wanglab/gogpt-training-data huggingface dataset:
Protein: Matrix remodeling-associated protein 8 (Limitrin) (Q9BRK3)
Organism: Homo sapiens (Human)
Function: Transmembrane protein which can modulate activity of various signaling pathways, probably via binding to integrin ITGAV:ITGB3. Mediates heterophilic cell-cell interactions in vitro (By similarity). Inhibits osteoclastogenesis downstream of TNFSF11/RANKL and CSF1, where it may function by attenuating signaling via integrin ITGB3 and MAP kinase p38 (By similarity). Plays a role in cartilage formation where it promotes proliferation and maturation of growth plate chondrocytes (By similarity). Stimulates formation of primary cilia in chondrocytes (By similarity). Enhances expression of genes involved in the hedgehog signaling pathway in chondrocytes, including the hedgehog signaling molecule IHH; may also promote signaling via the PTHLH/PTHrP pathway (By similarity). Plays a role in angiogenesis where it suppresses migration of endothelial cells and also promotes their apoptosis. Inhibits VEGF-induced activation of AKT and p38 MAP kinase in endothelial cells. Also inhibits VTN (vitronectin)-mediated integrin ITGAV:ITGB3 signaling and activation of PTK2/FAK. May play a role in the maturation and maintenance of the blood-brain barrier (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:23386276}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9DBV4}. Cytoplasm {ECO:0000250|UniProtKB:Q9DBV4}. Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q9DBV4}. Nucleus {ECO:0000269|PubMed:23386276}. Note=Primarily localizes to the cell membrane (PubMed:23386276). Detected in the cilium of primary chondrocytes (By similarity). Highly expressed at areas of cell-cell contact and may localize to tight junctions (By similarity). Also found in the nucleus where it is detected in the soluble (as opposed to chromatin-bound) fraction (PubMed:23386276). {ECO:0000250|UniProtKB:Q9DBV4, ECO:0000269|PubMed:23386276}.
Interaction partners:
- Pseudokinase FAM20A
Sequence:
MALPSRILLWKLVLLQSSAVLLHSGSSVPAAAGSSVVSESAVSWEAGARAVLRCQSPRMVWTQDRLHDRQRVLHWDLRGPGGGPARRLLDLYSAGEQRVYEARDRGRLELSASAFDDGNFSLLIRAVEETDAGLYTCNLHHHYCHLYESLAVRLEVTDGPPATPAYWDGEKEVLAVARGAPALLTCVNRGHVWTDRHVEEAQQVVHWDRQPPGVPHDRADRLLDLYASGERRAYGPLFLRDRVAVGADAFERGDFSLRIEPLEVADEGTYSCHLHHHYCGLHERRVFHLTVAEPHAEPPPRGSPGNGSSHSGAPGPDPTLARGHNVINVIVPESRAHFFQQLGYVLATLLLFILLLVTVLLAARRRRGGYEYSDQKSGKSKGKDVNLAEFAVAAGDQMLYRSEDIQLDYKNNILKERAELAHSPLPAKYIDLDKGFRKENCK
Protein: Uncharacterized oxidoreductase YJR096W (EC 1.-.-.-) (P47137)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized protein YNL134C
Sequence:
MVPKFYKLSNGFKIPSIALGTYDIPRSQTAEIVYEGVKCGYRHFDTAVLYGNEKEVGDGIIKWLNEDPGNHKREEIFYTTKLWNSQNGYKRAKAAIRQCLNEVSGLQYIDLLLIHSPLEGSKLRLETWRAMQEAVDEGLVKSIGVSNYGKKHIDELLNWPELKHKPVVNQIEISPWIMRQELADYCKSKGLVVEAFAPLCHGYKMTNPDLLKVCKEVDRNPGQVLIRWSLQHGYLPLPKTKTVKRLEGNLAAYNFELSDEQMKFLDHPDAYEPTDWECTDAP
