wanglab/gogpt-training-data huggingface dataset:
Protein: Metadherin (H0YB56)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPSAWSQDTGDANTNGKDWGRSWS
Protein: AT3g52230/F4F15_340 (Q9SUY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g68680
- Sequence-specific DNA binding transcription factor
- Early endosome antigen
- YlmG homolog protein 1-2, chloroplastic
- Expressed protein
- At4g16450
- Protein KINASE OF THE OUTER CHLOROPLAST MEMBRANE 1
- At3g49350
- V-type proton ATPase subunit c3
- 26S proteasome regulatory particle chain RPT6-like protein
Sequence:
MAEEAQVDRSNGSDSSSPPIKLPPFITNLFAFLQPKPPPATIDANAPKPTGEKEPLKSTYETVTFPYNPPKSAEPIKFEAEPSSGRTSNSVILWQVYALGGFLVLKWAWARWNERNERSDKKEATGDDDQKDDDEDDQSSDGHED
Protein: R3D1 (Q27IS7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FAPRRHYNNLVGLGNGNAVSGSPVKGAPLGQRHVKLKKEKISAQVAQLSQPGQLQLSDVGDPALAGGSGLQGGVGLMGVILPSDEALKFVSETDANGLAMKTPVSILQELLSRRGITPGYELVQIEGAIHEPTFRFRVSFKDKDTPFTAMGAGRSKKEAKHAAARALIDKLIGAQLPESPSSSAGPSVTGLTVAGSGGDGNANATGGGDASDKTVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTLTTQHSNKVSQFHKTLKNATGKKLLRLQKTCLKNNKIDYIKLLGEIATENQFEVTYVDIEEKTFSGQFQCLVQLSTLPVGVCHGS
Protein: Synaptotagmin-3 (Synaptotagmin III) (SytIII) (P40748)
Organism: Rattus norvegicus (Rat)
Function: Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain. Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis. Plays a role in dendrite formation by melanocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11823420}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSGDYEDDLCRRALILVSDLCARIRDADTNDRCQEFNELRIRGYPRGPDADISVSLLSVIVTFCGIVLLGVSLFVSWKLCWVPWRDKGGSAVGGGPLRKDLAPGVGLAGLVGGGGHHLGASLGGHPLLGGPHHHAHPAHHPPFAELLEPGGLGGSEPPEPSYLDMDSYPEAAVASVVAAGVKPSQTSPELPSEGGTGSGLLLLPPSGGGLPSAQSHQQVTSLAPTTRYPALPRPLTQQTLTTQADPSSEERPPALPLPLPGGEEKAKLIGQIKPELYQGTGPGGRRTGGGSGEAGAPCGRISFALRYLYGSDQLVVRILQALDLPAKDSNGFSDPYVKIYLLPDRKKKFQTKVHRKTLNPIFNETFQFSVPLAELAQRKLHFSVYDFDRFSRHDLIGQVVLDNLLELAEQPPDRPLWRDILEGGSEKADLGELNFSLCYLPTAGLLTVTIIKASNLKAMDLTGFSDPYVKASLISEGRRLKKRKTSIKKNTLNPTYNEALVFDVAPESVENVGLSIAVVDYDCIGHNEVIGVCRVGPEAADPHGREHWAEMLANPRKPVEHWHQLVEEKTLSSFTKGGKGLSEKENSE
Protein: Prokineticin receptor 1b (Putative prokineticin receptor) (D3TZW2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Prokineticin
- Prokineticin-1
- NMDA receptor synaptonuclear signaling and neuronal migration factor
- Prokineticin receptor
- DNA helicase
- Uncharacterized protein.
