRIISENPQKGSPYIIHAEGNERGTKVTPGFEEKEGELLVRGPSVFREYWDKPEETKSAFTSDGWFRTGDTAVFKDARYWIRGRTSVDIIKTGGYKVSALEIERHLLAHPSITDVAVIGVPDMTWGQRVTAVVALQEGHSLSHGDLKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKKELLKQLYPSGQRSQPGQG
Protein: 16.9 kDa class I heat shock protein 1 (16.9 kDa heat shock protein 1) (OsHsp16.9A) (P27777)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MSLVRRSNVFDPFSLDLWDPFDSVFRSVVPATSDNDTAAFANARIDWKETPESHVFKADLPGVKKEEVKVEVEEGNVLVISGQRSKEKEDKNDKWHRVERSSGQFMRRFRLPENAKVDQVKAGLENGVLTVTVPKAEVKKPEVKAIEISG
Protein: Endolysin A (EC 3.-.-.-) (Gene 10 protein) (Gp10) (Lysis protein) (Lysozyme) (O64203)
Organism: Mycobacterium phage D29 (Mycobacteriophage D29)
Function: Endolysin that degrades host peptidoglycans and participates with the holin protein in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.
Interaction partners:
Sequence:
MTLIVTRDHAQWVHDMCRARAGNRYGYGGAFTLNPRDTTDCSGLVLQTAAWYGGRKDWIGNRYGSTESFRLDHKIVYDLGFRRLPPGGVAALGFTPVMLVGLQHGGGGRYSHTACTLMTMDIPGGPVKVSQRGVDWESRGEVNGVGVFLYDGARAWNDPLFHDFWYLDAKLEDGPTQSVDAAEILARATGLAYNRAVALLPAVRDGLIQADCTNPNRIAMWLAQIGHESDDFKATAEYASGDAYDTRTDLGNTPEVDGDGRLYKGRSWIMITGKDNYRDFSRWAHGRGLVPTPDYFVVHPLELSELRWAGIGAAWYWTVERPDINALSDRRDLETVTRRINGGLTNLDDRRRRYNLALAVGDQLLTLIGDDDELADPTIQRFIREIHGALFNTVVTQSPYGDPQNPDGSEPRSNLWQLHELIKNGDGMGHARYVEESARAGDLRELERVVRAAKGLGRDRSPEFIARARNVLAQIEAANPEYLQAYIARNGAL
Protein: Phosphoinositide phospholipase C (EC 3.1.4.11) (Q5FWA6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWKSEGKEGQVLECSLINSIRQAAIPKDPKILAALEAVGKSENDLEGRILCVCSGTDLVNIGFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFLTNTTGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPAAFTYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEELKKKGLISSDGFCRYLMSDENAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVVLDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRPLPSPNDLKRKILIKNKRLKPEVEKKQLEALKSMMEAGESAAPASILEDDNEEEIESADQEEEAHPEYKFGNELSADDYSHKEAVANSVKKTSDDLEHENNKKGLVTVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVEFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGTYVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKKFLSITEKRADQMRAMGIETSDIADVPSDTSKKKKKKKKKK
Protein: Mvb12p (A0A1D8PSU3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Vacuolar protein sorting-associated protein 28
- Protein kinase C-like 1
Sequence:
MIDTDKPDPILKQVPLIKNPAFQPPRPITLSNNYNKLIPTLSSTVVPPKLNISDTEIDSWLNEIRSLREQIKNKQTNDNNRQCTKYENWIREQSNKIAPGFNYTVMQPQKSMRNQERKLTTKKEEEEQEEEESDDNNDNDKDNGSGYDEMNELDRIFGTTKLN
