wanglab/gogpt-training-data huggingface dataset:
Protein: Calcium-binding protein NCSA (Neuronal calcium sensor 1 homolog) (Q75K28)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May prevent cells from entering development prematurely in the presence of environmental nutrients.
Interaction partners:
- Probable serine/threonine-protein kinase roco11
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco8
Sequence:
MGNQLGTLKKEEVELLQNSSHFDSRELRALYKQFRKDSPSGTINKQEFKEIMTQMGVGDQFLQDLLFNVFDKNKDSTINFQEFVCGLSSITRGTPEEKIEFAFSLYDIDGNGYITRSEMESILESMYKLVGTFVTCSGKKFDPHDLIEEFFDSMDDDGDGYISLEEYKRGTLKNPDIIQGLKLLNQ
Protein: Uncharacterized response regulatory protein Rv3143 (P9WGL7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- NADH-quinone oxidoreductase subunit J
- NADH-quinone oxidoreductase subunit G
- NADH-quinone oxidoreductase subunit C
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit D
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit N
Sequence:
MPDSSTALRILVYSDNVQTRERVMRALGKRLHPDLPDLTYVEVATGPMVIRQMDRGGIDLAILDGEATPTGGMGIAKQLKDELASCPPILVLTGRPDDTWLASWSRAEAAVPHPVDPIVLGRTVLSLLRAPAH
Protein: Interleukin-13 receptor subunit alpha-2 (IL-13 receptor subunit alpha-2) (IL-13R subunit alpha-2) (IL-13R-alpha-2) (IL-13RA2) (CD antigen CD213a2) (O88786)
Organism: Mus musculus (Mouse)
Function: Binds as a monomer with high affinity to interleukin-13 (IL13).
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:Q14627}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14627}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
Interaction partners:
- Interleukin-13
- Interleukin-4 receptor subunit alpha
- Interleukin-4
- Interleukin-13 receptor subunit alpha-1
- Cytosolic non-specific dipeptidase
- Interleukin-6
- Insulin-like growth factor-binding protein 3 receptor
- Interferon gamma
- Interleukin-5
- Ephrin type-A receptor 2
Sequence:
MAFVHIRCLCFILLCTITGYSLEIKVNPPQDFEILDPGLLGYLYLQWKPPVVIEKFKGCTLEYELKYRNVDSDSWKTIITRNLIYKDGFDLNKGIEGKIRTHLSEHCTNGSEVQSPWIEASYGISDEGSLETKIQDMKCIYYNWQYLVCSWKPGKTVYSDTNYTMFFWYEGLDHALQCADYLQHDEKNVGCKLSNLDSSDYKDFFICVNGSSKLEPIRSSYTVFQLQNIVKPLPPEFLHISVENSIDIRMKWSTPGGPIPPRCYTYEIVIREDDISWESATDKNDMKLKRRANESEDLCFFVRCKVNIYCADDGIWSEWSEEECWEGYTGPDSKIIFIVPVCLFFIFLLLLLCLIVEKEEPEPTLSLHVDLNKEVCAYEDTLC