- Heparan-sulfate 6-O-sulfotransferase 1-A
Sequence:
MQDANISHVAAVYVSPHSPVPVLDVHDYTDFYDMMDYGVPAEEMPDTTQGLAYFVATIVIGVVLVCIMLVCGFGNFVFIATLARYKKLRNLTNLLIANLAVSDFIVAVVCCPFLVDYYVVKQLSWDHGKVLCASVNYLRTVSLYVSTNALLAIAVDRYMAIVHPLRPRMKHQTAYCLITGVWVVPVLISIPSAYFASATKVPHGANHSKTFCAQIWTVDQQLYYRSYYLFIFAVEFVGPVLTMALCYLRISKELWFKSVPGFQTEQIRKRLRCRRKTVMVLIGILTAYILCWAPYYGYTILRDFHPTLISREKNSLVAFYIIECIAMSNSMINTFCFVSVKNNTVKYFKRIVLLRWKSTYTSRKSTEETDIHPQTHSECRKGAEISVCHVTHITDD
Protein: Cysteine and histidine-rich domain-containing protein 1 (CHORD domain-containing protein 1) (CHORD-containing protein 1) (CHP-1) (Protein morgana) (Q9UHD1)
Organism: Homo sapiens (Human)
Function: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling. Involved in stress response. Prevents tumorigenesis.
Interaction partners:
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Activator of 90 kDa heat shock protein ATPase homolog 1
- Protein SGT1 homolog
Sequence:
MALLCYNRGCGQRFDPETNSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRHNSEKPPEPVKPEVKTTEKKELCELKPKFQEHIIQAPKPVEAIKRPSPDEPMTNLELKISASLKQALDKLKLSSGNEENKKEEDNDEIKIGTSCKNGGCSKTYQGLESLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTKGKHMWTKKDAGKKVVPCRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFDQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQWASLELPAAKKQEKQKDATTD
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9VYN5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Armadillo segment polarity protein
- Axin
- Protein smoothened
- Kinesin-like protein costa
- Transcriptional activator cubitus interruptus
- CG11379-PA
- C2H2-type domain-containing protein
- Coiled-coil domain-containing protein 25
- Doublecortin-like and CAM kinase-like protein
Sequence:
MERLRSSQNREVRIGNYKVVRKIGCGSFGDIYLGIYIHSGERVAIKVESSKVRHPQLNYERRIYRALRPAHGLPRIRYFHKEEHYQAMVMDLLGPSLERLFQFCERAFTIKTVLLLAEQMLRRVEYVHNRGFLHRDIKPDNFLMGLGTMSKQVYLIDFGLSKKYLDITTGVHIPYREERSLTGTARYASIGAHAGVESARRDDMVAVGYVLMYFNRGSLPWQDLKASTKQQKYERIHEKKISVSIEVLCEGFPCEFTMYLNYCRGMGFYDKPNYDFICRMFRMLRNGLNLRPGLIYDWDMLMMKFHNTQKNPGIGMRVFPPKQKEDDGISGEPIIKDEKCNFWP
Protein: Tubulin beta-8 chain (Beta-8-tubulin) (P29516)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin alpha-6 chain
- Tubulin alpha-2 chain
- Tubulin alpha-5 chain
- Tubulin alpha-1 chain
- Gamma-tubulin complex component 4
- Mitotic spindle checkpoint protein MAD2
- Actin-11
- Tubulin beta-7 chain
- Tubulin alpha-4 chain
- Tubulin beta-5 chain
Sequence:
MREILHIQGGQCGNQIGAKFWEVVCAEHGIDSTGRYQGENDLQLERVNVYYNEASCGRFVPRAVLMDLEPGTMDSVRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSTVCDIPPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEEEGYEYEEDEVEVQEEQ
Protein: Inositol phosphorylceramide synthase catalytic subunit AUR1 (IPC synthase catalytic subunit AUR1) (EC 2.7.1.227) (Aureobasidin A resistance protein) (Phosphatidylinositol:ceramide phosphoinositol transferase) (P36107)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the inositol phosphorylceramide synthase which catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:10888667, ECO:0000269|PubMed:19726565}; Multi-pass membrane protein {ECO:0000269|PubMed:10888667, ECO:0000269|PubMed:19726565}.