Protein: Melanoma-associated antigen H1 (MAGE-H1 antigen) (Q5PPP4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPRGRKSRRRRNAKAAEENRNNRKIQASEASKTPMAASVTPSTPEEYLSGPEEDTSTPEKASSTLAEASSTALVQKPVTRSNFQGTKKSLLMSILALIFIMGNSAKEALVWKVLGKLGMQPGRQHSIFGDPKKVVTEEFVRRGYLIYKPVPRSSPVEYEFFWGPRAHVESSKLKVMHFVARVRNRCSKDWPCNYDWDSDDDAEVEAILNSGARGSSAP
Protein: LD46256p (Q95TK0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAVKRALRKYHESRSQAAAKLQLIRDELLLLPPPPPPPLTTKPANLEKPVLVQKKPKFRYFHFDPFKCAIVKTYTRTLRSAYRPPFDPKHFAMLMKTGRLPQIPPGFLRHRPPFIPAHVDAVTRGAMLKEFFSKHPPPPLAMPMPVPNGMPYYLSGPPPTSSGAAVSPVPVNVLPQPIPVLDGSGYQGYPQSATMVPLPVPVPVPVPLPVPLPVSTDTTPSPALETPYFTPPPLPELPPLPELPSQFTVSSVPTITEIMPVDILQKLGPLPKTLDVDDGGGTASPEDISDDLKEVEAKPAEQHVVGVKPQLLVETQ
Protein: Fatty acid-binding protein, intestinal (B5XC78)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
- Fatty acid-binding protein, liver
Sequence:
MAFNGTWKVERNENYDKFMEQMGINVMKRKLAEHDNLKVIIEQTGDKFHIKESSTFRNKDIDFTLGVQFDYALADGTEVSGAWEMDGDVLKGKFTRKDNSKVLTTTRALVGGELVQSYNYDGVDAKRIFKKA
Protein: Fibroleukin (Cytotoxic T-lymphocyte-specific protein) (Fibrinogen-like protein 2) (Prothrombinase) (P12804)
Organism: Mus musculus (Mouse)
Function: Converts prothrombin to thrombin.
Subcellular location: Secreted.
Interaction partners:
- Prothrombin
- Low affinity immunoglobulin gamma Fc region receptor II
- Tissue factor
- Vitamin K-dependent protein C
- Tissue factor pathway inhibitor
Sequence:
MRLPGWLWLSSAVLAACRAVEEHNLTEGLEDASAQAACPARLEGSGRCEGSQCPFQLTLPTLTIQLPRQLGSMEEVLKEVRTLKEAVDSLKKSCQDCKLQADDHRDPGGNGGNGAETAEDSRVQELESQVNKLSSELKNAKDQIQGLQGRLETLHLVNMNNIENYVDNKVANLTVVVNSLDGKCSKCPSQEHMQSQPVQHLIYKDCSDHYVLGRRSSGAYRVTPDHRNSSFEVYCDMETMGGGWTVLQARLDGSTNFTREWKDYKAGFGNLEREFWLGNDKIHLLTKSKEMILRIDLEDFNGLTLYALYDQFYVANEFLKYRLHIGNYNGTAGDALRFSRHYNHDLRFFTTPDRDNDRYPSGNCGLYYSSGWWFDSCLSANLNGKYYHQKYKGVRNGIFWGTWPGINQAQPGGYKSSFKQAKMMIRPKNFKP
Protein: Metaxin-1 (Mitochondrial outer membrane import complex protein 1) (B0BN02)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
MRLGGPPRNVRSGQRFERSRCSRGHVQFGKSPQRPLSRTRCPSSKPCLSPAVRGYARQRHRESPKRAWTAALLPYGGRLRTSPRRSSEGQCSTSSSAAASPAARSHASLDLKLRVATQAETRGCSSWREKADAYERVLPGQRMCKMAAPMELFCWSGGWGLPSVDLDSLAVLTYTRFTCAPLKVHKISNPWQSPSGTLPALRTSSGKVITEPHKIITHLRKEIHTFWIDAKNYVEVTRKWYAEAMPFPLNFFLPGRMQRRHMERLQLLCGEHRLESEEELEKELYQEARECLTLLSHRLGSRKFFFGDAPASLDAFVFSHLVLLLQAKLPSGKLQAHLRGLQNLCVYCTHILNLYFPRDATDVPPPPCQTPAGPETEEEPYRRRTQILSVLAGLAAMVGYALLSGIVSIQRASPARAPCTQALDLAEEDEED
Protein: SUPpressor (Q94207)
Organism: Caenorhabditis elegans