Protein: Caldesmon 1, isoform CRA_i (Testis secretory sperm-binding protein Li 227n) (A0A140VKA0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDDFERRRELRRQKREEMRLEAERIAYQRNDDDEEEAARERRRRARQERLRQKQEEESLGQVTDQVEVNAQNSVPDEEAKTTTTNTQVEGDDEAAFLERLARREERRQKRLQEALERQKEFDPTITDASLSLPSRRMQNDTAENETTEKEEKSESRQERYEIEETETVTKSYQKNDWRDAEENKKEDKEKEEEEEEKPKRGSIGENQIKDEKIKKDKEPKEEVKSFMDRKKGFTEVKSQNGEFMTHKLKHTENTFSRPGGRASVDTKEAEGAPQVEAGKRLEELRRRRGETESEEFEKLKQKQQEAALELEELKKKREERRKVLEEEEQRRKQEEADRKLREEEEKRRLKEEIERRRAEAAEKRQKMPEDGLSDDKKPFKCFTPKGSSLKIEERAEFLNKSVQKSSGVKSTHQAAIVSKIDSRLEQYTSAIEGTKSAKPTKPAASDLPVPAEGVRNIKSMWEKGNVFSSPTAAGTPNKETAGLKVGVSSRINEWLTKTPDGNKSPAPKPSDLRPGDVSSKRNLWEKQSVDKVTSPTKV
Protein: Integral membrane protein (O05771)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MSGGLFGLLDHVAVLARLAAASIDDIGAAAGRATAKAAGVVIDDTAVTPQYVHRITAERELPIIKRIAIGSVRNKLLLILPGALLLSQLVPWLLTPLLMLGATYLCYEGAEKVCGVIGGRGHDAAPQVAERELVAGAIRTDFILSAEIMVIALNEVADQPFVPRLIVLVIVALVITAAVYGVVAVIVQMDDVGLRLTQTASRFGQRIGGGLVAGMPKLLSALSAVGMGAMLWVGGHIVLVGSDHLGWHAPYRLVHHLDDHLVGSAGGALTWLVSTAACAATGLVIGIVVVALVHLVCFRPPRSRSL
Protein: Low-density lipoprotein receptor-related protein 8 (LRP-8) (Apolipoprotein E receptor 2) (Q14114)
Organism: Homo sapiens (Human)
Function: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (By similarity). Together with its ligand, apolipoprotein E (apoE), may indirectly play a role in the suppression of the innate immune response by controlling the survival of myeloid-derived suppressor cells (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:30873003}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:Q924X6}. Note=Isoforms that contain the exon coding for a furin-type cleavage site are proteolytically processed, leading to a secreted receptor fragment. {ECO:0000250|UniProtKB:Q924X6}.
Interaction partners:
- Apolipoprotein E
- Reelin
- Very low-density lipoprotein receptor
- Beta-2-glycoprotein 1
- Spondin-1
- Disabled homolog 1
- Sorting nexin-17
- Clusterin
- Amyloid beta precursor protein binding family B member 1
- Alpha-2-macroglobulin receptor-associated protein
Sequence:
MGLPEPGPLRLLALLLLLLLLLLLQLQHLAAAAADPLLGGQGPAKDCEKDQFQCRNERCIPSVWRCDEDDDCLDHSDEDDCPKKTCADSDFTCDNGHCIHERWKCDGEEECPDGSDESEATCTKQVCPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCATLCAPHEFQCGNRSCLAAVFVCDGDDDCGDGSDERGCADPACGPREFRCGGDGGGACIPERWVCDRQFDCEDRSDEAAELCGRPGPGATSAPAACATASQFACRSGECVHLGWRCDGDRDCKDKSDEADCPLGTCRGDEFQCGDGTCVLAIKHCNQEQDCPDGSDEAGCLQGLNECLHNNGGCSHICTDLKIGFECTCPAGFQLLDQKTCGDIDECKDPDACSQICVNYKGYFKCECYPGYEMDLLTKNCKAAAGKSPSLIFTNRHEVRRIDLVKRNYSRLIPMLKNVVALDVEVATNRIYWCDLSYRKIYSAYMDKASDPKEQEVLIDEQLHSPEGLAVDWVHKHIYWTDSGNKTISVATVDGGRRRTLFSRNLSEPRAIAVDPLRGFMYWSDWGDQAKIEKSGLNGVDRQTLVSDNIEWPNGITLDLLSQRLYWVDSKLHQLSSIDFSGGNRKTLISSTDFLSHPFGIAVFEDKVFWTDLENEAIFSANRLNGLEISILAENLNNPHDIVIFHELKQPRAPDACELSVQPNGGCEYLCLPAPQISSHSPKYTCACPDTMWLGPDMKRCYRAPQSTSTTTLASTMTRTVPATTRAPGTTVHRSTYQNHSTETPSLTAAVPSSVSVPRAPSISPSTLSPATSNHSQHYANEDSKMGSTVTAAVIGIIVPIVVIALLCMSGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEDEDELHIGRTAQIGHVYPAAISSFDRPLWAEPCLGETREPEDPAPALKELFVLPGEPRSQLHQLPKNPLSELPVVKSKRVALSLEDDGLP
Protein: Opacity protein opA54 (Q04877)
Organism: Neisseria gonorrhoeae
Function: Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation.