Interaction partners:
- Inositol phosphorylceramide synthase regulatory subunit KEI1
- Serine palmitoyltransferase 2
- Serine palmitoyltransferase 1
- Mannosyl phosphorylinositol ceramide synthase regulatory protein CSG2
- Mannosyl phosphorylinositol ceramide synthase SUR1
- Protein ORM2
- Scramblase ANY1
- Ceramide synthase LAC1
- Alkaline ceramidase YPC1
- Ceramide synthase LAG1
Sequence:
MANPFSRWFLSERPPNCHVADLETSLDPHQTLLKVQKYKPALSDWVHYIFLGSIMLFVFITNPAPWIFKILFYCFLGTLFIIPATSQFFFNALPILTWVALYFTSSYFPDDRRPPITVKVLPAVETILYGDNLSDILATSTNSFLDILAWLPYGLFHFGAPFVVAAILFVFGPPTVLQGYAFAFGYMNLFGVIMQNVFPAAPPWYKILYGLQSANYDMHGSPGGLARIDKLLGINMYTTAFSNSSVIFGAFPSLHSGCATMEALFFCYCFPKLKPLFIAYVCWLWWSTMYLTHHYFVDLMAGSVLSYVIFQYTKYTHLPIVDTSLFCRWSYTSIEKYDISKSDPLAADSNDIESVPLSNLELDFDLNMTDEPSVSPSLFDGSTSVSRSSATSITSLGVKRA
Protein: Charged multivesicular body protein 6 (Chromatin-modifying protein 6) (Vacuolar protein sorting-associated protein 20) (Vps20) (hVps20) (Q96FZ7)
Organism: Homo sapiens (Human)
Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. In the ESCRT-III complex, it probably serves as an acceptor for the ESCRT-II complex on endosomal membranes.
Subcellular location: Endomembrane system. Endosome membrane; Lipid-anchor. Late endosome membrane {ECO:0000305}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Localizes to endosomal membranes.
Interaction partners:
- Vacuolar protein sorting-associated protein 4A
- Charged multivesicular body protein 2a
- RNF103-CHMP3 readthrough
- Vacuolar-sorting protein SNF8
- Charged multivesicular body protein 3
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein-sorting-associated protein 25
- Vacuolar protein sorting-associated protein 28 homolog
- Charged multivesicular body protein 4a
- Charged multivesicular body protein 5
Sequence:
MGNLFGRKKQSRVTEQDKAILQLKQQRDKLRQYQKRIAQQLERERALARQLLRDGRKERAKLLLKKKRYQEQLLDRTENQISSLEAMVQSIEFTQIEMKVMEGLQFGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGSFTQEDEDAILEELSAITQEQIELPEVPSEPLPEKIPENVPVKARPRQAELVAAS
Protein: Uncharacterized protein At5g02240 (Q94EG6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase iron-sulfur protein 6
- At1g72040
Sequence:
MANLPTVLVTGASGRTGQIVYKKLKEGSDKFVAKGLVRSAQGKEKIGGEADVFIGDITDADSINPAFQGIDALVILTSAVPKMKPGFDPTKGGRPEFIFEDGQYPEQVDWIGQKNQIDAAKVAGVKHIVVVGSMGGTNPDHPLNKLGNGNILVWKRKAEQYLADSGTPYTIIRAGGLLDKEGGVRELLVGKDDELLQTDTKTVPRADVAEVCIQALLFEEAKNKAFDLGSKPEGTSTPTKDFKALFSQVTSRF
Protein: Ninjurin-1 (Nerve injury-induced protein 1) [Cleaved into: Secreted ninjurin-1 (Soluble ninjurin-1) (sNinJ1)] (O70131)
Organism: Mus musculus (Mouse)
Function: Homophilic transmembrane adhesion molecule involved in various processes such as inflammation, cell death, axonal growth, cell chemotaxis and angiogenesis. Promotes cell adhesion by mediating homophilic interactions via its extracellular N-terminal adhesion motif (N-NAM). Involved in the progression of the inflammatory stress by promoting cell-to-cell interactions between immune cells and endothelial cells. Involved in leukocyte migration during inflammation by promoting transendothelial migration of macrophages via homotypic binding. Promotes the migration of monocytes across the brain endothelium to central nervous system inflammatory lesions (By similarity). Acts as a regulator of Toll-like receptor 4 (TLR4) signaling triggered by lipopolysaccharide (LPS) during systemic inflammation; directly binds LPS. Acts as a mediator of both programmed and necrotic cell death. Plays a key role in the induction of plasma membrane rupture during programmed and necrotic cell death: oligomerizes in response to death stimuli to mediate plasma membrane rupture (cytolysis), leading to release intracellular molecules named damage-associated molecular patterns (DAMPs) that propagate the inflammatory response. Plays a role in nerve regeneration by promoting maturation of Schwann cells. Acts as a regulator of angiogenesis. Promotes the formation of new vessels by mediating the interaction between capillary pericyte cells and endothelial cells. Also mediates vascular functions in penile tissue as well as vascular formation. Promotes osteoclasts development by enhancing the survival of prefusion osteoclasts. Also involved in striated muscle growth and differentiation. Also involved in cell senescence in a p53/TP53 manner, possibly by acting as an indirect regulator of p53/TP53 mRNA translation.
