wanglab/gogpt-training-data huggingface dataset:
Protein: Protein Wnt-5a (P22725)
Organism: Mus musculus (Mouse)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. In the presence of FZD4, activates beta-catenin signaling. In the presence of ROR2, inhibits the canonical Wnt pathway by promoting beta-catenin degradation through a GSK3-independent pathway which involves down-regulation of beta-catenin-induced reporter gene expression. Suppression of the canonical pathway allows chondrogenesis to occur and inhibits tumor formation. Stimulates cell migration. Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor. Mediates motility of melanoma cells (By similarity). Required during embryogenesis for extension of the primary anterior-posterior axis and for outgrowth of limbs and the genital tubercle. Inhibits type II collagen expression in chondrocytes (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:17117926}.
Interaction partners:
- Tyrosine-protein kinase transmembrane receptor ROR2
- Tyrosine-protein kinase RYK
- Frizzled-3
- Frizzled-4
- Frizzled-2
- Frizzled-5
- Frizzled-9
- Nuclear receptor ROR-alpha
- Frizzled-6
- Frizzled-7
Sequence:
MKKPIGILSPGVALGTAGGAMSSKFFLMALATFFSFAQVVIEANSWWSLGMNNPVQMSEVYIIGAQPLCSQLAGLSQGQKKLCHLYQDHMQYIGEGAKTGIKECQYQFRHRRWNCSTVDNTSVFGRVMQIGSRETAFTYAVSAAGVVNAMSRACREGELSTCGCSRAARPKDLPRDWLWGGCGDNIDYGYRFAKEFVDARERERIHAKGSYESARILMNLHNNEAGRRTVYNLADVACKCHGVSGSCSLKTCWLQLADFRKVGDALKEKYDSAAAMRLNSRGKLVQVNSRFNSPTTQDLVYIDPSPDYCVRNESTGSLGTQGRLCNKTSEGMDGCELMCCGRGYDQFKTVQTERCHCKFHWCCYVKCKKCTEIVDQFVCK
Protein: Ectonucleoside triphosphate diphosphohydrolase 7 (NTPDase 7) (EC 3.6.1.15) (Lysosomal apyrase-like protein 1) (Q9NQZ7)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner. Preferentially hydrolyzes nucleoside 5'-triphosphates, with substrate preference for UTP > GTP > CTP. Hydrolyzes ATP and nucleoside diphosphates only to a minor extent.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:11278936}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MARISFSYLCPASWYFTVPTVSPFLRQRVAFLGLFFISCLLLLMLIIDFRHWSASLPRDRQYERYLARVGELEATDTEDPNLNYGLVVDCGSSGSRIFVYFWPRHNGNPHDLLDIKQMRDRNSQPVVKKIKPGISAMADTPEHASDYLRPLLSFAAAHVPVKKHKETPLYILCTAGMRLLPERKQLAILADLVKDLPLEFDFLFSQSQAEVISGKQEGVYAWIGINFVLGRFDHEDESDAEATQELAAGRRRTVGILDMGGASLQIAYEVPTSTSVLPAKQEEAAKILLAEFNLGCDVQHTEHVYRVYVTTFLGFGGNFARQRYEDLVLNETLNKNRLLGQKTGLSPDNPFLDPCLPVGLTDVVERNSQVLHVRGRGDWVSCGAMLSPLLARSNTSQASLNGIYQSPIDFNNSEFYGFSEFFYCTEDVLRIGGRYHGPTFAKAAQDYCGMAWSVLTQRFKNGLFSSHADEHRLKYQCFKSAWMYQVLHEGFHFPYDYPNLRTAQLVYDREVQWTLGAILYKTRFLPLRDLRQEGVRQAHGSWFRLSFVYNHYLFFACILVVLLAIFLYLLRLRRIHHRQTRASAPLDLLWLEEVVPMMGVQVGP
Protein: Serine/threonine-protein kinase PDIK1L (EC 2.7.11.1) (PDLIM1-interacting kinase 1-like) (Q8N165)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:14631099}.