Subcellular location: Cell outer membrane.
Interaction partners:
Sequence:
MNPARKKPSLLFSSLLFSSLLFSSLLFSSLLFPSAAQAAGEGNGRGPYVQADLAYAYEHITHDYPEPTGTKKDKISTVSDYFRNIRTHSIHPRVSVGYDFGGWRIAADYARYRKWNNNKYSVNIKELLRNDNANSGGNKHLNIKTRKTEHRENGTFHAASSLGLSAVYDFDTGSRFKPYIGMRVAYGHVRHQVRSVQQETIAVTTYPQNAASSVTTNAPIRKLPHHESRSISSLGFGAVAGVGIDITPKLTLDAGYRYHNWGRLENTRFKTHEASLGVRYRF
Protein: Glucan 1,3-beta-glucosidase (EC 3.2.1.58) (Exo-1,3-beta-glucanase) (GP29) (Soluble cell wall protein 9) (P15703)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:9748433}. Note=Tightly bound to cell wall.
Interaction partners:
- Glucan 1,3-beta-glucosidase I/II
- Glucan 1,3-beta-glucosidase 2
- 1,3-beta-glucan synthase component FKS1
- 1,3-beta-glucan synthase component GSC2
- Invertase 2
- Sporulation-specific glucan 1,3-beta-glucosidase
- 1,3-beta-glucanosyltransferase GAS1
- 1,3-beta-glucan synthase component FKS3
- Exocyst complex component SEC6
- Covalently-linked cell wall protein 14
Sequence:
MRFSTTLATAATALFFTASQVSAIGELAFNLGVKNNDGTCKSTSDYETELQALKSYTSTVKVYAASDCNTLQNLGPAAEAEGFTIFVGVWPTDDSHYAAEKAALQTYLPKIKESTVAGFLVGSEALYRNDLTASQLSDKINDVRSVVADISDSDGKSYSGKQVGTVDSWNVLVAGYNSAVIEASDFVMANAFSYWQGQTMQNASYSFFDDIMQALQVIQSTKGSTDITFWVGETGWPTDGTNFESSYPSVDNAKQFWKEGICSMRAWGVNVIVFEAFDEDWKPNTSGTSDVEKHWGVFTSSDNLKYSLDCDFS
Protein: Pentatricopeptide repeat-containing protein At1g15480, mitochondrial (Q9XI21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At3g02490
- Small ribosomal subunit protein mS77
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- At4g13070
- DEAD-box ATP-dependent RNA helicase 32
- Polynucleotidyl transferase, ribonuclease H-like superfamily protein
- Alba DNA/RNA-binding protein
- Small ribosomal subunit protein mS86
- UBP1-associated proteins 1B
- Mitochondrial import inner membrane translocase subunit TIM14-2
Sequence:
MFALSKVLRRSQSLRLGACNAVYSKLDIPLGERNIAIESNALIHDKHEALPRFYELSWSSSTGRRSLSSDAGAKTTGDDDDLEDKNVDLATPDETSSDSEDGEEFSGDEGDIEGAELELHVPESKRPSEMFKAIVSVSGLSVGSALDKWVEQGKDTNRKEFESAMLQLRKRRMFGRALQMTEWLDENKQFEMEERDYACRLDLISKVRGWYKGEAYIKTIPESFRGELVYRTLLANHVATSNVRTAEAVFNKMKDLGFPLSTFTCNQMLILYKRVDKKKIADVLLLLEKENLKPNLNTYKILIDTKGSSNDITGMEQIVETMKSEGVELDLRARALIARHYASAGLKEKAEKVLKEMEGESLEENRHMCKDLLSVYGYLQREDEVRRVWKICEENPRYNEVLAAILAFGKIDKVKDAEAVFEKVLKMSHRVSSNVYSVLLRVYVDHKMVSEGKDLVKQMSDSGCNIGALTWDAVIKLYVEAGEVEKAESSLSKAIQSKQIKPLMSSFMYLMHEYVRRGDVHNTEKIFQRMKQAGYQSRFWAYQTLIQAYVNAKAPAYGMKERMKADNIFPNKRLAAQLAKADPFKKTPLSDLLD
Protein: Transcobalamin-2 (TC-2) (Transcobalamin II) (TC II) (TCII) (Q9R0D6)
Organism: Rattus norvegicus (Rat)
Function: Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P20062}.
