wanglab/gogpt-training-data huggingface dataset:
Protein: Glycoprotein hormones alpha chain (Anterior pituitary glycoprotein hormones common subunit alpha) (Follicle-stimulating hormone alpha chain) (FSH-alpha) (Follitropin alpha chain) (Luteinizing hormone alpha chain) (LSH-alpha) (Lutropin alpha chain) (Thyroid-stimulating hormone alpha chain) (TSH-alpha) (Thyrotropin alpha chain) (P01216)
Organism: Mus musculus (Mouse)
Function: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01215}.
Interaction partners:
- Follitropin subunit beta
- Thyrotropin subunit beta
- Follicle-stimulating hormone receptor
- Thyrotropin receptor
- Lutropin subunit beta
- Lutropin-choriogonadotropic hormone receptor
- Prolactin
- Pro-opiomelanocortin
- Osteopontin
- Somatotropin
Sequence:
MDYYRKYAAVILVMLSMFLHILHSLPDGDFIIQGCPECKLKENKYFSKLGAPIYQCMGCCFSRAYPTPARSKKTMLVPKNITSEATCCVAKAFTKATVMGNARVENHTECHCSTCYYHKS
Protein: Formin BNR1 (Q5AAF4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: May organize microtubules by mediating spindle positioning and movement in the budding process. Required for cytokinesis and the maintenance of polarized hyphal growth.
Subcellular location: Bud neck. Cell septum. Note=Localizes only at septal sites in both yeast and hyphal stages.
Interaction partners:
- GTP-binding protein RHO1
- Actin
- Profilin
- Bud6p
- Formin-binding protein
- Cell division control protein 42 homolog
- Ras GTPase-activating-like protein IQG1
- Formin BNI1
- Rga2p
- Pea2p
Sequence:
MNEPPPKRQSVFAKGMKKLQRSKSLLNFAEQAKPPTPENFSSLDPKSNLNSIGLSLVGYGLSSDHLPPPRLDTDSESVSSRTSSPTLHVTTKFNPKQRVESFQTATNFKNQIPPEEIVDQLFEKLLSIRVFPDEAVYSLKKQPVERKWELLLREHETNHHFDLKKLSEQATDKFLTNRDRFQEHEFLIMSRSTTQEPKPKLKPLRIVSGGEDYDDEETPTVTKLVHDDSSTSKLSIESGGSSGAPTETESLLGLVNKKLKIRDGSPDWYVSRIMANKLSLKDCKKLERKLVENNVVKNSGVTWTQGFINAQGETALSVVLTKINKKSIKSNEEFDKEYLIVKCLKHINSEKRDETSSLKEKVYVVKALVFLLVSPRLTTRILVTEVLVMLMLLRDKTLWKSALDGLSSLQDRNGDYVIFQPWLNAFEETIIKYSWSQNKAGELSNLKNYATITLILINSMVDMCSSLKRRISIRRDFGNARILNIFEKLAQIEDTRIDNEIEKYEMYAEEDYNEYVEGKKKRNSKQLPNIPQSKLKLLQVSDFVTTPEANTSLEEDELTPELEDNLSGTESSFDEKSFMTKLKEAEDIESDGAMKSVLQRLMKLKQSERSTEDVHKMLVLVDSMLQHVTNESRVIGTDAHSVLNITIQKLMDRLSTEDMARRAVAESKMLSRQLELVKEEKELLEKELETNKIETIRELKKENYYQAELIATQERQLSKLQQKIEQLQSPNNTALPVVDVGQQGFGNGTVASLKDTSSSSPSKRPPTPPGLYSMQKGSLRGGISAPPMLDFKDARPVSDLQDSRPVSDLQDAPRLVESSAPPLPESKDPVAQPPPPESKDSVAPPPPPVPDFIKSAAPPPPPLPGFMNASAPPPPPVPEFIKSSAPPPPPLPGFITTTPPPPPPLPGFITTTPPPPPMPGMLQPGKVKELGTLFKEKHKQEPQKGITKTKADVVPSIRPKNKLKQMHWDKLENIEKTFWNNLEDSVLSNKLIEQGVLGEVEQVFAAKTATIKKKTAVESQQQPTKKSFLSRDLSQQFGINLHMFANLSEEKLVLKVLRCNSEILENHSVLEFFNNEALVELSDSLFRNLAPYSTDPRTRKKPMKNPEELERADRIFLELCYNLRHYWRSRSRALLFSQTYKKDYIDLMRKLNIVDEANAALKKSESLQNVLGIIRTVGNFMNDDAKQALGFKLDTLQRLKFMKDDQNSMTFLHYIEKIVRHSFPEYGSFVDDLNVLSTLHNISIEQLETDCEEMSRSVKNITDSLERGKLSNKKDLHPEDRILTTISSPMLNAKNKNAMLQSHLKRTAGELNSLMTFFGENPKDATARNTFFYKFVTFITEYKKAHVENIQREEEQRTYEIRKKILEDKIAKKEKLKEESAEPEAVVDTAEESSAVIDSLLEKLKSSTPITTNRAKTKNRRSKALSFYSENPLEIVADTKYESVNNLKRRMTTRKRTTDGETSPKSEQFMSRAQAMLHQLRNKEE