Subcellular location: [Ninjurin-1]: Cell membrane {ECO:0000269|PubMed:24917672, ECO:0000269|PubMed:27815839, ECO:0000269|PubMed:31091274, ECO:0000269|PubMed:33472215, ECO:0000269|PubMed:38396301}; Multi-pass membrane protein {ECO:0000255}. Synaptic cell membrane {ECO:0000269|PubMed:27815839}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Secreted ninjurin-1]: Secreted {ECO:0000269|PubMed:23142597, ECO:0000269|PubMed:32883094}.
Interaction partners:
Sequence:
MESGTEEYELNGDLRPGSPGSPDALPPRWGLRNRPINVNHYANKKSAAESMLDIALLMANASQLKAVVEQGNDFAFFVPLVVLISISLVLQIGVGVLLIFLVKYDLNNPAKHAKLDFLNNLATGLVFIIVVVNIFITAFGVQKPVMDVAPRQ
Protein: Protein translocase subunit SecE (Protein transport protein Sec61 gamma subunit homolog) (Q8TZK2)
Organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Function: Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00422, ECO:0000269|PubMed:20855604}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00422, ECO:0000269|PubMed:20855604}.
Interaction partners:
- Protein translocase subunit SecY
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein eL31
- Transcription elongation factor Spt5
- Signal recognition particle receptor FtsY
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL24
Sequence:
MAELQERIRHFWKESRRAFLVTKKPNWATYKRAAKITGLGIILIGLIGMLIRIVGILILGG
Protein: AMP phosphorylase (AMPpase) (EC 2.4.2.57) (Nucleoside monophosphate phosphorylase) (NMP phosphorylase) (Q5JCX3)
Organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Function: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP, dCMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.
Interaction partners:
- Deoxyribose-phosphate aldolase
- Ribose 1,5-bisphosphate isomerase
- Uridine phosphorylase
- Uracil phosphoribosyltransferase
- Thiamine thiazole synthase
- Peptidyl-prolyl cis-trans isomerase
Sequence:
MKAKIRILDMFSGRYTVLINEEDAKEAKLHPDDLVKIEAGKKAVYGSVALSNLVGKGEVGISRDVLDLHNFSEGETVSVIPAGTPESVRYIKKKMHGEKLRKVEIEAIVRDIVDRKLRDIEISSFVTALEINGLDMDEIAALTIAMAETGDMLDIDRKPIMDVHSIGGVPGNKTNILVVPIVAAAGLTIPKTSSRAITSAAGTADVVEVFADVSFSLDEIKRIVEKVGACLVWGGALNLAPADDITIKAERALSIDPTGLMLASIMSKKYAMGSQYVLIDIPTGKGVKVETVEEARSLARDFIELGKRLGQYVEVAITYGGQPIGHTVGPALEAREALSALMTGKGPGSLIEKATGLAGILLEMGGVAPAGTGKKMAKEILESGKAWEKMKEIIEAQGGDPNIKPEEIPIGDKTYTFTAATSGYVTAIDNRAITAIARAAGAPEDKGAGIELYVKVGEKVKEGDPLFTIHAEHEARLDQAIVLARRTEPIRIEGMVLQRIGNI
Protein: Vacuolar protein sorting-associated protein 8 homolog (Q8N3P4)
Organism: Homo sapiens (Human)
Function: Plays a role in vesicle-mediated protein trafficking of the endocytic membrane transport pathway. Believed to act as a component of the putative CORVET endosomal tethering complexes which is proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Functions predominantly in APPL1-containing endosomes.