Interaction partners:
- CTD small phosphatase-like protein 2
- Retinal guanylyl cyclase 2
- Receptor-type tyrosine-protein phosphatase kappa
- Ubiquitin-like-conjugating enzyme ATG3
- Autophagy protein 5
- Phosphoinositide 3-kinase regulatory subunit 4
- UPF0688 protein C1orf174
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Ubiquitin-like protein ATG12
Sequence:
MVSSQPKYDLIREVGRGSYGVVYEAVIRKTSARVAVKKIRCHAPENVELALREFWALSSIKSQHPNVIHLEECILQKDGMVQKMSHGSNSSLYLQLVETSLKGEIAFDPRSAYYLWFVMDFCDGGDMNEYLLSRKPNRKTNTSFMLQLSSALAFLHKNQIIHRDLKPDNILISQTRLDTSDLEPTLKVADFGLSKVCSASGQNPEEPVSVNKCFLSTACGTDFYMAPEVWEGHYTAKADIFALGIIIWAMLERITFIDTETKKELLGSYVKQGTEIVPVGEALLENPKMELLIPVKKKSMNGRMKQLIKEMLAANPQDRPDAFELELRLVQIAFKDSSWET
Protein: Fesur1p (Q5ADP7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase iron-sulfur protein 4
- 4Fe-4S ferredoxin-type domain-containing protein
- Ribosomal protein/NADH dehydrogenase domain-containing protein
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase chain 2
- Uncharacterized protein
- Zinc finger CHCC-type domain-containing protein
- Cytochrome b-c1 complex catalytic subunit, mitochondrial
Sequence:
MYSLSKRTLFQQLNKRISSTTTSSTIIPLSSLSSSSHISTRRYVSTKELTPQTLPTDFPLMSEKKATNAADYVLTSLDMIANWARKSSFWPVTFGLACCAVEMMHVSAPRYDQDRLGIIFRASPRQSDIMIVAGTLTNKMAPALRQVYDQMPDPKWVISMGSCANGGGYYHYSYSVVRGCDRVIPVDIYVPGCPPTAEALMYGVFQLQKKMMKTRITRLWYRS
Protein: NAD kinase 2 (F4HY34)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MFLCFCPCHVPIMSRLSPATGISSRLRFSIGLSSDGRLIPFGFRFRRNDVPFKRRLRFVIRAQLSEAFSPDLGLDSQAVKSRDTSNLPWIGPVPGDIAEVEAYCRIFRSAERLHGALMETLCNPVTGECRVPYDFSPEEKPLLEDKIVSVLGCILSLLNKGRKEILSGRSSSMNSFNLDDVGVAEESLPPLAVFRGEMKRCCESLHIALENYLTPDDERSGIVWRKLQKLKNVCYDAGFPRSDNYPCQTLFANWDPIYSSNTKEDIDSYESEIAFWRGGQVTQEGLKWLIENGFKTIVDLRAEIVKDTFYQTALDDAISLGKITVVQIPIDVRMAPKAEQVELFASIVSDSSKRPIYVHSKEGVWRTSAMVSRWKQYMTRPITKEIPVSEESKRREVSETKLGSNAVVSGKGVPDEQTDKVSEINEVDSRSASSQSKESGRFEGDTSASEFNMVSDPLKSQVPPGNIFSRKEMSKFLKSKSIAPAGYLTNPSKILGTVPTPQFSYTGVTNGNQIVDKDSIRRLAETGNSNGTLLPTSSQSLDFGNGKFSNGNVHASDNTNKSISDNRGNGFSAAPIAVPPSDNLSRAVGSHSVRESQTQRNNSGSSSDSSDDEAGAIEGNMCASATGVVRVQSRKKAEMFLVRTDGVSCTREKVTESSLAFTHPSTQQQMLLWKTTPKTVLLLKKLGQELMEEAKEEVHEKLLVFQICFQAASFLYHQENMNVLVEPEVHDVFARIPGFGFVQTFYIQDTSDLHERVDFVACLGGDGVILHASNLFKGAVPPVVSFNLGSLGFLTSHPFEDFRQDLKRVIHGNNTLDGVYITLRMRLRCEIYRKGKAMPGKVFDVLNEIVVDRGSNPYLSKIECYEHDRLITKVQGDGVIVATPTGSTAYSTAAGGSMVHPNVPCMLFTPICPHSLSFRPVILPDSAKLELKIPDDARSNAWVSFDGKRRQQLSRGDSVRIYMSQHPLPTVNKSDQTGDWFRSLIRCLNWNERLDQKAL
Protein: MAP kinase kinase mkk-4 (EC 2.7.12.2) (Q20347)
Organism: Caenorhabditis elegans
Function: Activity is required in presynaptic neurons, in a dose-dependent manner, for normal presynaptic development and morphology. Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15707898}.