Interaction partners:
- CD320 antigen
- E3 ubiquitin-protein ligase CBL
- Low-density lipoprotein receptor-related protein 2
- Methionine synthase
- Cubilin
Sequence:
MELLKALLLLSGVLGALAEFCVIPKMDGQLVEKLGQRLLPWMDRLSSEQLNPSIYVGLRLSSMQAGTKENLYLHNLKLHYQQCLLRSTSSDDNSGCQTKISGGSLALYLLALRANCELLGSRKGDRMVSQLKWFLEDEKKAIGHHHEGHPHTSYYQYGLSILALCVHRKRVHDSVVGKLLYAVEHDYFTYQGHLSVDTEAMAGLAFTCLERFNFNSDLRPRITTAIETVREKILKAQAPEGYFGNIYSTPLALQMLMTSPGVGLGPACLKARKSLLLSLQDGAFQNPMMISQLLPVLNHKTYLNLISPDCQAPRVMLVPATEDPVHLSEVSVTLKVSSVLPPYERTVSVFAGASLEDVLNRARDLGEFTYGTQASLSGPYLTSVLGKEAGDREYWQLLRVPDTPLLQGIADYKPKNGETIELRLVKM
Protein: Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial (Glu-AdT subunit A) (EC 6.3.5.7) (HMG2-induced ER-remodeling protein 2) (Loss of respiratory capacity protein 6) (Q03557)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). Required for HMG2-induced ER-remodeling.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150, ECO:0000269|PubMed:11914276, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:19417106}.
Interaction partners:
- Glutamyl-tRNA
- Glutamyl-tRNA
- Asparagine--tRNA ligase, mitochondrial
- Asparagine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Glutamate--tRNA ligase, mitochondrial
- Aspartate--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, mitochondrial
- Glutamate--tRNA ligase, cytoplasmic
- Required for respiratory growth protein 7
Sequence:
MPLKRSLKESIERLSSFQSKYNIFTSINPSPYSITNKKGTKETLTGCVASIKDNIVTKDFPTTCASHILENFKSPFDATVVKLLKQAGVHILGKTNLDEFGMGSGGVHSIRGPVINPLYPHEDKKIMGGSSSGAAASVACDLVDFALGTDTGGSVRLPACYGSVLGFKPSYGRLSRFGVIAYSQSLDTVGILSKKINVLRKVFHTLDKYDMKDPTSLSVELRELIEGNKKVRRPLKVGIVKEFSHESMPIGFHRLYLSLLEKLINLGLEIYPVSIPSVKNCLPIYYTLSPAEAASNLSRYDGIRYGYRDSELDIKDGILFAPTRSKFGTEVKNRIILGNYNLCSDAFKNNFIKAEKLRVNLIDEFDGIFRFPNVLTNSKGNPDGLDLLIVPTSSKLPGSIRDFEEEEAKSPANSYINDVFTVPMSLAGLPSLSMPLKEKTPIGLQVVGQYGDDSTVLDFVESIS
Protein: Alanyl-tRNA editing protein AlaX-M (AlaX-M) (AlaXp) (Alanyl-tRNA deacylase AlaX-M) (Q8Q0A4)
Organism: Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Function: Functions in trans to edit the amino acid moiety from mischarged Ser-tRNA(Ala). Recognition depends, at least in part, on the acceptor stem of tRNA(Ala).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MTEALYFLDCYLKEFEATVEKVTEGKYIVLDRTAFYPESGGQPSDTGKLVRERDGAEFKVVYAGKFNGDISHEISPEGETGAEGLKVGDKVKGIIDWDRRYRHMRMHTATHVIANVIEKEAGAQITGNQLGLDQSRVDFSLEAFDREKFAEYEKIANEIIAENHSVNLYLVSRKEAEERLSRLTTLAKGFSEEITEVRLVEIEGVTIEACGGSHLKNTGEIKGIKIEKLQNKGKSNRRMYFSLLDQASGLK
Protein: Centrin, putative (Q57VP6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-repair protein, putative
- Trypanin
- ADP-ribosylation factor-like protein 2
Sequence:
MSTTNRGGNSPVAQSVNRSIAPGMSLSGSALAVLTEEQRQEIKEAFDLFDTDGSGTIDVKELKVAMRALGFEPRKDEVRRLIASTMEERGDPAPVKPGTAPGADNHVIGFAEFVDLMARKMNERDSREEMLKAFHLFDDDKTGKITFKNLKRVAQELGENMTDSEIQEMIDEADRDGDGEVSEEEFLRIMKKTSLY
Protein: L-lactate dehydrogenase C chain (LDH-C) (EC 1.1.1.27) (LDH testis subunit) (LDH-X) (P00342)
Organism: Mus musculus (Mouse)
Function: Possible role in sperm motility.