Subcellular location: Early endosome {ECO:0000269|PubMed:25266290}.
Interaction partners:
- Vacuolar protein sorting-associated protein 16 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Transforming growth factor-beta receptor-associated protein 1
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 33A
- Vam6/Vps39-like protein
- Vacuolar protein sorting-associated protein 33B
- Ras-related protein Rab-5A
- Vacuolar protein sorting-associated protein 41 homolog
- Charged multivesicular body protein 2a
Sequence:
MENEPDHENVEQSLCAKTSEEELNKSFNLEASLSKFSYIDMDKELEFKNDLIDDKEFDIPQVDTPPTLESILNETDDEDESFILEDPTLLNIDTIDSHSYDTSSVASSDSGDRTNLKRKKKLPDSFSLHGSVMRHSLLKGISAQIVSAADKVDAGLPTAIAVSSLIAVGTSHGLALIFGKDQNQALRLCLGSTSVGGQYGAISALSINNDCSRLLCGFAKGQITMWDLASGKLLRSITDAHPPGTAILHIKFTDDPTLAICNDSGGSVFELTFKRVMGVRTCESRCLFSGSKGEVCCIEPLHSKPELKDHPITQFSLLAMASLTKILVIGLKPSLKVWMTFPYGRMDPSSVPLLAWHFVAVQNYVNPMLAFCRGDVVHFLLVKRDESGAIHVTKQKHLHLYYDLINFTWINSRTVVLLDSVEKLHVIDRQTQEELETVEISEVQLVYNSSHFKSLATGGNVSQALALVGEKACYQSISSYGGQIFYLGTKSVYVMMLRSWRERVDHLLKQDCLTEALALAWSFHEGKAKAVVGLSGDASKRKAIVADRMVEILFHYADRALKKCPDQGKIQVMEQHFQDMVPVIVDYCLLLQRKDLLFSQMYDKLSENSVAKGVFLECLEPYILSDKLVGITPQVMKDLIVHFQDKKLMENVEALIVHMDITSLDIQQVVLMCWENRLYDAMIYVYNRGMNEFISPMEKLFRVIAPPLNAGKTLTDEQVVMGNKLLVYISCCLAGRAYPLGDIPEDLVPLVKNQVFEFLIRLHSAEASPEEEIYPYIRTLLHFDTREFLNVLALTFEDFKNDKQAVEYQQRIVDILLKVMVENSDFTPSQVGCLFTFLARQLAKPDNTLFVNRTLFDQVLEFLCSPDDDSRHSERQQVLLELLQAGGIVQFEESRLIRMAEKAEFYQICEFMYEREHQYDKIIDCYLRDPLREEEVFNYIHNILSIPGHSAEEKQSVWQKAMDHIEELVSLKPCKAAELVATHFSGHIETVIKKLQNQVLLFKFLRSLLDPREGIHVNQELLQISPCITEQFIELLCQFNPTQVIETLQVLECYRLEETIQITQKYQLHEVTAYLLEKKGDIHGAFLIMLERLQSKLQEVTHQGENTKEDPSLKDVEDTMVETIALCQRNSHNLNQQQREALWFPLLEAMMAPQKLSSSAIPHLHSEALKSLTMQVLNSMAAFIALPSILQRILQDPVYGKGKLGEIQGLILGMLDTFNYEQTLLETTTSLLNQDLHWSLCNLRASVTRGLNPKQDYCSICLQQYKRRQEMADEIIVFSCGHLYHSFCLQNKECTVEFEGQTRWTCYKCSSSNKVGKLSENSSEIKKGRITPSQVKMSPSYHQSKGDPTAKKGTSEPVLDPQQIQAFDQLCRLYRGSSRLALLTELSQNRSSESYRPFSGSQSAPAFNSIFQNENFQLQLIPPPVTED
Protein: Zinc finger MYND domain-containing protein 19 (Melanin-concentrating hormone receptor 1-interacting zinc finger protein) (MCH-R1-interacting zinc finger protein) (Q9CQG3)
Organism: Mus musculus (Mouse)
Function: May be involved as a regulatory molecule in GPR24/MCH-R1 signaling.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Armadillo repeat-containing protein 8
Sequence:
MTDFKLGIVRLGRVAGKTKYTLIDEQDIPLVESYSFEARMEVDADGNGAKIFAYAFDKNRGRGSGRLLHELLWERHRGGVAPGFQVVHLNAVTVDNRLDNLQLVPWGWRPKAEETSSKQREQSLYWLAIQQLPTDPIEEQFPVLNVTRYYNANGDVVEEEENSCTYYECHYPPCTVIEKQLREFNICGRCQVARYCGSQCQQKDWPAHKKHCRERKRPFQHELEPER
Protein: H(+)/Cl(-) exchange transporter 3 (Chloride channel protein 3) (ClC-3) (Chloride transporter ClC-3) (P51791)
Organism: Mus musculus (Mouse)