Protein: Endoglucanase H (EC 3.2.1.4) (Cellulase H) (Endo-1,4-beta-glucanase H) (EgH) (P16218)
Organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
Function: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Interaction partners:
- Thermostable beta-glucosidase B
- Glycosyltransferase 36
- Cellulosomal-scaffolding protein A
- Glycosyltransferase 36
- Beta-glucosidase A
- Glycoside hydrolase family 5
- Beta-glucosidase
- Cellulase/esterase CelE
Sequence:
MKKRLLVSFLVLSIIVGLLSFQSLGNYNSGLKIGAWVGTQPSESAIKSFQELQGRKLDIVHQFINWSTDFSWVRPYADAVYNNGSILMITWEPWEYNTVDIKNGKADAYITRMAQDMKAYGKEIWLRPLHEANGDWYPWAIGYSSRVNTNETYIAAFRHIVDIFRANGATNVKWVFNVNCDNVGNGTSYLGHYPGDNYVDYTSIDGYNWGTTQSWGSQWQSFDQVFSRAYQALASINKPIIIAEFASAEIGGNKARWITEAYNSIRTSYNKVIAAVWFHENKETDWRINSSPEALAAYREAIGAGSSNPTPTPTWTSTPPSSSPKAVDPFEMVRKMGMGTNLGNTLEAPYEGSWSKSAMEYYFDDFKAAGYKNVRIPVRWDNHTMRTYPYTIDKAFLDRVEQVVDWSLSRGFVTIINSHHDDWIKEDYNGNIERFEKIWEQIAERFKNKSENLLFEIMNEPFGNITDEQIDDMNSRILKIIRKTNPTRIVIIGGGYWNSYNTLVNIKIPDDPYLIGTFHYYDPYEFTHKWRGTWGTQEDMDTVVRVFDFVKSWSDRNNIPVYFGEFAVMAYADRTSRVKWYDFISDAALERGFACSVWDNGVFGSLDNDMAIYNRDTRTFDTEILNALFNPGTYPSYSPKPSPTPRPTKPPVTPAVGEKMLDDFEGVLNWGSYSGEGAKVSTKIVSGKTGNGMEVSYTGTTDGYWGTVYSLPDGDWSKWLKISFDIKSVDGSANEIRFMIAEKSINGVGDGEHWVYSITPDSSWKTIEIPFSSFRRRLDYQPPGQDMSGTLDLDNIDSIHFMYANNKSGKFVVDNIKLIGATSDPTPSIKHGDLNFDNAVNSTDLLMLKRYILKSLELGTSEQEEKFKKAADLNRDNKVDSTDLTILKRYLLKAISEIPI
Protein: Serine protease inhibitor A3N (Serpin A3N) (Q91WP6)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Transcription factor PU.1
- Haptoglobin
Sequence:
MAFIAALGLLMAGICPAVLCFPDGTLGMDAAVQEDHDNGTQLDSLTLASINTDFAFSLYKELVLKNPDKNIVFSPLSISAALAVMSLGAKGNTLEEILEGLKFNLTETSEADIHQGFGHLLQRLNQPKDQVQISTGSALFIEKRQQILTEFQEKAKTLYQAEAFTADFQQPRQAKKLINDYVRKQTQGMIKELVSDLDKRTLMVLVNYIYFKAKWKVPFDPLDTFKSEFYAGKRRPVIVPMMSMEDLTTPYFRDEELSCTVVELKYTGNASALFILPDQGRMQQVEASLQPETLRKWKNSLKPRMIDELHLPKFSISTDYSLEDVLSKLGIREVFSTQADLSAITGTKDLRVSQVVHKAVLDVAETGTEAAAATGVKFVPMSAKLYPLTVYFNRPFLIMIFDTETEIAPFIAKIANPK
Protein: Alpha-xylosidase (EC 3.2.1.177) (Q5AW25)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the liberation of alpha-xylose from the non-reducing terminal glucose of xyloglucan oligosaccharides.
Subcellular location: Secreted {ECO:0000305|PubMed:16844780}.