Subcellular location: Cytoplasm.
Interaction partners:
- Pyruvate kinase PKLR
- Pyruvate kinase PKM
- Putative aspartate aminotransferase, cytoplasmic 2
- Aspartate aminotransferase, cytoplasmic
- Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
- Probable D-lactate dehydrogenase, mitochondrial
- Aspartate aminotransferase, mitochondrial
- Pyruvate carboxylase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- NADP-dependent malic enzyme, mitochondrial
Sequence:
MSTVKEQLIQNLVPEDKLSRCKITVVGVGNVGMACAISILLKGLADELALVDADTNKLRGEALDLLHGSLFLSTPKIVFGKDYNVSANSKLVIITAGARMVSGETRLDLLQRNVAIMKAIVPGIVQNSPDCKIIIVTNPVDILTYVVWKISGFPVGRVIGSGCNLDSARFRYLIGEKLGVNPTSCHGWVLGEHGDSSVPIWSGVNVAGVTLKSLNPAIGTDSDKEHWKNVHKQVVEGGYEVLNMKGYTSWAIGLSVTDLARSILKNLKRVHPVTTLVKGFHGIKEEVFLSIPCVLGQSGITDFVKVNMTAEEEGLLKKSADTLWNMQKDLQL
Protein: Catenin beta 1 (A0A2R8Y5Z1)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}.
Interaction partners:
Sequence:
MELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL
Protein: Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (EC 6.2.1.4) (GTP-specific succinyl-CoA synthetase subunit beta) (G-SCS) (GTPSCS) (Succinyl-CoA synthetase beta-G chain) (SCS-betaG) (P53590)
Organism: Sus scrofa (Pig)
Function: GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03221}.
Interaction partners:
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Citrate synthase, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Acetyltransferase component of pyruvate dehydrogenase complex
Sequence:
IPAAPVAAQARKLLRDLAFRPPLLAARSQVVQLTPRRWLNLQEYQSKKLMSDNGVKVQRFFVADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFSSGLKGGVHLTKDPEVVGQLAKQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEVAASNPELIFKEQIDIIEGIKDSQAQRMAENLGFLGPLQNQAADQIKKLYNLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKESQVYQAFKLLTADPKVEAILVNIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVHEAQNILTNSGLPITSAVDLEDAAKKAVASVTKK
Protein: Protein Wnt-11 (O73864)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. May play a role in the formation of dermal structure in limb buds. Is likely to signal over only few cell diameters (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Tyrosine-protein kinase RYK
- Frizzled class receptor 6
- Frizzled class receptor 7a
- Frizzled class receptor 2
- Frizzled-3
- Low density lipoprotein receptor-related protein 5
- Frizzled-5
- Frizzled-4
- Secreted frizzled-related protein 5.