Function: May influence large dense-core vesicle exocytosis in adrenal chromaffin cells.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:18923035}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 1]: Lysosome membrane {ECO:0000269|PubMed:26342074, ECO:0000269|PubMed:28972156}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:28972156}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P51792}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:P51790}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Early endosome membrane {ECO:0000269|PubMed:16222710}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:26342074, ECO:0000269|PubMed:28972156}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:16222710, ECO:0000269|PubMed:28972156}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000269|PubMed:26342074}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:26342074, ECO:0000269|PubMed:28972156}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000269|PubMed:24603049}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Bestrophin-1
Sequence:
MESEQLFHRGYYRNSYNSITSASSDEELLDGAGAIMDFQTSEDDNLLDGDTAAGTHYTMTNGGSINSSTHLLDLLDEPIPGVGTYDDFHTIDWVREKCKDRERHRRINSKKKESAWEMTKSLYDAWSGWLVVTLTGLASGALAGLIDIAADWMTDLKEGICLSALWYNHEQCCWGSNETTFEERDKCPQWKTWAELIIGQAEGPGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDCGPLESSSLCDYRNDMNASKIVDDIPDRPAGVGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDWFIFKEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNGYPFLDAKEEFTHTTLAADVMRPRRSDPPLAVLTQDNMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESARKKQEGIVGSSRVCFAQHTPSLPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKDILRHMAQTANQDPASIMFN
Protein: Exosome complex component CSL4 homolog (Q9XXD2)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000269|PubMed:34365510, ECO:0000269|PubMed:36763670}. Nucleus, nucleolus {ECO:0000269|PubMed:34365510, ECO:0000269|PubMed:36763670}. Nucleus, nucleoplasm {ECO:0000269|PubMed:36763670}. Note=As a part of exosome complex, translocates from the nucleolus to nucleoplasm in response to cold-warm shock. {ECO:0000269|PubMed:36763670}.
Interaction partners:
- Exosome complex component RRP46 homolog
- Ribosomal RNA-processing protein 42
- Exosome complex component RRP4 homolog
- Exosome complex component RRP40
- Exosome complex component RRP45
- Putative exosome complex component RRP41
- Nuclear nucleic acid-binding protein C1D
- Exoribonuclease phosphorolytic domain-containing protein
- Ribosomal RNA-processing protein 43
- Probable exosome complex exonuclease RRP44
Sequence:
MLAETLVAPGDKVLDAIGEYRMGKGLYEANRRIFASVAGFVNVYGFRDKSDNLVQVIEVRRSEDQLDNELLPFHGAIVTAKVMAVGLRFAKCDIISIGDKVYKKRFSALLPKKKLRPLEPELSEPFKNFVRPNDYILAKVCEDAEIKDKFVLSIAEDELGVVLCRGRFGEPMQKVDWNTVVSTRTGKTEPRKMAKVPQKCTLPTQSVA