Interaction partners:
Sequence:
MKFTEGMWLLREGIRIDWMSNVERLNVDKDTVNLLLNKFQRHRGDTLNSSTVSARVTSPLEGIIGVKLVHWAGGLDNGPHYELNTSAGHTEITHEKGKNLKYTSGRLELDINIAPNELAFTFTTGADGQDKRKKLTGHSFRSIGYVGDSTTPKSQLSDGIFYERQGYTLAELDLSVGEKLYGLGERFGPFVKNGQSVNIWNEDGGTSSELAYKNIPFYISSNGYGVFVNHPGKVSLELQSERTTRVNVSVEGEELEYFVIEGKNPKEILKRWTDLTGKPALVPAWSYGLWLTTSFTTNYSERTVTGFLDGFKDRNLPLSVFHFDCFWMKSYQWCDFEFDADMFPDAAGYLARLKERGLKLSIWINPYVGQASPLFEIGKREGYFIKRIDGSVWQWDLWQAGMAVVDFTNPAACSWYTGHLKRLMDLGIDTFKTDFAERIPFKNITYHDGSDPARMHNYYALLYNKVVYETMTSISGKSNSLLFARSTSVGGQKYPVHWGGDCESTYEAMAESLRGGLSLGLAGYIFWASDIGGFEGTPPPALYKRWVQFGLLSSHSRLHGSSSFRVPWIYGEDCSDVLRDCVKRKISLTPYLLAEALNGHRSGTPLMRPMFMEFPEDLNTYPLDTQYMFGSNLLVAPVFSDEGIVTFYVPRTPEEEGRKQWISWFDHGKKYEGGRWYTETHGFDTLPILIRPGSVTPINYKLEKPEGNPLDGLEILVNGSIDKEVEIEIVDPETTHKVLKVMTVSERETENGVEVIARLDGVDGNENSVKVNWVGHGVTK
Protein: Gustatory and odorant receptor 21a (Q9VPT1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gustatory and odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. Gr21a and Gr63a together are sufficient for carbon dioxide detection and avoidance behavior. It is possible that the CO(2) receptors Gr63a and Gr21a activate the TRPC channels through Galpha49B and Plc21C. This innate olfactory avoidance behavior can be inhibited by inhibitory interactions of the odors such as 1-hexanol and 2,3-butanedione with Gr21a and Gr63a.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Gustatory and odorant receptor 63a
- Odorant receptor coreceptor
- Glycine--tRNA ligase
- Odorant receptor 22a
- Odorant receptor 67d
- Gustatory receptor for bitter taste 93a
- Odorant receptor 85b
- Putative odorant receptor 92a
- Odorant receptor 42b
- Ionotropic receptor 8a
Sequence:
MTFLDRTMSFWAVSRGLTPPSKVVPMLNPNQRQFLEDEVRYREKLKLMARGDAMEEVYVRKQETVDDPLELDKHDSFYQTTKSLLVLFQIMGVMPIHRNPPEKNLPRTGYSWGSKQVMWAIFIYSCQTTIVVLVLRERVKKFVTSPDKRFDEAIYNVIFISLLFTNFLLPVASWRHGPQVAIFKNMWTNYQYKFFKTTGSPIVFPNLYPLTWSLCVFSWLLSIAINLSQYFLQPDFRLWYTFAYYPIIAMLNCFCSLWYINCNAFGTASRALSDALQTTIRGEKPAQKLTEYRHLWVDLSHMMQQLGRAYSNMYGMYCLVIFFTTIIATYGSISEIIDHGATYKEVGLFVIVFYCMGLLYIICNEAHYASRKVGLDFQTKLLNINLTAVDAATQKEVEMLLVAINKNPPIMNLDGYANINRELITTNISFMATYLVVLLQFKITEQRRIGQQQA
Protein: Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (DLDH) (O00087)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes (By similarity). Malfunction of this protein blocks the progression of cell cycle from G1 to S phase.
Subcellular location: Mitochondrion matrix {ECO:0000305}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Probable pyruvate dehydrogenase protein X component, mitochondrial
- Probable aminomethyltransferase, mitochondrial
- Putative glycine dehydrogenase
- Putative glycine cleavage system H protein, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
Sequence:
MLNSVIKRSALCRFKFTCLQVSECRPAQIEISKRLYSAKASGNGEYDLCVIGGGPGGYVAAIRGAQLGLKTICVEKRGTLGGTCLNVGCIPSKALLNNSHIYHTVKHDTKRRGIDVSGVSVNLSQMMKAKDDSVKSLTSGIEYLFKKNKVEYAKGTGSFIDPQTLSVKGIDGAADQTIKAKNFIIATGSEVKPFPGVTIDEKKIVSSTGALSLSEVPKKMTVLGGGIIGLEMGSVWSRLGAEVTVVEFLPAVGGPMDADISKALSRIISKQGIKFKTSTKLLSAKVNGDSVEVEIENMKNNKRETYQTDVLLVAIGRVPYTEGLGLDKLGISMDKSNRVIMDSEYRTNIPHIRVIGDATLGPMLAHKAEDEGIAAVEYIAKGQGHVNYNCIPAVMYTHPEVAWVGITEQKAKESGIKYRIGTFPFSANSRAKTNMDADGLVKVIVDAETDRLLGVHMIGPMAGELIGEATLALEYGASAEDVARVCHAHPTLSEATKEAMMAAWCGKSIHF
Protein: Inositol monophosphatase 2 (IMP 2) (IMPase 2) (EC 3.1.3.25) (Inositol-1(or 4)-monophosphatase 2) (Myo-inositol monophosphatase A2) (O14732)
Organism: Homo sapiens (Human)
Function: Can use myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. Has been implicated as the pharmacological target for lithium Li(+) action in brain.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17068342}.