Protein: Endonuclease (EC 3.1.30.-) (Q7JXB9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Endonuclease G inhibitor, isoform A
- Cytochrome c-1
- Cytochrome c-2
- Serine protease HTRA2, mitochondrial
- Ribonuclease Z, mitochondrial
- BG1
- ATP-dependent Clp protease proteolytic subunit
Sequence:
MSAPRVGGVLALGATALGAFYLGTHVERERQHNGSTSGLPRLPGLPTFGTVSAASLIPAQENNVSLTATPSRIGQIMKYGFPGLDHVRSHSDYVLSYDRRNRVPHWVFEHLTAESVAKNDAVDRSKCDFKQDESIHPFFRSQNTDYRRSGYDRGHMAAAGNHRLHQKHCDETFYLSNMAPQVGQGFNRDAWNTLEAHVRRLTKTYSNVYVCTGPLYLPHKEDDGKSYVKYEVIGANTVAVPTHFYKVIVGESADHKLHMESYVMPNQVISNDTPISVFQVPPESVERSAGLLFFDQINRKQLTTINGKKV
Protein: Transmembrane protein 14B (Q9NUH8)
Organism: Homo sapiens (Human)
Function: Primate-specific protein involved in cortical expansion and folding in the developing neocortex. May drive neural progenitor proliferation through nuclear translocation of IQGAP1, which in turn promotes G1/S cell cycle transitions.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEKPLFPLVPLHWFGFGYTALVVSGGIVGYVKTGSVPSLAAGLLFGSLAGLGAYQLYQDPRNVWGFLAATSVTFVGVMGMRSYYYGKFMPVGLIAGASLLMAAKVGVRMLMTSD
Protein: Glucocorticoid receptor (Nuclear receptor subfamily 3 group C member 1) (A0A1D5PRD7)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MDSKELLKSSDQDETRKNALMSTKGGIVMDFHPPFRGGASAQAPVSAAPLPVSSQSDSAQQPALADFSKGLVNNVPPPDLSKAVSLSMGLYMGETDAKVMGNDLGFSQQGQTGISSGETDFRLLEESIASLNKSSSLAEDAKGAVSSEAPLEPDFVGMAGRGPLEPGASVQSQVGSNGGSLKLFSEDQSTLDILQDLELPSVSPGKEPNGSPWRLDPLLDDGGLLSPISADDTFLLEGNLGEDCKPPILSDTKPKINDRGDLLPSSKMPMPQVKTEKEDFIELCTPGIKQENVGPIYCQANFSGSNMLGTKVSAISIHGVSTSGGQMYHYDLNTASLSQQQDQKPIFNIIPSLPAGSENWNRCQGSGDEALAPLGTLNLSGRPAFSNGYSSPGLRSDVSSSPSTTSATAGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQTTATGTREAAEAAGNKSVVPASLPQLTPTLVSLLEVIEPEVLYSGYDSTLPDSSWRIMSTLNMLGGRQVVAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYKQSNGNLLCFAPDLIINEQRMNLPCMYEQCKHMLMVARELSRLQVSYEEYLCMKTLLLLSTIPKEGLKSQTLFEEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHDVVENLLSFCFQTFLDKSMSIEFPEMLAEIISNQIPKYSNGNIKKLLFHQK
Protein: Immunoglobulin lambda variable 2-8 (Ig lambda chain V-II region BO) (Ig lambda chain V-II region MGC) (P01709)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MAWALLLLTLLTQGTGSWAQSALTQPPSASGSPGQSVTISCTGTSSDVGGYNYVSWYQQHPGKAPKLMIYEVSKRPSGVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYAGSNNF
Protein: F-box only protein 40 (P62932)
Organism: Mus musculus (Mouse)
Function: Probable substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex that may function in myogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17928169}.