Interaction partners:
- Stress-activated protein kinase jnk-1
- GLH-binding kinase 1
- Stress-activated protein kinase JNK
- Beta-arrestin arr-1
- Serine/threonine-protein kinase akt-1
- Serine/threonine-protein kinase akt-2
- Cell death abnormality protein 2
- mitogen-activated protein kinase kinase
- Calponin-homology
- Calponin-homology
Sequence:
MVQEDDENLRNSMSLRPTSLSTRPTSLSVNGNEKTLPEESVLRSLSTGTLKYPDDEHLYTFSSANLQDLGAIGNGNFGTVYKMRHKETGKLIAVKRIRCNNIGHREQIRLLREHDTIVKSEKGPNIVKFYGAIFSEGDCWICMELMDISMDLLYKRVYMVKNSRLNENVVGHITVCTVDALDYLKKELKIIHRDVKPSNILVDGTGAVKLCDFGICGQLEESFAKTHDAGCQPYLAPERITSSDKYDVRSDVWSLGITLYEIATGKFPYQEWNSLFDQIATVVSGDPPILHPDSDDFHYSLPLVKFINTCLTKDRRHRPKYDTLKSFDFYRIYAVAGPEIEEAKRILGVEAIDTRNHPVDHRG
Protein: Protein SYS1 homolog (Q8N2H4)
Organism: Homo sapiens (Human)
Function: Involved in protein trafficking. May serve as a receptor for ARFRP1.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15077113}; Multi-pass membrane protein {ECO:0000269|PubMed:15077113}.
Interaction partners:
- ADP-ribosylation factor-related protein 1
- ADP-ribosylation factor-like protein 3
- Conserved oligomeric Golgi complex subunit 3
- Guanine nucleotide exchange factor subunit RIC1
Sequence:
MAGQFRSYVWDPLLILSQIVLMQTVYYGSLGLWLALVDGLVRSSPSLDQMFDAEILGFSTPPGRLSMMSFILNALTCALGLLYFIRRGKQCLDFTVTVHFFHLLGCWFYSSRFPSALTWWLVQAVCIALMAVIGEYLCMRTELKEIPLNSAPKSNV
Protein: Insulin-like growth factor 2 (Insulin-like growth factor II) (Q9PUD0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000406}.
Interaction partners:
Sequence:
MDDYHVFCASCRKTEETRTTMRSLIVFVLSLSMLISNVTAGETLCGGELVDTLQFVCGEDGFYISRPNRSNSRRPQRGIVEECCFRSCELHLLQQYCAKPVKSERDVSSTSLQVFPVSQALHKDTINVKYSKYEVWQQKAAQRLRRGVPSILLARKFRRQMEKIQDEEQTSFHRPLMTLPNRQPAIVPHVQISTSRK
Protein: FERM domain-containing protein (Krev interaction trapped/cerebral cavernous malformation 1 isoform a) (G5EDH0)
Organism: Caenorhabditis elegans
Interaction partners:
- Forkhead box protein O
- WW domain-containing protein
- Integrin Cytoplasmic domain-Associated Protein homolog
- Sorting nexin-17 homolog
- 3-ketosteroid oxygenase
- Nuclear hormone receptor family member daf-12
- CCM gene homolog
Sequence:
MAEVSVAIVRLKISALSDKAIPSAQDFEICVKEEPSTAKNFGPVKHDYNIKKRVTVGGHTIGADVFKLPNFSFEPSKVSTLEDMIHDYFKRTGNIIRRSVRIPLHDDLHQPSSSTKPFVGHVPGLSLVCVPVFNKESVEVANSRYENLQKMVNLCHNQPEMFDIHTKNMILILERWLIDSQTFDSYFLSHFFMKESSRTRIKTCVHNPAFIDLQEQCIRHMSHSVRSNVSSASADLDDRVHVANIAKIAMLRYNKFTISVINPAFNPNFASEDSSCVYFYPGIKQCRAQRAASSTSQDMRSRLYPLHKAAEDGNAEEIRRFLKIGMDSNLRDDDSWTPLHYACFHGHLEVVHELLNSPQMTAINAQNKGGATALQYAVINGNEYLVEILTSHASIDVNIQNNEGYRPIDYCGNHPAIQKILELQIFKSKINVDTSIGSFSIKSRSPEEATVGEVLDRLAEETQLNREQMNCFALFVYSESMSLQLQPDSLIDGKLKVDKWNTTIRKLVGDIPFETPRLKLKRNAYATARMEIVTKVDNNSFAWSTILDEAIHSYLAGHLIANSKEEITKFAAIVCRTMHGRDFKPSSKNLSNLYPQYMLDNHDRGKLADRLKAQLRKNETQNDMQLEAEFISMARGLVTYGASFFDVDVFTKKSMGTEQGLVGVNDHGLHIIFKKTWTVKNFRFDEFTASNKESKTLEIDAQRVRDSYYILVSTQMKFLTGILRKFQKS