- Secreted frizzled-related protein 1
Sequence:
MTEYRNFLLLFITSLSVIYPCTGISWLGLTINGSSVGWNQTHHCKLLDGLVPDQQQLCKRNLELMHSIVRAARLTKSACTSSFSDMRWNWSSIESAPHFTPDLAKGTREAAFVVSLAAAVVSHAIARACASGDLPSCSCAAMPSEQAAPDFRWGGCGDNLRYYGLQMGSAFSDAPMRNRRSGPQDFRLMQLHNNAVGRQVLMDSLEMKCKCHGVSGSCSVKTCWKGLQDISTISADLKSKYLSATKVIPRQIGTRRQLVPREMEVRPVGENELVYLVSSPDYCTQNAKQGSLGTTDRQCNKTASGSESCGLMCCGRGYNAYTEVLVERCQCKYHWCCYVSCKTCKRTVERYVSK
Protein: Metalloproteinase inhibitor 4 (Tissue inhibitor of metalloproteinases 4) (TIMP-4) (P81556)
Organism: Rattus norvegicus (Rat)
Function: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor.
Subcellular location: Secreted.
Interaction partners:
- Matrix metalloproteinase-9
- 72 kDa type IV collagenase
- Matrix metalloproteinase-14
- Stromelysin-1
- Neutrophil collagenase
- Matrilysin
- Matrix metalloproteinase-24
- Macrophage metalloelastase
- Matrix metalloproteinase-16
Sequence:
MPWSPLAALSWALVLRLLALLWPPGRGEACSCAPAHPQQHVCHSALVIRAKISSEKVVPASEDPADTQKMIRYEIKQIKMFKGFEKAKDIQYVYTPFDSSLCGVKLETNSQKQYLLTGQILSDGKVFIHLCNYIEPWEDLSLVQRESLNHHYHQNCGCQITTCYAVPCTISAPDECLWTDWLLERKLYGYQAQHYVCMKHVDGICSWYRGHLHLRKEYVDIVQP
Protein: beta-N-acetylhexosaminidase (EC 3.2.1.52) (Q8IRB6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKSTRTALGVALLLALVSQLAAHSSDDLVYGYECRSGYCQKVELSEENYVKAISLPVCRLFCGSSIGTLWPKPTGTVRLDTLMRQVDISFIDFNFNGIARQQKLWRAVEDRFMNMLEAQIPDRKVLARGGYRMSVNINTPDEPTPARLTLDTDESYTLDIDTDASGHVLANITASNFFGARHGLETLAQLIVYDDIRREVQVTANATINDAPVYKWRGLLLDTSRNYYSVKSIKRTLEGMALVKLNTFHWHITDSHSFPLEVKKRPELHKLGAYSQRQVYTRRDVAEVVEYGRVRGIRVMPEFDAPAHVGEGWQHKNMTACFNAQPWKSFCVEPPCGQLDPTVNEMYDVLEDIYGTMFDQFNPDIFHMGGDEVSTSCWNSSQPIQQWMKKQGWGLETADFMRLWGHFQTEALGRVDKVANGTHTPIILWTSGLTEEPFIDEYLNPERYIIQIWTTGVDPKVKKILERGYKIIVSNYDALYLDCGGAGWVTDGNNWCSPYIGWQKVYDNSLKSIAGDYEHHVLGAEGAIWSEQIDEHTLDNRFWPRASALAERLWSNPAEGWRQAESRLLLHRQRLVDNGLGAEAMQPQWCLQNEHECPIDAYDAQV
Protein: Uncharacterized ABC transporter permease Rv0072 (P9WG17)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probably part of an ABC transporter complex. Probably responsible for the translocation of the substrate across the membrane (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized ABC transporter ATP-binding protein Rv0073
- Uncharacterized ABC transporter ATP-binding protein Rv2564
- Uncharacterized ABC transporter ATP-binding protein Rv0986
Sequence:
MLFAALRDMQWRKRRLVITIISTGLIFGMTLVLTGLANGFRVEARHTVDSMGVDVFVVRSGAAGPFLGSIPFPDVDLARVAAEPGVMAAAPLGSVGTIMKEGTSTRNVTVFGAPEHGPGMPRVSEGRSPSKPDEVAASSTMGRHLGDTVEVGARRLRVVGIVPNSTALAKIPNVFLTTEGLQKLAYNGQPNITSIGIIGMPRQLPEGYQTFDRVGAVNDLVRPLKVAVNSISIVAVLLWIVAVLIVGSVVYLSALERLRDFAVFKAIGTPTRSIMAGLALQALVIALLAAVVGVVLAQVLAPLFPMIVAVPVGAYLALPVAAIVIGLFASVAGLKRVVTVDPAQAFGGP