Interaction partners:
- S-phase kinase-associated protein 1
Sequence:
MGRARKPPPALHRHCEGCFNRHCHVPVEPSVSCLVISCHLLCGATFHMCKESEHTLLCPLEQVPCLNSEYGCPLSMARHKLAKHLQVCPASVVCCSMEWIRWPNVDSETFLHENIMKETPSEECLDTALALQDQKVLFRSLKMVELFPETRDATEEEPDMNGDTSWEETGGAVGGVDARLAPNSCLPATSRQMMELSQEERDALAKTKEGMDLDKFGKWESMFSKEHAASVLTGSLGKSEDKNGDVAGKEQCSSNVRIGDAEGSAERRGPQESQKSQELPATMEMTGLAPWQDGVLERLKTAVDAKDYNMYLVHNGRMLIHFGQMPACTPKERDFVYGNLEAQEVKTVYTFKIPVSYCGKRARLGDAMLKCRPSEHKAVDTSDLGISVEDLPKSDLIKTTLQCALERELKGHVISESRSIDGLFMDLATQTYNFEPEQFSSETVLADLLGTAQPGGLHVELHSECVTRRHNKSSSAFTFTCNKFFRRDEFPLHFKNVHTDIQSSLDGWFQHRCPLAYLGCTFVQNHFRPPGQKAKVIYSQELKTFAIKPEVAPELSEKWKSDHLSGRDGKSLNSLTSLPLEVLQYIAGFLDSISLSQLSQVSVLMRNICATLLQERGMVLSQWKKKRYSHGGTSWKVHNQIWQFSSLFSKINSWEFNDVTSMSEHLKTCPFNIVERKTDPIRLTSMCQPQEKARESLVSTFRARPRGRHF
Protein: Ras-related protein Rab-36 (EC 3.6.5.2) (O95755)
Organism: Homo sapiens (Human)
Function: Protein transport. Probably involved in vesicular traffic (By similarity).
Subcellular location: Golgi apparatus membrane; Lipid-anchor.
Interaction partners:
- Radial spoke head 14 homolog
- Conserved oligomeric Golgi complex subunit 6
- Large ribosomal subunit protein uL23
- RILP-like protein 2
Sequence:
MRSSLTPLGPPVSRDRVIASFPKWYTPEACLQLREHFHGQVSAACQRRNTGTVGLKLSKVVVVGDLYVGKTSLIHRFCKNVFDRDYKATIGVDFEIERFEIAGIPYSLQIWDTAGQEKFKCIASAYYRGAQVIITAFDLTDVQTLEHTRQWLEDALRENEAGSCFIFLVGTKKDLLSGAACEQAEADAVHLAREMQAEYWSVSAKTGENVKAFFSRVAALAFEQSVLQDLERQSSARLQVGNGDLIQMEGSPPETQESKRPSSLGCC
Protein: Monoacylglycerol lipase ABHD2 (EC 3.1.1.23) (2-arachidonoylglycerol hydrolase) (Abhydrolase domain-containing protein 2) (Acetylesterase) (EC 3.1.1.6) (Lung alpha/beta hydrolase 2) (Progesterone-sensitive lipase) (EC 3.1.1.79) (Protein PHPS1-2) (P08910)
Organism: Homo sapiens (Human)
Function: Progesterone-dependent acylglycerol lipase that catalyzes hydrolysis of endocannabinoid arachidonoylglycerol (AG) from cell membrane. Acts as a progesterone receptor: progesterone-binding activates the acylglycerol lipase activity, mediating degradation of 1-arachidonoylglycerol (1AG) and 2-arachidonoylglycerol (2AG) to glycerol and arachidonic acid (AA). Also displays an ester hydrolase activity against acetyl ester, butanoate ester and hexadecanoate ester. Plays a key role in sperm capacitation in response to progesterone by mediating degradation of 2AG, an inhibitor of the sperm calcium channel CatSper, leading to calcium influx via CatSper and sperm activation. May also play a role in smooth muscle cells migration (By similarity).