Protein: Adhesion G protein-coupled receptor E2 (EGF-like module receptor 2) (EGF-like module-containing mucin-like hormone receptor-like 2) (CD antigen CD312) (Q9UHX3)
Organism: Homo sapiens (Human)
Function: Cell surface receptor that binds to the chondroitin sulfate moiety of glycosaminoglycan chains and promotes cell attachment. Promotes granulocyte chemotaxis, degranulation and adhesion. In macrophages, promotes the release of inflammatory cytokines, including IL8 and TNF. Signals probably through G-proteins. Is a regulator of mast cell degranulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22310662, ECO:0000269|PubMed:26841242}; Multi-pass membrane protein. Cell projection, ruffle membrane {ECO:0000269|PubMed:17928360}; Multi-pass membrane protein. Note=Localized at the leading edge of migrating cells. {ECO:0000269|PubMed:17928360}.
Interaction partners:
- Complement decay-accelerating factor
- Lysophosphatidic acid receptor 1
- Guanine nucleotide-binding protein subunit alpha-12
- CD59 glycoprotein
Sequence:
MGGRVFLVFLAFCVWLTLPGAETQDSRGCARWCPQDSSCVNATACRCNPGFSSFSEIITTPMETCDDINECATLSKVSCGKFSDCWNTEGSYDCVCSPGYEPVSGAKTFKNESENTCQDVDECQQNPRLCKSYGTCVNTLGSYTCQCLPGFKLKPEDPKLCTDVNECTSGQNPCHSSTHCLNNVGSYQCRCRPGWQPIPGSPNGPNNTVCEDVDECSSGQHQCDSSTVCFNTVGSYSCRCRPGWKPRHGIPNNQKDTVCEDMTFSTWTPPPGVHSQTLSRFFDKVQDLGRDYKPGLANNTIQSILQALDELLEAPGDLETLPRLQQHCVASHLLDGLEDVLRGLSKNLSNGLLNFSYPAGTELSLEVQKQVDRSVTLRQNQAVMQLDWNQAQKSGDPGPSVVGLVSIPGMGKLLAEAPLVLEPEKQMLLHETHQGLLQDGSPILLSDVISAFLSNNDTQNLSSPVTFTFSHRSVIPRQKVLCVFWEHGQNGCGHWATTGCSTIGTRDTSTICRCTHLSSFAVLMAHYDVQEEDPVLTVITYMGLSVSLLCLLLAALTFLLCKAIQNTSTSLHLQLSLCLFLAHLLFLVAIDQTGHKVLCSIIAGTLHYLYLATLTWMLLEALYLFLTARNLTVVNYSSINRFMKKLMFPVGYGVPAVTVAISAASRPHLYGTPSRCWLQPEKGFIWGFLGPVCAIFSVNLVLFLVTLWILKNRLSSLNSEVSTLRNTRMLAFKATAQLFILGCTWCLGILQVGPAARVMAYLFTIINSLQGVFIFLVYCLLSQQVREQYGKWSKGIRKLKTESEMHTLSSSAKADTSKPSTVN
Protein: Syncytin-2 (ERV-FRD provirus ancestral Env polyprotein) (Envelope polyprotein) [Cleaved into: Surface protein (SU); Transmembrane protein (TM)] (P61556)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. The interaction with MFSD2A is apparently important for this process (By similarity).