Interaction partners:
- C2H2-type domain-containing protein
- Regulator of microtubule dynamics protein 1
- Ubiquitin-conjugating enzyme E2 ubc-18
- F-box domain-containing protein
- Microtubule-associated protein
Sequence:
MPSCEIKFDFNDSDESVTVRETRIILLLPVIRRAVELQYPDFATEENAVIEAPFRVPFKKDAGVFLFDTIARYAAPTDDNVHEITVEQSYPEAGPKTLDELKEIIELANFWECTTYMECIGFAIAKKLEDKTIEEIAAFMGVECNPPGNFFAEEDGWIHPPADAFQNVQ
Protein: Uncharacterized transporter C36.03c (O59700)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized transcriptional regulatory protein C530.05
- Brefeldin A resistance protein
- Uncharacterized protein PB2B2.06c
Sequence:
MYNNNSSTSSDSSNSEEKANAQHASSTDSTSEHTDPAVADEGFPAEQYQSADLEKQQLLIEEGPGGFPYITNPERFYVSLEPSDPRLAVNWPTHVKILHVALLAFTTLTASWGSSVFSAAATIFAAKYHIGLTVALLGMSLYVCGFASGPILWAPISELVGRKIPLIVGMFMFSIFSIAVAVAKDVQTVMICRFFSGFCASSPLSVVAAAFADMFDNKTRGPAVCIFACITFAGPLIGPIAGGFLAKSYLGWRWTEYITSFMGFFSTLCLLFMKECYSRTITEQEAARLRVEYNNNFIRAKSEEEYIDFKALAKRYLAVPFVLLFCEPIVFLLTLYMSFVYGILYLLLEAYPIIFAEKRHFSLGVDALPYIGLLVGVILGAALIAYFQGYYNRKLDANGGKPVPEARLPPMMIGSVLFPAGIFWLAWSGYYTHVHWIVPTLSGLLTGCGILTIFMQSLIYLIDAYLFRAASVIAANTIMRSLVAAGFPLFAVQMFHNMGIGWAGSLLGFIATALIPIPTLFFIFGKRIRLMSKNTVNL
Protein: Ferrochelatase, mitochondrial (EC 4.98.1.1) (Heme synthase) (Protoheme ferro-lyase) (P22315)
Organism: Mus musculus (Mouse)
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27599036}; Peripheral membrane protein {ECO:0000269|PubMed:27599036}; Matrix side {ECO:0000269|PubMed:27599036}.
Interaction partners:
- Protoporphyrinogen oxidase
- Frataxin, mitochondrial
- ATP-binding cassette sub-family B member 10, mitochondrial
- Mitoferrin-1
- Uroporphyrinogen decarboxylase
- Heme oxygenase 2
- Heme oxygenase 1
- Protoheme IX farnesyltransferase, mitochondrial
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
Sequence:
MLSASANMAAALRAAGALLREPLVHGSSRACQPWRCQSGAAVAATTEKVHHAKTTKPQAQPERRKPKTGILMLNMGGPETLGEVQDFLQRLFLDRDLMTLPIQNKLAPFIAKRRTPKIQEQYRRIGGGSPIKMWTSKQGEGMVKLLDELSPATAPHKYYIGFRYVHPLTEEAIEEMERDGLERAIAFTQYPQYSCSTTGSSLNAIYRYYNEVGQKPTMKWSTIDRWPTHPLLIQCFADHILKELNHFPEEKRSEVVILFSAHSLPMSVVNRGDPYPQEVGATVHKVMEKLGYPNPYRLVWQSKVGPVPWLGPQTDEAIKGLCERGRKNILLVPIAFTSDHIETLYELDIEYSQVLAQKCGAENIRRAESLNGNPLFSKALADLVHSHIQSNKLCSTQLSLNCPLCVNPVCRKTKSFFTSQQL
Protein: Cathepsin S (EC 3.4.22.27) (P25326)
Organism: Bos taurus (Bovine)
Function: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P25774}. Secreted {ECO:0000250|UniProtKB:P25774}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P25774}.