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000305|PubMed:26989199}; Single-pass type II membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Sperm surface protein Sp17
Sequence:
MNAMLETPELPAVFDGVKLAAVAAVLYVIVRCLNLKSPTAPPDLYFQDSGLSRFLLKSCPLLTKEYIPPLIWGKSGHIQTALYGKMGRVRSPHPYGHRKFITMSDGATSTFDLFEPLAEHCVGDDITMVICPGIANHSEKQYIRTFVDYAQKNGYRCAVLNHLGALPNIELTSPRMFTYGCTWEFGAMVNYIKKTYPLTQLVVVGFSLGGNIVCKYLGETQANQEKVLCCVSVCQGYSALRAQETFMQWDQCRRFYNFLMADNMKKIILSHRQALFGDHVKKPQSLEDTDLSRLYTATSLMQIDDNVMRKFHGYNSLKEYYEEESCMRYLHRIYVPLMLVNAADDPLVHESLLTIPKSLSEKRENVMFVLPLHGGHLGFFEGSVLFPEPLTWMDKLVVEYANAICQWERNKLQCSDTEQVEADLE
Protein: Exosome complex component Rrp41 (EC 3.1.13.-) (Q9UXC2)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Catalytic component of the exosome, which is a complex involved in RNA degradation. Has 3'->5' exoribonuclease activity. Can also synthesize heteromeric RNA-tails. Binds RNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00591}.
Interaction partners:
- Exosome complex component Csl4
- Exosome complex component Rrp4
- Exosome complex component Rrp42
- DNA primase DnaG
- K Homology domain-containing protein
- Ribosomal RNA small subunit methyltransferase Nep1
- Ribosome assembly factor SBDS
- Probable Brix domain-containing ribosomal biogenesis protein
- RNA 3'-terminal phosphate cyclase
- Pre mRNA splicing protein
Sequence:
MREMLQVERPKLILDDGKRTDGRKPDELRSIKIELGVLKNADGSAIFEMGNTKAIAAVYGPKEMHPRHLSLPDRAVLRVRYHMTPFSTDERKNPAPSRREIELSKVIREALESAVLVELFPRTAIDVFTEILQADAGSRLVSLMAASLALADAGIPMRDLIAGVAVGKADGVIILDLNETEDMWGEADMPIAMMPSLNQVTLFQLNGSMTPDEFRQAFDLAVKGINIIYNLEREALKSKYVEFKEEGV
Protein: Complement component 6 (Q91X70)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Complement C5
- Complement component C9
- Complement component C7
- Complement component C8 beta chain
- Complement component C8 gamma chain
- Complement component C8 alpha chain
- ADP/ATP translocase 4
- ADP/ATP translocase 2
- Apoptosis regulator BAX
- ADP/ATP translocase 1
Sequence:
MTRHLTLCFILLVMLIDKSEACFCDHYPWTHWSSCSKSCNSGTQSRQRQVVVNDYYWKNLCDKLCIKQETRECNLQTCPINCVLGDYGTWSDCDPCTEKQVKVKSVLRPSQFGGQPCTEPLVTFQPCVPSKLCKIEETNCKNKFLCDSGRCIPSKLECNGENDCGDNSDERNCGRTKPVCTRIYTPIPSVQLMGTGFHFLAGEPRGEVLDNSFTGGICKLVKTSRASNPYRVSANLENVNFEVQTIEDDLKTEFYKNLISFEKNKNEDSLSVDERTKFFPIPIFHFSEKNEHSHYSSAFNKVIKASHKKDSSFIRIHKLIKVLNFTMKATDLQLSDVFLKALVHLPLEYNSAVYSRIFDDFGTHYFTSGSLGGKYDLIYQFSRQELQNSGLTEEEAQNCVQYETKKLKFLYMEIHKEDTCTKNKLSEKYGGSFLQGSEKSISLVQGGRSQQAAALAWEKGTSGPEENVYSEWLESVKENPAVVDYKLAPITDLVRNIPCAVTKRNNLRRALQEYAAKFDPCQCAPCPNNGRPRLSGTECLCVCQSGTYGENCERRSPGYKSDAVDGNWGCWSSWSACNAAYRRSRTRECNNPAPQRGGQSCGGKDQQEEDCTVSIMENVGQPCINDDEEMKEVDLAEPEAESGCSQPPLPENAFTWNEKKLYSVGEEVEISCLTGFTAVGFQYLRCLPDRTWSQGDVECQRTSCLKPVVQDVLTISPFQRVYQIGESIELTCPRGFVVAGPSRYTCKEDSWTPPISNSLTCEQGVRDHP
Protein: Target of wingless, isoform G (M9PEJ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGCGQSKIHLYPRKSKSKANGKKGGHADSDAETDEDEGHIEDAEKAQQRDREKHDESEELSNKDIQESDEDVAVSLLRAKNLSLLQSHQQNFFRMLDKKIDEGPDYDSASETEIALEEARLNALRQHWESASITASICSSASRSLQTTPIRQVQVPLKQPPRGAGLLIQPSSASAVTASTSSSSSSTIVALPTTEYLPQHVLTGRQVVQQQQQQQQQQAAVLYQQQQQQLILLPQLDPNVVNTSTAAAAAQLVQLQQQHQQQQQQLQLQQQQQLQLNQQQQQQLYQQQQQQYLLTLPAGSKPQSVSPKRLIYGGPAATTLLCATGDVHFSIKCNAPETYEPPTAPHSQIQQQQPPPPPPGAYYGEMMHGVQAAPAAEYKFPPAISVQRLAPQVQRQLRETQELIKDSCPQLYAAGYGSPGPPIRNPSRNPTRTRPTLETQFSQELS
Protein: Trans-3-hydroxy-L-proline dehydratase (T3LHyp dehydratase) (t3HypD) (EC 4.2.1.77) (4-hydroxyproline 2-epimerase) (4Hyp 2-epimerase) (4HypE) (EC 5.1.1.8) (Trans-L-3-hydroxyproline dehydratase) (A9CH01)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Can also catalyze the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), albeit with 30-fold lower efficiency. Is likely involved in both degradation pathways that convert t3LHyp to L-proline and t4LHyp to alpha-ketoglutarate, which would allow A.tumefaciens to grow on t3LHyp or t4LHyp as a sole carbon source. Displays no proline racemase activity.
Interaction partners:
- Cis-3-hydroxy-L-proline dehydratase
- D-amino acid dehydrogenase, small subunit
- Dihydrodipicolinate synthase
- ABC transporter, substrate binding protein
- Delta
Sequence:
MRSIKTVHVISAHAEGEVGDVIVGGVKPPPGETIWEQSRFIARDETLRNFVLNEPRGGVFRHVNLLVPPKHPDADAAFIIMEPEDTPPMSGSNSICVSTVLLDGGIVPMQEPETHMLLEAPGGLVKVRAECRNGKAERIFVQNLPSFAAKLDAELEVEGLGKLKVDTAYGGDSFVIVDAEAMGFSLKPEEAHEIARLGVRITNAANKALGFDHPENPDWRHFSFCLFAGKVERTAEGLRAGAAVAIQPGKVDRSPTGTALSARMAVLHARGEMKEGETLTAVSLIGSTFTGRILGTTTVGDRPAILPEISGRGWITGIHQHMLDPSDPWPEGYRLTDTWGAR