Subcellular location: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Surface protein]: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=The surface protein is not anchored to the membrane, but localizes to the extracellular surface through its binding to TM. {ECO:0000250|UniProtKB:Q9UQF0}.; SUBCELLULAR LOCATION: [Transmembrane protein]: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium-dependent lysophosphatidylcholine symporter 1
- FA complementation group M
Sequence:
MGLLLLVLILTPLLAAYRHPDFPLLEKAQQLLQSTGSPYSTNCWLCTSSSTETPGTAYPASPREWTSIEAELHISYQWDPNLKGLMTPANSLLSTVKQDFPDIRQKPPIFGPIFTNINLMGKAPICVTAKRKNGTNVGTLPSTVCNVTFTVDPNQQTYQTYTHNQFRHQPRFPKPPNITFPQGTLLDKSTQFCQGRPSSCRTRNFWFRPADYNQCLQIPNLSSPAEWVLLDQTRNSLFWENKTKGANQSQTPCIQVLAGMTIATSYLGISPVSEFFGTSLTPLFHFHISTCLKTQGAFYICGQSIHQCLPTNWTGTCTIGYVTPDIFIAPGNLSLPIPIYGNSQLPRARRAIHFIPLLAGLGILAGTGTGIAGITKASFTYSQLSKEIAKNIDTMAKTLTTVQEQIDSLAAVVLQNRRGLDMLTAAQGGICLALDEKCCFWVNQSGKVQDNIRQLLNQASSLRERATQGWLNWEGTWKWFSWVLPFIGPLVSLLLLLLFGPCLLNLITQFVSSRLQAIKLQTNGAGCRPRNIQESPF
Protein: Long-chain fatty acid transport protein 1 (Arachidonate--CoA ligase) (EC 6.2.1.15) (Fatty acid transport protein) (Fatty acid transport protein 1) (FATP-1) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Solute carrier family 27 member 1) (Very long-chain acyl-CoA synthetase) (EC 6.2.1.-) (P97849)
Organism: Rattus norvegicus (Rat)
Function: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport at the plasma membrane. Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane-associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Probably involved in fatty acid transport across the blood barrier (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15848183, ECO:0000269|PubMed:19380575}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q60714}. Endomembrane system {ECO:0000269|PubMed:15848183}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q60714}. Cytoplasm {ECO:0000269|PubMed:15848183}. Note=Plasma membrane and intracellular membranes, at least in adipocytes. In adipocytes, but not myocytes, insulin via the mTORC1 signaling pathway induces a rapid translocation of SLC27A1 from intracellular compartments to the plasma membrane, paralleled by increased LCFA uptake. Insulin-dependent translocation from the cytoplasm to the cell membrane is regulated by EPRS1. Predominantly cytoplasmic in myocytes. {ECO:0000250|UniProtKB:Q60714}.
Interaction partners:
- Diacylglycerol O-acyltransferase 2
- Arachidonate--CoA ligase
- Platelet glycoprotein 4
- Beta-alanine-activating enzyme
- Lysosome membrane protein 2
- Aspartate aminotransferase, mitochondrial
- Fatty acid-binding protein, intestinal
- Scavenger receptor class B member 1
- Fatty acid synthase
- Long-chain-fatty-acid--CoA ligase 1
Sequence:
MRTPGAGTASVASLGLLWLLGLPWTWSAAAAFGVYVGSGGWRFLRIVCKTARRDLFGLSVLIRVRLELRRHRRAGDTIPRIFQAVAQRQPERLALVDASSGICWTFAQLDTYSNAVANLFLQLGFAPGDVVAVFLEGRPEFVGLWLGLAKAGVVAALLNVNLRREPLAFCLGTSAAKALIYGGEMAAAVAEVSEQLGKSLLKFCSGDLGPESVLPDTQLLDPMLAEAPTTPLAQAPGKGMDDRLFYIYTSGTTGLPKAAIVVHSRYYRIAAFGHHSYSMRANDVLYDCLPLYHSAGNIMGVGQCIIYGLTVVLRKKFSASRFWDDCVKYNCTVVQYIGEICRYLLRQPVRDVERRHRVRLAVGNGLRPAIWEEFTQGFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILTHVYPIRLVKVNEDTMEPLRDSQGLCIPCQPGEPGLLVGQINQQDPLRRFDGYVSDSATNKKIAHSVFRKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEAVLSRLLGQTDVAVYGVAVPGVEGKSGMAAIADPHNQLDPNSMYQELQKVLASYAQPIFLRLLPQVDTTGTFKIQKTRLQREGFDPRQTSDRLFFLDLKQGRYLPLDERVHARICAGDFSL
Protein: Toll-like receptor 5b (F8W3J5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Myeloid differentiation primary response protein MyD88
- Toll-like receptor 5
- Chemokine
- Mucin 5.3.