Interaction partners:
- Ia antigen-associated invariant chain
- BH3-interacting domain death agonist
- Apoptosis regulator Bcl-2
- Procathepsin L
- Interleukin-10 receptor subunit alpha
- Cyclic AMP-responsive element-binding protein 1
- Cathepsin L
- Bcl-2-like protein 1
- Interleukin-10 receptor subunit beta
- Legumain
Sequence:
MNWLVWALLLCSSAMAHVHRDPTLDHHWDLWKKTYGKQYKEKNEEVARRLIWEKNLKTVTLHNLEHSMGMHSYELGMNHLGDMTSEEVISLMSSLRVPSQWPRNVTYKSDPNQKLPDSMDWREKGCVTEVKYQGACGSCWAFSAVGALEAQVKLKTGKLVSLSAQNLVDCSTAKYGNKGCNGGFMTEAFQYIIDNNGIDSEASYPYKAMDGKCQYDVKNRAATCSRYIELPFGSEEALKEAVANKGPVSVGIDASHSSFFLYKTGVYYDPSCTQNVNHGVLVVGYGNLDGKDYWLVKNSWGLHFGDQGYIRMARNSGNHCGIANYPSYPEI
Protein: Gamma-aminobutyric acid receptor subunit beta-2 (GABA(A) receptor subunit beta-2) (GABAAR subunit beta-2) (P63138)
Organism: Rattus norvegicus (Rat)
Function: Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel (By similarity). The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer (By similarity). The alpha1/beta2/gamma2 receptor and the alpha2/beta2/gamma2 receptor exhibit synaptogenic activity (By similarity). Functions also as histamine receptor and mediates cellular responses to histamine.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47870}. Cell membrane {ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47870}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25172774}. Note=The beta-2 subunits are present in Golgi synapses and on the extrasynaptic membranes (alpha-1/6-beta-2/3-gamma-2 receptors), and in some of the mossy fiber to granule cell synapses (alpha-6-beta-2/3-gamma-2 receptors). Present in GABAergic and glutamatergic synapses on granule cells (PubMed:9464994). The beta-2 subunit (alpha-6-beta-2/3-delta receptors) are found only on the extrasynaptic somatic and dendritic membranes (PubMed:9464994). {ECO:0000269|PubMed:9464994}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid receptor subunit beta-3
- Trafficking kinesin-binding protein 2
- Huntingtin-associated protein 1
- Vesicle-fusing ATPase
- Inactive phospholipase C-like protein 1
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor subunit alpha-2
Sequence:
MWRVRKRGYFGIWSFPLIIAAVCAQSVNDPSNMSLVKETVDRLLKGYDIRLRPDFGGPPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGDDNAVTGVTKIELPQFSIVDYKLITKKVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFMALLEYALVNYIFFGRGPQRQKKAAEKAANANNEKMRLDVNKMDPHENILLSTLEIKNEMATSEAVMGLGDPRSTMLAYDASSIQYRKAGLPRHSFGRNALERHVAQKKSRLRRRASQLKITIPDLTDVNAIDRWSRIFFPVVFSFFNIVYWLYYVN
Protein: 5-hydroxytryptamine receptor 2C (5-HT-2C) (5-HT2C) (5-HTR2C) (5-hydroxytryptamine receptor 1C) (5-HT-1C) (5-HT1C) (Serotonin receptor 2C) (P34968)
Organism: Mus musculus (Mouse)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including ergot alkaloid derivatives, 1-2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down-stream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores. Regulates neuronal activity via the activation of short transient receptor potential calcium channels in the brain, and thereby modulates the activation of pro-opiomelacortin neurons and the release of CRH that then regulates the release of corticosterone. Plays a role in the regulation of appetite and feeding behavior, responses to anxiogenic stimuli and stress. Plays a role in insulin sensitivity and glucose homeostasis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P28335}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 2A