Interaction partners:
- Inositol-3-phosphate synthase 1
- Inositol monophosphatase 1
- Inositol polyphosphate 1-phosphatase
- Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol oxygenase
- Inositol polyphosphate-4-phosphatase type I A
- Inositol polyphosphate 4-phosphatase type II
- Myotubularin
- Transcription termination factor 2
Sequence:
MKPSGEDQAALAAGPWEECFQAAVQLALRAGQIIRKALTEEKRVSTKTSAADLVTETDHLVEDLIISELRERFPSHRFIAEEAAASGAKCVLTHSPTWIIDPIDGTCNFVHRFPTVAVSIGFAVRQELEFGVIYHCTEERLYTGRRGRGAFCNGQRLRVSGETDLSKALVLTEIGPKRDPATLKLFLSNMERLLHAKAHGVRVIGSSTLALCHLASGAADAYYQFGLHCWDLAAATVIIREAGGIVIDTSGGPLDLMACRVVAASTREMAMLIAQALQTINYGRDDEK
Protein: Protein spire homolog 2 (Spir-2) (Q8WWL2)
Organism: Homo sapiens (Human)
Function: Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport (By similarity). Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis. Also acts in the nucleus: together with SPIRE1 and SPIRE2, promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8K1S6}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8K1S6}. Cell membrane {ECO:0000250|UniProtKB:Q8K1S6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8K1S6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8K1S6}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8K1S6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8K1S6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8K1S6}. Note=Detected at the cleavage furrow during asymmetric oocyte division and polar body extrusion. {ECO:0000250|UniProtKB:Q8K1S6}.
Interaction partners:
- Unconventional myosin-Va
- Formin-2
- Formin-1
Sequence:
MARAGSCGGAAAGAGRPEPWELSLEEVLKAYEQPLNEEQAWAVCFQGCRGLRGSPGRRLRDTGDLLLRGDGSVGAREPEAAEPATMVVPLASSEAQTVQSLGFAIYRALDWGLDESEERELSPQLERLIDLMANNDSEDSGCGAADEGYGGPEEEEEAEGVPRSVRTFAQAMRLCAARLTDPRGAQAHYQAVCRALFVETLELRAFLARVREAKEMLQKLREDEPHLETPRAELDSLGHTDWARLWVQLMRELRRGVKLKKVQEQEFNPLPTEFQLTPFEMLMQDIRARNYKLRKVMVDGDIPPRVKKDAHELILDFIRSRPPLKQVSERRLRPLPPKQRSLHEKILEEIKQERRLRPVRGEGWAARGFGSLPCILNACSGDAKSTSCINLSVTDAGGSAQRPRPRVLLKAPTLAEMEEMNTSEEEESPCGEVTLKRDRSFSEHDLAQLRSEVASGLQSATHPPGGTEPPRPRAGSAHVWRPGSRDQGTCPASVSDPSHPLLSNRGSSGDRPEASMTPDAKHLWLEFSHPVESLALTVEEVMDVRRVLVKAEMEKFLQNKELFSSLKKGKICCCCRAKFPLFSWPPSCLFCKRAVCTSCSIKMKMPSKKFGHIPVYTLGFESPQRVSAAKTAPIQRRDIFQSLQGPQWQSVEEAFPHIYSHGCVLKDVCSECTSFVADVVRSSRKSVDVLNTTPRRSRQTQSLYIPNTRTLDFK
Protein: Cathepsin B (EC 3.4.22.1) (APP secretase) (APPS) (Cathepsin B1) [Cleaved into: Cathepsin B light chain; Cathepsin B heavy chain] (P07858)
Organism: Homo sapiens (Human)
Function: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Cleaves matrix extracellular phosphoglycoprotein MEPE. Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis.