- Interleukin family protein
Sequence:
MIRAHRMGYTFILILFGLCLNTEVVKSTSECSVIGYNAICINRGLHQVPELPAHVNYVDLSLNSIAELNETSFSRLQDLQFLKVEQQTPGLVIRNNTFRGLSSLIILKLDYNQFLQLETGAFNGLANLEVLTLTQCNLDGAVLSGNFFKPLTSLEMLVLRDNNIKKIQPASFFLNMRRFHVLDLTFNKVKSICEEDLLNFQGKHFTLLRLSSITLQDMNEYWLGWEKCGNPFKNTSITTLDLSGNGFKESMAKRFFDAIAGTKIQSLILSNSYNMGSSFGHTNFKDPDNFTFKGLEASGVKTCDLSKSKIFALLKSVFSHFTDLEQLTLAQNEINKIDDNAFWGLTHLLKLNLSQNFLGSIDSRMFENLDKLEVLDLSYNHIRALGDQSFLGLPNLRKLNLTGNAVESVHTFAALPNLNKLYLGKNRISSVSSLPNIAHNLSTLDLEFNKLHALSDLYTILREFPQIENIFLQGNTFSSCYNQKQIVLSDKLQLLHLGLSSMQLIWSEGKCLNVFADLHQLQQLSLTANGLQSLPKDIFKDLTSLFFLDLSFNSLKYLPTDVFPKSLQILNLDYNSIYSVDPNLFSTLSYLSLMNNDFRCDCDLKDFQTWLNQTNVTFVHPIEDVTCASPEDQYMVPVVKSSIQCENEEEERRTEKLRLVLFIVCTVLIILFTASTIVYISRRGVIFKMYKKLIGELVDGKREEPDPDRFLYDVYLCFSSKDMKWVERALLKRLDSQFSEHNTLRCCFEERDFIPGEDHLTNMRSAIQNSRKTICVVSEHFLKDGWCLETFTLAQKRMQAELEDILVVLVVGNIPQYRLLKYKQVRSFIENRSYLVWPDDCQDLEWFYDQLLHKIRKDIKINQTTKEIKREEANFNTNTAV
Protein: Diacylglycerol O-acyltransferase 2 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase 2) (Q54GC1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- phosphatidate phosphatase
- PA-phosphatase related-family protein DDB_G0284367
- Serine aminopeptidase S33 domain-containing protein
- Uncharacterized protein
- Lipase
- Diacylglycerol kinase A
- Seipin
- Pseudouridine synthase RsuA/RluA-like domain-containing protein
- RNA-binding S4 domain-containing protein
Sequence:
MVRFVPWNVPLYRRLETMAVAIYAMVLPVCLIMAFNLIVIPLFWGIAIPYLVWMFYFDTKHESGGRRVSLVRNSILWRYFRDYFPISLIINSNYDPKKNYIFAYHPHGIISIGAFCNFATNANNIDEKLPGLKVHLLTLESNFKIPFLRDVLMSFGMSSVSKKSCENILNSGAGESICLVVGGAEESLDARPGLNEITLKKRKGFIKLALVNGASLVPVYSFGENDIYDQVPNPRGSLVRKIQTKIKDLTGIAPPLFMGRGIFNYDFGLLPVRHKIVTVVGEPIDIPKIKSPTDQVIEHYHQIYVEALQNLFDKHKNSCADKETGNLKIN
Protein: E3 ubiquitin-protein ligase RNF25 (EC 2.3.2.27) (RING finger protein 25) (RING finger protein AO7) (Q7SXJ6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27007149}.