- 5-hydroxytryptamine receptor 2B
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent L-type calcium channel subunit alpha-1C
- 5-hydroxytryptamine receptor 1B
- Guanine nucleotide-binding protein subunit alpha-11
- Voltage-dependent L-type calcium channel subunit alpha-1F
- Voltage-dependent L-type calcium channel subunit alpha-1S
- 5-hydroxytryptamine receptor 1A
Sequence:
MVNLGTAVRSLLVHLIGLLVWQFDISISPVAAIVTDTFNSSDGGRLFQFPDGVQNWPALSIVVIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDESKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYFLTIYVLRRQTLMLLRGHTEEELRNISLNFLKCCCKKGDEEENAPNPNPDQKPRRKKKEKRPRGTMQAINNEKKASKVLGIVFFVFLIMWCPFFITNILSVLCGKACNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSKYLRCDYKPDKKPPVRQIPRVAATALSGRELNVNIYRHTNERVVRKANDTEPGIEMQVENLELPVNPSNVVSERISSV
Protein: Nanos homolog 3 (NOS-3) (P60324)
Organism: Mus musculus (Mouse)
Function: Plays a role in the maintenance of the undifferentiated state of germ cells regulating the spermatogonia cell cycle and inducing a prolonged transit in G1 phase. Affects cell proliferation probably by repressing translation of specific mRNAs. Maintains the germ cell lineage by suppressing both Bax-dependent and -independent apoptotic pathways. Essential in the early stage embryo to protect the migrating primordial germ cells (PGCs) from apoptosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:19861488, ECO:0000269|PubMed:21421998}. Cytoplasm {ECO:0000269|PubMed:19861488, ECO:0000269|PubMed:21421998}. Cytoplasm, Stress granule {ECO:0000269|PubMed:19861488}. Cytoplasm, P-body {ECO:0000269|PubMed:19861488}. Note=Co-localizes with PUM2, EIF2S1 and TIAL1 in the stress granules. Co-localizes with DCP1A in the P-body. {ECO:0000269|PubMed:19861488}.
Interaction partners:
- Dead end protein homolog 1
- Deleted in azoospermia-like
- PR domain zinc finger protein 14
- Pumilio homolog 2
- ATP-dependent RNA helicase DDX4
- Transcription factor AP-2 gamma
- Stimulated by retinoic acid gene 8 protein
- Piwi-like protein 1
- Pumilio homolog 1
Sequence:
MGTFNLWTDYLGLARLVGALHKEEELDVRLDPKPEPKPSSESQQASKESSAAPERLCSFCKHNGESRAIYQSHVLKDEAGRVLCPILRDYVCPQCGATQEHAHTRRFCPLTSQGYTSVYCYTTRNSAGKKLTRPDKAKTQDAGHRLGGEAAAGVYAGSKSGRKPPGPSPSACCPSTTA
Protein: Myosin light polypeptide 6 (G2 catalytic) (LC17-GI) (LC17-NM) (Myosin light chain alkali smooth-muscle/non-muscle isoforms) (P02607)
Organism: Gallus gallus (Chicken)
Function: Regulatory light chain of myosin. Does not bind calcium.
Interaction partners:
- Myosin-11
- Myosin regulatory light chain 2, smooth muscle major isoform
- EF-hand domain-containing protein
- Myosin regulatory light chain 2, smooth muscle minor isoform
- Myosin-9
- Myosin regulatory light chain 2A, cardiac muscle isoform
- Actin, aortic smooth muscle
- Myosin light chain kinase, smooth muscle
- Myosin motor domain-containing protein
- Myosin light chain kinase family member 4.