Subcellular location: Lysosome {ECO:0000269|PubMed:16733801}. Melanosome {ECO:0000269|PubMed:17081065}. Secreted, extracellular space {ECO:0000250|UniProtKB:A1E295}. Apical cell membrane {ECO:0000250|UniProtKB:P10605}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10605}; Extracellular side {ECO:0000250|UniProtKB:P10605}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells (By similarity). {ECO:0000250|UniProtKB:P10605, ECO:0000269|PubMed:17081065}.
Interaction partners:
- Cystatin-A
- NACHT, LRR and PYD domains-containing protein 3
- Cystatin-C
- Annexin A2
- Cathepsin D
- Procathepsin L
- Cathepsin S
- HLA class II histocompatibility antigen gamma chain
- Cystatin-B
- Apoptosis regulator Bcl-2
Sequence:
MWQLWASLCCLLVLANARSRPSFHPLSDELVNYVNKRNTTWQAGHNFYNVDMSYLKRLCGTFLGGPKPPQRVMFTEDLKLPASFDAREQWPQCPTIKEIRDQGSCGSCWAFGAVEAISDRICIHTNAHVSVEVSAEDLLTCCGSMCGDGCNGGYPAEAWNFWTRKGLVSGGLYESHVGCRPYSIPPCEHHVNGSRPPCTGEGDTPKCSKICEPGYSPTYKQDKHYGYNSYSVSNSEKDIMAEIYKNGPVEGAFSVYSDFLLYKSGVYQHVTGEMMGGHAIRILGWGVENGTPYWLVANSWNTDWGDNGFFKILRGQDHCGIESEVVAGIPRTDQYWEKI
Protein: Haloalkane dehalogenase 3 (EC 3.8.1.5) (P9WMR9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons.
Interaction partners:
- Haloalkane dehalogenase 2
- Haloalkane dehalogenase 1
- Alcohol dehydrogenase B
- Probable zinc-type alcohol dehydrogenase
- Probable alcohol dehydrogenase adh
- Probable alcohol dehydrogenase AdhA
- Uncharacterized oxidoreductase Rv0770
Sequence:
MTAFGVEPYGQPKYLEIAGKRMAYIDEGKGDAIVFQHGNPTSSYLWRNIMPHLEGLGRLVACDLIGMGASDKLSPSGPDRYSYGEQRDFLFALWDALDLGDHVVLVLHDWGSALGFDWANQHRDRVQGIAFMEAIVTPMTWADWPPAVRGVFQGFRSPQGEPMALEHNIFVERVLPGAILRQLSDEEMNHYRRPFVNGGEDRRPTLSWPRNLPIDGEPAEVVALVNEYRSWLEETDMPKLFINAEPGAIITGRIRDYVRSWPNQTEITVPGVHFVQEDSPEEIGAAIAQFVRRLRSAAGV
Protein: HAT transposon superfamily (Transposase-like protein) (Q9LIE1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Retrotransposon ORF-1 protein
- Retrotransposon ORF-1 protein
- Retrotransposon ORF-1 protein
- Zinc finger BED domain-containing protein DAYSLEEPER
- TOM1-like protein 2
- TOM1-like protein 1
Sequence:
MDSDLEPVALTPQKQDSAWKHCEVYKYGDRVQMRCLYCRKMFKGGGITRVKEHLAGKKGQGTICDQVPDEVRLFLQQCIDGTVRRQRKRRKSSPEPLPIAYFPPCEVETQVAASSDVNNGFKSPSSDVVVGQSTGRTKQRTYRSRKNNAFERNDLANVEVDRDMDNLIPVAISSVKNIVHPTSKEREKTVHMAMGRFLFDIGADFDAANSVNVQPFIDAIVSGGFGVSIPTHEDLRGWILKSCVEEVKKEIDECKTLWKRTGCSVLVQELNSNEGPLILKFLVYCPEKVVFLKSVDASEILDSEDKLYELLKEVVEEIGDTNVVQVITKCEDHYAAAGKKLMDVYPSLYWVPCAAHCIDKMLEEFGKMDWIREIIEQARTVTRIIYNHSGVLNLMRKFTFGNDIVQPVCTSSATNFTTMGRIADLKPYLQAMVTSSEWNDCSYSKEAGGLAMTETINDEDFWKALTLANHITAPILRVLRIVCSERKPAMGYVYAAMYRAKEAIKTNLAHREEYIVYWKIIDRWWLQQPLYAAGFYLNPKFFYSIDEEMRSEIHLAVVDCIEKLVPDVNIQDIVIKDINSYKNAVGIFGRNLAIRARDTMLPAEWWSTYGESCLNLSRFAIRILSQTCSSSIGSVRNLTSISQIYESKNSIERQRLNDLVFVQYNMRLRRIGSESSGDDTVDPLSHSNMEVLEDWVSRNQVCIEGNGSSDWKSLEFIKRSEEVAVVIDETEDLGSGFDDAEIFKGEKEASYEGGYSENLFT
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Q8MXS0)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
Sequence:
MPEYGASLEELRALMEYRSAEAKEKIETDYGGTTGLCERLKTDPNNGLPNNEEELERRRNVFGANEIPPHPPKCFLQLVWEALQDVTLVILLVSAIVSLALSFYRPPGEDTAGSDDSEHDAGWIEGVAILISVIVVVLVTALNDYTKERQFRGLQAKIETEHRFFVLRGGQSVQVVVNELVVGDIAQIKYGDLIPSDGIIIQSNDLKMDESSLTGESDQIRKSPEHDPIILSGTHVMEGSGKMLVTAVGVNSQTGIIMTLLGAAKTVAEEERKTAKREGGDGASGAEEGTAQALLDSKGDEAMANGKAVAAAESDGKKERSVLQAKLTRLAIQIGYAGSFVAGCTVLILIIRFCISRYAIDGKSFSLADFQHFINFLIIGVTVLVVAVPEGLPLAVTLSLAYSVKKMMLDNNLVRHLDACETMGNATAICSDKTGTLTTNRMTVVQSFVNDVHYKDTPKIESLDQNTAKLMMDCISINSSYSSQVIPPKQLGEQATQLGNKTECGMLGFVLALGKSYQEIRDRHPEETIPKVYTFNSVRKSMSTVINLPDGGYRVFSKGASEIVTKRCKYFLGKNGTLTKFSSKDAENLVRDVIEPMASDGLRTICVAYKDYVPSSKKTADNQIAYSSEPDWENEEMIVGDMTAIAVLGIQDPVRPEVPAAITRCQEAGITVRMVTGDNINTARSIATACGILKPGEDFIALEGKEFNARIRDENGEVSQEKLDLIWPKLRVLARAQPSDKYVLVKGIIDSRVTDSREVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSIAKFLQFQLTVNVVAVVVAFVGACAIQDTPLKAVQMLWVNLIMDTLASLALATEMPTEELLKRKPYGRTSPLISRTMCKNILGHAVYQLVILFTLIFYGEVCFNIPSGRWAPLHSPPSKHFTIVFNTFVMMTLFNEINARKIHGERNIFKGLFSNPIYYVIWIATMISQVVIIQFGGRWFSTSALNTTEWLWCLAFGVGTLLWGQIVTSIPTGSLPANMTIGSGEAPTNDPLMPDYEDSDTHEKRSGQILWVRGLTRLQTQIRVVKAFQAGLDRREPSLTGQSAARLREISRQLRLQVDSENRSRSTSRGNIKETNNL
Protein: Growth hormone (Q0QBG9)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MMAAGPRTSLLLAFTLLCLLWTQVVGAXPAMSLSRLFANAVLRAQHXHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTSKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDVTPRAGQILKQTYDKFDTNMRSDDALLKNYXLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: Tenascin-R (TN-R) (Janusin) (Restrictin) (Q92752)
Organism: Homo sapiens (Human)
Function: Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. These interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediate inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Aggrecan core protein