Interaction partners:
Sequence:
MAAESDVLSEIEVLQSIYLDELNVTQNDEGGWTVSLVLHPSTAEDCLSQFVRLTLTMDLDSQYPYSSPYISIHNPRGLSDDKLLSLQKSLQMEAEECVGTPVLYQLIERAKEILTDSNIPHGNCVICLYDFKEGEVFTKTSCYHYFHSHCLGRYITHSEMELKDRERELEEDKTRDRTEEEELAVVCPVCRESLTYDLDALLSSPAPVLCQQEDAVIGGEFKKKWEALQKILERQKEKGGVIDPEAESNRFLIHINEAPVNLSDTPGMTDSSGAESSQSLPSSSPDSTSTTQTSQNQHTAGQPQRKHTGDFKRGRRGRGAGRGGPARHMVPAPGEERLGKHIQSSDKINSANSGPTNTTSQVESTAQRQACELSENTAQLRQPLTNEENKPVSQDMLTSEPKDGQEVSQQKECISKEVTQTILQEGHPEREHVGRGDKRGSRGSARHHGHWQDRNYKGPGHWDNSGSAGHRGGAYRTREGGAGRGHRGGGAYRGGGRGMHQRVEKEFRKEGVL
Protein: Ferredoxin--NAD(P)(+) reductase fdr (EC 1.18.1.2) (EC 1.18.1.3) (Carbazole 1,9a-dioxygenase, ferredoxin reductase component) (CARDO) (D5IGG6)
Organism: Sphingomonas sp
Function: Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol.
Interaction partners:
Sequence:
MTDTHYDVVIVGAGHGGAQTAIALRQNGFAGTIAIIGAEPDLPYERPPLSKEYLAAEKGFERILIRPASFWNDRHIAMHLGCAVERVDPTQRLVFLADGRSMGYGDLVWCAGGSARRLDCTGHDLGGVHYVRTRADTDALAAELPGVSKVVIIGGGYIGLEAAAVMAKFGKNVTLIEALDRVLARVAGEPLSRFFEEKHRSRGVDVRLRTKVGCLLGQDGRVTHVELNDADPIPADLVIVGIGIIPAISPLVVAGAKASNGLLVDASGRTSIPHVYALGDCAAHVNSFAPNDIPIRLESVQNANDQAVVVARTICGTAAQYHAVPWFWSSQYDIRLQTVGLTAGYDQTFVRGDPATGSFTVVYGRDGRVIALDCVNATKDYVQGKRLVEAKALIEPGMTDPQYPLKNFMTPSPA
Protein: V-type proton ATPase subunit E2 (V-ATPase subunit E2) (Vacuolar H(+)-ATPase subunit E isoform 2) (Vacuolar proton pump subunit E2) (Q9C9Z8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity).
Subcellular location: Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit F
- V-type proton ATPase catalytic subunit A
- Vacuolar ATP synthase catalytic subunit-related / V-ATPase-related / vacuolar proton pump-like protein
- V-type proton ATPase subunit H
- V-type proton ATPase subunit C
- V-type proton ATPase subunit d1
- V-type proton ATPase subunit d2
Sequence:
MNDADVSKQIQQMVRFIRQEAEEKANEISISAEEEFNIERLQLLESAKRKLRQDYDRKLKQVDIRKRIDYSTQLNASRIKYLQAQDDVVTAMKDSAAKDLLRVSNDKNNYKKLLKSLIIESLLRLKEPSVLLRCREMDKKVVESVIEDAKRQYAEKAKVGSPKITIDEKVFLPPPPNPKLPDSHDPHCSGGVVLASQDGKIVCENTLDARLDVAFRQKLPQIRTRLVGAPETSRA
Protein: DNA repair exonuclease (EC 3.1.-.-) (Q8NR87)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Interaction partners:
- ATPase involved in DNA repair
- UmuC domain-containing protein
- DNA polymerase I
- Uncharacterized protein
- ABC-type transporter, ATPase component
- Superfamily II DNA/RNA helicases, SNF2 family
- ATP-dependent DNA helicase RecQ
- DNA repair protein RecN
- SWIM-type domain-containing protein
- Error-prone DNA polymerase