Protein: FI18312p1 (Protein tyrosine phosphatase 52F (EC 3.1.3.48)) (A1ZAB3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MEATNWKQSHRRIHALILILWIAGVQGQTVGSLVAVSESQELAEKVEVTVVSTVYTLGFSISNEADYSIDKVICRNGSGSETEANAAHVCENLNPCTFYTSVVSFRSNVSGKPPPSDQTIYAYTEYKQPKTTVTSVVATANTIKVTWQTNDRACVESFGITAKATDYTKSFQLLNDKSSQTFVNLSACLTHTITLDTRNNASVVVDTDATDVDTQYAEPGDLVMNVTNLASGITMITWGDPSEKNCISNYVFKWQRNDCGTDQNQDTTTDVPSTETTNEIDYVTTTPMETTPDTPSDEVKCEWTDVSSDGKLREYLLTDLQGCDLYTFQVFINENSTAKASQTFTSAEKLVSAVYEPSPTAYPTQLHWTWFSPQNHPKCVANYSVTLTGPIQRSENKTMNVITEETFAIFDDLDPCGIYLVEIVPNQLNGSAGTKYQEQSTVGEDQPSVIQDPVVEAEAYSMEVSWKTPEYADLCIDGYRLSGWMEDDKLVEVEALSITTQNTTVVFDKNLLACQVYIIQIIPYTKENLDGQLRQVGVETKAAIVDYTKVKLEMKNAGSEFIDLIAFNADYNNSCPTIFALFTCNATTQVRNPYAERYVEGHSKQGFNASLSPLSPYATYVCKVILYNVAGPSEPVVDADMHTTTYFPEQPESVMLEKSTVSSLLFNWQPPTYTNGPIKYYQAFLMRHEASYFVPADCAIVEQDTKSETKGDPSVNFTGLAPAVRYMMQVAAQNDFGMGVYTEPVIGITLPAVSDSVTQLTVLTQGPVNNNAVYEANVTITWKVPCKSNGDIEYFQLAFNGTRNNFAPVSFERRVELDTGNKQGRMSYTETEMQPQFDYTVEVSVKNRDVEQLSSSVPGSWQSPAGLPTIPSDELIKQMRANVEETSNPTKTAIVRLPADIMTSASGDIKWMALMISQKNCAGVPHLKYDVSSDWPKVLSYQEAGADGTGDCSLEYQTTEERWHPEPVQRQRRDGEVTSDEEIVFTIGLDKCSEVQKTYCNGPLLPDTDYNVVVRLFTASGYSDAAVLNFKTKAAIKVTLILVSVCSCLLLAFVLGLTVLWVRKRLAWKRDSGQGIEDPFGNVIAKNFAIFYTEVAKPEKLAREFKEITVVALELSYSASELGCHKNRYADIFPYDKNRVILDIDAEGSDYINASFIDGHTRKKEYIATQGPKPESVMDFWRMILQYNVRVIVQVTQFREGNTIKCHEYYPYNVRGLTVTIKSKEVLELYDRTELTVVHDKYGLKEKVIHYYFKKWPDHGVPEDPMHLIMFVKKVKAEKRPSYSPIVVHCSAGVGRTGTFIGLDLIMQRLKSESKINIFETVKKLRFQRMKMVQTQQQYTFLYACTYELVKHKIPRAALKMDGRPKSVTVPAIPSPKKVSFPDVDVGSEYVSSAPITDLDDGRPIVQLPSRFSGLRRNSPPGENDNPTSSSNM
Protein: Dip5p (A0A1D8PCR4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVFGYNSDKGLSNEEKRSSTADLESVITQHTNNYDLYIARSNPSAHNAEEGHQLRQELHARHVSLIAIGGALGTGLLIGTGSALKTAGPGAILVAYGAIGFVVYMVMTALGEIASFIPLPGFANYGKRYADEALGFACGIVYLIKYLVLPANQLTAGALTMQYWVSRDRVNPGVWITVFLVVITFINFLGVKVFGEIEFWMSILKVLTCLGLILLLWIIALGGGPTHERLGFRYWKNPGAFIHYSNSAQDVAIGGSKGRFVAFVSVLVTAVFAYLGSELVAVTFSETRNPRRAIPKAIKLTLYRILVFYILSILFVGMCVSSKDPLLLGAKGTNAGASPFVIAIKNAKIHGLDHLINACILLFVISASNSDMYVCSRSVYSLSVDGYLPKFFSKTNRMGVPYYGVLLSFLFCLLAYMNVSSGSAEVFTYFVNVVSLTGLIAWACILTFHIRFMKALKAQGLDRKKDLVYRSPLQPYGSYISLVICIVIIFIKNFTVFLGDTFDYKNFITGYIVLPVFLIFFFGYKIVYKTKWLKPEEVDLDTFRDVIDAEFEKFEAEEAERKAIREAEGKRFDAQWFYDKFLGWIF
Protein: Glutamate receptor (E7ENK3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}.