Sequence:
MCDFSEEQTAEFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVMKVLGNPKSDEMNLKTLKFEQFLPMMQTIAKNKDQGCFEDYVEGLRVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEVEQLVAGHEDSNGCINYEELVRMVLSG
Protein: Uncharacterized protein C513.04 (Q9UT62)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTAKMAEPLYFRIWSSLNIICLMVTFLNVQLSKTPIVLMPLFIALLKNNRKRETKKQTISVLVQKREEKTKLVLDDANNHNHAFLYHCQYLGQKKHVVIQ
Protein: Peroxinectin A (EC 1.11.1.7) (Q6TMK4)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Superoxide-generating NADPH oxidase heavy chain subunit A
- Peroxiredoxin-4
- NADPH oxidase activator
Sequence:
MRLNLISFFIIFTILVSISNSQEFRSYTGEGNNKQNPKQGSIFTPFIRLANPIKFNKNGFPNITNQPSRAISNIIFDQQTHIGSKEHLTDMFNMWGQFLIHNMALSKPEPNSWPIKVPKCDQYFDPACIGNKTMNYFRTRATEVPCDVGKTVVDEDGKCYEQINSLGSYIDGNVLYGNSEEICKNLRSLSGGEMKMTVTDVGDLPPKNVPGVPMDNDANLFPIDQLYSVGERRGNENPGLLSIHTLLLRDHNRLARKFARLHPEWDDERVFQQSRSCIIEQIQKITYDEYLPTTLGSFPSYTGYDANVNAQVSNEFTTTAFRFGHSEVGPFMEYYSENGTRLQPLPIKFSYFNPHALNRGVEPLIRGLIINEEENIDIYMISDLRNFLFGKPGQGGLDLASRNLQRNRDHGIPPYNSLRRQLGLRPVQTWSDITSDPQIQNRLKNAYKSVDDIDSYVGGLAEDHMEGSCVGQTFYLIIYEQFFRTRAGDRFWYETPEMRMVNRECETTTFAEVIKRTTSNIGYVQPNVFRK
Protein: Glutamate racemase (EC 5.1.1.3) (P9WPW9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Interaction partners:
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- O-phosphoserine sulfhydrylase
- Uncharacterized protein Rv1337
- dITP/XTP pyrophosphatase
- Phosphoribosylformylglycinamidine synthase subunit PurQ
- CysO-cysteine peptidase
- Sulfur carrier protein CysO
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Uncharacterized aminopeptidase Rv1333
- Alanine racemase
Sequence:
MNSPLAPVGVFDSGVGGLTVARAIIDQLPDEDIVYVGDTGNGPYGPLTIPEIRAHALAIGDDLVGRGVKALVIACNSASSACLRDARERYQVPVVEVILPAVRRAVAATRNGRIGVIGTRATITSHAYQDAFAAARDTEITAVACPRFVDFVERGVTSGRQVLGLAQGYLEPLQRAEVDTLVLGCTHYPLLSGLIQLAMGENVTLVSSAEETAKEVVRVLTEIDLLRPHDAPPATRIFEATGDPEAFTKLAARFLGPVLGGVQPVHPSRIH
Protein: LP03106p (Q7K1P6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FVATMKAVLCAIFVTLLAAIGQGLPTQLEDENHGSFAGQVSQLIALQLLKFNKDIDANQVHSPLGVASILAMLAEASEGDTYSEFEQVFGYPKDRTKLRDAYKRILGSYQNRDAAVALPSFQTWLYIYRNNSAREEFKDLLEKHYYVDVKDISRQEYDWNEPNTSLQLSEEKDNTDSTEGSTEQSNSKDVIGFETLKRIKLDDEDIPAIPSDGYGQEIIDKEASKFDRDVDDKQYVEKPVAQAEAELLQKEQKQQATTESELESQPEETTTLSVEKQEKPDMAAEENPAEKQQNKRSDQEESQIKNLEENETVQEEEKLAKIMAAPALTAGEPEKVRLPLQKLENAVKTAAKDGADEIMLALESHLPSVSRVNGARSLFQQDDITSALSANSITGRSAGSKSKMLLFNGLYYRGSWANPFYQLRDGSDEFFFMTNEDAVKAPMMHARGKFQVADLPQVKARVLSLPYETSRYALCIVLPDETEGLSDVISQLQTSDFLLAKKQFQMKELHISMPKFQVEETSRSEAMLKQMGLKKVFSRTEAQLSLLSEDPDVHVDEIVQFVNVRVDEGGSSANSLSAATMQARTPSVESTVLPVPEPEPELPGVERFEVNRPFAYFIVDCQEQFVLASGKIYTPEFKEDLPSVSIEVELEQS