Sequence:
MSTVHDEMGVMNTTVKFLHSSDLQIGMTRWFLSDEAQARFDDDRIRAIEKMGKIARKNQCEFIVLAGDVFEHNSLEQRTTGRALEALRSLKLPVYLLPGNHDPLTADSLFYRAKDIDGVTILSDTTVHGVAPGVEIIGAPLLHKMATSDLVAEALKDLEPTSNVRIAVGHGQAEARTTDHRADLIDLNTVEAKLADGTIDYLALGDTHSAQPVGTSGKVWFSGAPETTDFHDLDPDRVGGEVNSGKVLIVSASKGDVSVEEVEVGKWTFHALSKEITSGTDVEDFLDTLQAYPDKSRTVIKYGLRGTITLEQNRRLEEGIAGLEDVFASLKPRERTTDLVLEPGEEELANLDATGYAAEVLRELADSVVNGAAPEEDRDALNLLFRLSREV
Protein: Cortactin-binding protein-2 N-terminal domain-containing protein (Q95QQ9)
Organism: Caenorhabditis elegans
Interaction partners:
- MOB-like protein phocein
- DUF3402 domain-containing protein
- Striatin N-terminal domain-containing protein
- Serine/threonine-protein phosphatase 2A catalytic subunit
- Programmed cell death protein 10 homolog
- Germinal center kinase 1
- Probable serine/threonine-protein phosphatase PP2A regulatory subunit
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit beta
Sequence:
MPNLLDDSFDPTFQSTSKKLVLPSIRKVQPEYDNLPEEQGVNDFSSDELMKLLSFMEGEVQAREDVIDHLKRERTKILLSEAKYGKLNMNDPFAALRRDSAITGEQIDEEKIVQMYESQVDQLDKMMAVQKQSQRNAAVLLVALEKKQYKLVKKLEADREAKIRYAKQGDDLVAHLEKERNQLQQQIEFHIEEKRKAEIAKDKMEMTLGNEKKRHESIVLYLIQERKQMLLKMHELRVKAEQIMLQNQNDPTKPGPSSALSERELIEELKKEVTFLRAERESLTKTQKMVKTENLSLRETVRGQEADLQMLRRNLTLTGAKMSIDKPGNVLPQLPPDTGSLIMANRGAKPAVNRQQPAPPPVARLPNSATFPTEKSRLPRAPPPAVTTPVPRMSIGSLPASSSNVPRTMSSPVKKTPVMGVSSTAVRRPQSAATTTMPTTSVITNTSAVMPLSPDLEQLEAAIQSMNVVTASPPAYSTAMAKRSSSLPREANNNPPGAPIRRSTMNGGMHTSTTGVVSTRIAGPSSNVASERKLSGTVKRNGILAKAFGSSK
Protein: Protein Wnt-2b (Q98SN7)
Organism: Gallus gallus (Chicken)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway. Acts as an upstream regulator of FGF10 in the lateral plate mesoderm during limb initiation in the embryo.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q93097}. Secreted {ECO:0000250|UniProtKB:Q93097}.
Interaction partners:
- Low-density lipoprotein receptor-related protein
- Wnt inhibitory factor 1
- Porcupine O-acyltransferase.
- Notum, palmitoleoyl-protein carboxylesterase.
- Frizzled-1
- Frizzled-4
- Secreted frizzled-related protein 1
- Cerberus
- Secreted frizzled-related protein 2
- Frizzled-3
Sequence:
MLSPNRLAASPGIAVAPGRAECGAFPRTAGAAPRICLPFVLILLALTPRADSSWWYIGALGARVICDNIPGLVNKQRQLCQRYPDIMQSVGEGAKEWIRECQYQFRHHRWNCSTLDRDHTVFGRVMLRSSREAAFVYAISSAGVVYAITRACSQGELKACGCDPLKRGRAKDERGEFDWGGCSDNINYGIRFAKAFVDAKEKKVKDARALMNLHNNRCGRMAVKRFLKLECKCHGVSGSCTLRTCWLAMSDFRKTGDYLQKKYNGAIQVIMNQDGTGFTVANKNFRKPTKTDLVYFENSPDYCVMDKSAGSLGTAGRVCNKVSRGTDGCEVMCCGRGYDTTRVTRVTKCECKFHWCCAVRCKECEDTVDVHTCKAPKRAEWLDQT