Interaction partners:
Sequence:
MEHGTLLAQPGLWTRDTSWALLYFLCYILPQTAPQVLRIGGIFETVENEPVNVEELAFKFAVTSINRNRTLMPNTTLTYDIQRINLFDSFEASRRACDQLALGVAALFGPSHSSSVSAVQSICNALEVPHIQTRWKHPSVDNKDLFYINLYPDYAAISRAILDLVLYYNWKTVTVVYEDSTGLIRLQELIKAPSRYNIKIKIRQLPSGNKDAKPLLKEMKKGKEFYVIFDCSHETAAEILKQILFMGMMTEYYHYFFTTLDLFALDLELYRYSGVNMTGFRLLNIDNPHVSSIIEKWSMERLQAPPRPETGLLDGMMTTEAALMYDAVYMVAIASHRASQLTVSSLQCHRHKPWRLGPRFMNLIKEARWDGLTGHITFNKTNGLRKDFDLDIISLKEEGTEKAAGEVSKHLYKVWKKIGIWNSNSGLNMTDSNKDKSSNITDSLANRTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKELSNILGFIYDVKLVPDGKYGAQNDKGEWNGMVKELIDHRADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYVLLACLGVSCVLFVIARFTPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSSRQQTALVRNSDEGIQRVLTTDYALLMESTSIEYVTQRNCNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEDNKEASALGVENIGGIFIVLAAGLVLSVFVAIGEFIYKSRKNNDIEQKGKSSRIRFYFRNKVRFHGRKKQSLGVEKCLSFNAIMEELGISLKNQKKIKKKSRTKGKSSFTSILTCHQRRTQRKETVA
Protein: Nectin-2 (Herpes virus entry mediator B) (Herpesvirus entry mediator B) (HveB) (Murine herpes virus entry protein B) (mHveB) (Nectin cell adhesion molecule 2) (Poliovirus receptor homolog) (Poliovirus receptor-related protein 2) (CD antigen CD112) (P32507)
Organism: Mus musculus (Mouse)
Function: Modulator of T-cell signaling. Can be either a costimulator of T-cell function, or a coinhibitor, depending on the receptor it binds to. Upon binding to CD226, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Upon interaction with PVRIG, inhibits T-cell proliferation. These interactions are competitive. Probable cell adhesion protein.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q92692}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- T-cell immunoreceptor with Ig and ITIM domains
- CD226 antigen
- Afadin
- Nectin-3
- Nectin-1
- NKG2-D type II integral membrane protein
- Poliovirus receptor related immunoglobulin domain containing
- Cytotoxic and regulatory T-cell molecule
- Nectin-4
- Partitioning defective 3 homolog
Sequence:
MARAAVLPPSRLSPTLPLLPLLLLLLQETGAQDVRVRVLPEVRGRLGGTVELPCHLLPPTTERVSQVTWQRLDGTVVAAFHPSFGVDFPNSQFSKDRLSFVRARPETNADLRDATLAFRGLRVEDEGNYTCEFATFPNGTRRGVTWLRVIAQPENHAEAQEVTIGPQSVAVARCVSTGGRPPARITWISSLGGEAKDTQEPGIQAGTVTIISRYSLVPVGRADGVKVTCRVEHESFEEPILLPVTLSVRYPPEVSISGYDDNWYLGRSEAILTCDVRSNPEPTDYDWSTTSGVFPASAVAQGSQLLVHSVDRMVNTTFICTATNAVGTGRAEQVILVRESPSTAGAGATGGIIGGIIAAIIATAVAGTGILICRQQRKEQRLQAADEEEELEGPPSYKPPTPKAKLEEPEMPSQLFTLGASEHSPVKTPYFDAGVSCADQEMPRYHELPTLEERSGPLLLGATGLGPSLLVPPGPNVVEGVSLSLEDEEEDDEEEDFLDKINPIYDALSYPSPSDSYQSKDFFVSRAMYV
Protein: Striatin N-terminal domain-containing protein (G5EE12)
Organism: Caenorhabditis elegans
Interaction partners:
- DUF3402 domain-containing protein
- Cortactin-binding protein-2 N-terminal domain-containing protein
- Germinal center kinase 1