Protein: Epididymis secretory protein Li 52 (V9HWG7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPYEIKKVFASLPQVERGVSKIIGGDPKGNNFLYTNGKCVILRNIDNPALADIYTEHAHQVVVAKYAPSGFYIASGDVSGKLRIWDTTQKEHLLKYEYQPFAGKIKDIAWTEDSKRIAVVGEGREKFGAVFLWDSGSSVGEITGHNKVINSVDIKQSRPYRLATGSDDNCAAFFEGPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIYIYDGKTGEKVCALGGSKAHDGGIYAISWSPDSTHLLSASGDKTSKIWDVSVNSVVSTFPMGSTVLDQQLGCLWQKDHLLSVSLSGYINYLDRNNPSKPLHVIKGHSKSIQCLTVHKNGGKSYIYSGSHDGHINYWDSETGENDSFAGKGHTNQVSRMTVDESGQLISCSMDDTVRYTSLMLRDYSGQGVVKLDVQPKCVAVGPGGYAVVVCIGQIVLLKDQRKCFSIDNPGYEPEVVAVHPGGDTVAIGGVDGNVRLYSILGTTLKDEGKLLEAKGPVTDVAYSHDGAFLAVCDASKVVTVFSVADGYSENNVFYGHHAKIVCLAWSPDNEHFASGGMDMMVYVWTLSDPETRVKIQDAHRLHHVSSLAWLDEHTLVTTSHDASVKEWTITY
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I6AFV6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAALSGGGGSSSGGGGGGGGGGGGGGGGGAEQGQALFNGDMEPEAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGADFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQTPTDVSRNNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPVPQEEAFSAETTLPSGCSSAPPSDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDEKFPEVELQDQRDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSSSTEDRSRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGEFAAFK
Protein: RNA editing complex protein MP61 (Q86MW1)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MERGGRCLFRRWSTRALPSVSHTLRCRGTISNSGGEGNDPIAEPRRVRLVPSAPHGNNSSELFSVGVDPRSHTCDPDDPYSHIQIYRKDMVADAGGRAFQLSVDVPLKKFVDLFSDFDGKRCKLCNESYMQWHSHSSVIPHSGREALMLEMVRAYCGLPEDIAKMWWHRLNTSPAFNRIPKLSHDNSHTRKRRLQYLLKFLKDRDVIRDTFNVHNSSGAAGRSWEFERLEWIGDNVVKYVFNDRFNVIFPVREGGIRGRLGYAQFMIDGNDGLARAYDYLELQKLTLSDRVVSKFKSDVVETLFGELQLYIWSSETDAGTTCYPLPFTGEMFSLRALVWHVMEELAHVMFMYHVEHALAAIQRVVRENQLQFIRADPALRGHADLQSELANTVYAKKAASGPSKLTSTKVSPGARFRDGGASFYHEASNYDGFKRVCTLGGLLPRPFSPRELTSTTSFLPHLQEDSAMTRRVPVDWTRKLFDDCTGNATKKPGAANFVPWQAVTPQPRSRCSAEEAGRSTSRLGIPELKDALLVAELV
Protein: Gamma-aminobutyric acid type A receptor subunit alpha5 (G3V2Q9)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDNGMFSGFIMIKNLLLFCISMNLSSHFGFSQMPTSSVKDETNDNITIFTRILDGLLDGYDNRLRPGLGERITQVRTDIYVTSFGPVSDTEMEYTIDVFFRQSWKDERLRFKGPMQRLPLNNLLASKIWTPDTFFHNGKKSIAHNMTT
Protein: Oxidoreductase, short-chain dehydrogenase/reductase family (P71852)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTLAEAADAINFGLAGRVVLVTGGVRGVGAGISSVFAEQGATVITCARRAVDGQPYEFHRCDIRDEDSVKRLVGEIGERHGRLDMLVNNAGGSPYALAAEATHNFHRKIVELNVLAPLLVSQHANVLMQAQPNGGSIVNICSVSGRRPTPGTAAYGAAKAGLENLTTTLAVEWAPKVRVNAVVVGMVETERSELFYGDAESIARVAATVPLGRLARPADIGWAAAFLASDAASYISGATLEVHGGGEPPPYLGASSANK