- Probable serine/threonine-protein phosphatase PP2A regulatory subunit
- Serine/threonine-protein phosphatase 2A catalytic subunit
- MOB-like protein phocein
- FGFR1 oncogene partner 2 homolog
- Programmed cell death protein 10 homolog
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit alpha
Sequence:
MEDASQLSNSQNDKAKDETTRPQYTMSGILHFIQHEWTKNELDRTRWEAERAEMQARIAFLQGERKGQENLKQDLVRRIKMLEFCLKQERAKNYRLTHNGEEPPSLEESPNENSAPSENSHLTADLDAYINDAGEAGGSFRQGRLLLKRYLEEIGYSEHIMDVRSFRVKNLLGLLPQADLPSSERLNGRKEKSDSDSDDGHDDAALDADASKAFEEFDFLNNMDAKEKGSDDDWAGKGASFEKLIKQYKDDPKVKRRSRTSTEESEEKTSNDVQKNLETDVPPGIRSAIDAAAQEELPVRRQGRRSANFGYGNGNELDVALGMQDNDNMDIKDEFKDEDDDPNAQQVKWNIKVTLRSHLDSIRAMQFHPVEPVLFTASEDGLIKLWNLDQKKDEKHNSGGTELEPVYTFRGHKGPVLCLVLSPTGDHLYTGGIDGNICCFNVPSSNGDPFDSYDPRVLTETLTGHTDAIWSVAYHSSNSRLVSASSDSTVRLWEPGNGEPLIRTIGAPKSGILPTSVDFVSTETSHLLAAYTNCYAQIIDIDTGSTVMVFDFGAVTGSPTMNKIVSHPTMPLTLIGGEDRTIRYFDNTNGSIIHEAIAHVEGVSSLAIDPNGLYLLSGSHDGSIRMWNMEKRSCLQEISAHRKKNDSAVTSVAFHPSRSLIGSAGADSLAKVYVSGSN
Protein: Refilin-A (Regulator of filamin protein A) (RefilinA) (Q6ZTI6)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of the perinuclear actin network and nuclear shape through interaction with filamins. Plays an essential role in actin cytoskeleton formation in developing cartilaginous cells.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7TS73}. Note=Colocalizes with FLNA along actin bundle-like structures. {ECO:0000250|UniProtKB:Q7TS73}.
Interaction partners:
- Filamin-A
Sequence:
MVGHLHLQGMEDSLKEQGREGLLDSPDSGLPPSPSPSPPFYSLAPGILDARAGGAGASSEPPGPSEARAPPSQLPNPPASEMRPRMLPVFFGESIKVNPEPTHEIRCNSEVKYASEKHFQDKVFYAPVPTVTAYSETIVAAPNCTWRNYRSQLTLEPRPRALRFRSTTIIFPKHARSTFRTTLHCSLGRPSRWFTASVQLQLCQDPAPSLLGPATL
Protein: Ubiquinol-cytochrome c reductase complex assembly factor 1 (Basic FGF-repressed Zic-binding protein) (mbFZb) (Ubiquinol-cytochrome c reductase complex chaperone CBP3 homolog) (Q9CWU6)
Organism: Mus musculus (Mouse)
Function: Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Involved in cytochrome b translation and/or stability.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9NVA1}. Cytoplasmic vesicle {ECO:0000305}. Note=Cytoplasmic vesicular structures. {ECO:0000305}.
Interaction partners:
- Ubiquinol-cytochrome c reductase complex assembly factor 2
- Ubiquinol-cytochrome-c reductase complex assembly factor 3
- Complex III assembly factor LYRM7
- Testis expressed 51
- Tetratricopeptide repeat protein 19, mitochondrial
Sequence:
MALLVRVLRNQTSISQWVPVCSQLVSVSPTQRQWSSTSQWLQKNQSRVCLGSEQTVGADTAQNRKYHNTSKLLTTQDFPQPVEEKVGPFTKIIEAMGFTGPLKYSKWKIKIAALRMYTSCVEKTDFEEFFLRCQMPDTFNSWFLITLLHVWMCLVRMKQEGRTGKYMCRIIVHFMWEDVEQRGRVMGVNSYILKKNMALMTNNFYAAILGYDEGILSDDHGLAAALWRTFFNQKCEDPRQLELLVEYVRKQMQYLDSMNGEDLLLTGEVRWRPLVEKNPQSILKPHAPTYNDEGL