- Integrin alpha-9
- Integrin alpha-8
- Integrin alpha-V
- Integrin beta-3
- Integrin beta-6
- Integrin beta-1
- Syndecan-4
- Syndecan-1
- Neurocan core protein
Sequence:
MGADGETVVLKNMLIGINLILLGSMIKPSECQLEVTTERVQRQSVEEEGGIANYNTSSKEQPVVFNHVYNINVPLDNLCSSGLEASAEQEVSAEDETLAEYMGQTSDHESQVTFTHRINFPKKACPCASSAQVLQELLSRIEMLEREVSVLRDQCNANCCQESAATGQLDYIPHCSGHGNFSFESCGCICNEGWFGKNCSEPYCPLGCSSRGVCVDGQCICDSEYSGDDCSELRCPTDCSSRGLCVDGECVCEEPYTGEDCRELRCPGDCSGKGRCANGTCLCEEGYVGEDCGQRQCLNACSGRGQCEEGLCVCEEGYQGPDCSAVAPPEDLRVAGISDRSIELEWDGPMAVTEYVISYQPTALGGLQLQQRVPGDWSGVTITELEPGLTYNISVYAVISNILSLPITAKVATHLSTPQGLQFKTITETTVEVQWEPFSFSFDGWEISFIPKNNEGGVIAQVPSDVTSFNQTGLKPGEEYIVNVVALKEQARSPPTSASVSTVIDGPTQILVRDVSDTVAFVEWIPPRAKVDFILLKYGLVGGEGGRTTFRLQPPLSQYSVQALRPGSRYEVSVSAVRGTNESDSATTQFTTEIDAPKNLRVGSRTATSLDLEWDNSEAEVQEYKVVYSTLAGEQYHEVLVPRGIGPTTRATLTDLVPGTEYGVGISAVMNSQQSVPATMNARTELDSPRDLMVTASSETSISLIWTKASGPIDHYRITFTPSSGIASEVTVPKDRTSYTLTDLEPGAEYIISVTAERGRQQSLESTVDAFTGFRPISHLHFSHVTSSSVNITWSDPSPPADRLILNYSPRDEEEEMMEVSLDATKRHAVLMGLQPATEYIVNLVAVHGTVTSEPIVGSITTGIDPPKDITISNVTKDSVMVSWSPPVASFDYYRVSYRPTQVGRLDSSVVPNTVTEFTITRLNPATEYEISLNSVRGREESERICTLVHTAMDNPVDLIATNITPTEALLQWKAPVGEVENYVIVLTHFAVAGETILVDGVSEEFRLVDLLPSTHYTATMYATNGPLTSGTISTNFSTLLDPPANLTASEVTRQSALISWQPPRAEIENYVLTYKSTDGSRKELIVDAEDTWIRLEGLLENTDYTVLLQAAQDTTWSSITSTAFTTGGRVFPHPQDCAQHLMNGDTLSGVYPIFLNGELSQKLQVYCDMTTDGGGWIVFQRRQNGQTDFFRKWADYRVGFGNVEDEFWLGLDNIHRITSQGRYELRVDMRDGQEAAFASYDRFSVEDSRNLYKLRIGSYNGTAGDSLSYHQGRPFSTEDRDNDVAVTNCAMSYKGAWWYKNCHRTNLNGKYGESRHSQGINWYHWKGHEFSIPFVEMKMRPYNHRLMAGRKRQSLQF
Protein: Integration host factor subunit alpha (IHF-alpha) (P0A6X7)
Organism: Escherichia coli (strain K12)
Function: One of the 2 subunits of integration host factor (IHF), a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. Binds to hundreds of transcriptionally inactive, AT-rich DNA sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome.
Subcellular location: Cytoplasm, nucleoid {ECO:0000269|PubMed:21903814}. Note=Scattered throughout the nucleoid (PubMed:21903814). {ECO:0000269|PubMed:21903814}.
Interaction partners:
- Integration host factor subunit beta
- CRISPR-associated endonuclease Cas1
- RNA-binding protein Hfq
- DNA-binding protein HU-beta
- Phenylalanine--tRNA ligase beta subunit
- DNA-binding protein Fis
- DNA-binding protein HU-alpha
- CRISPR-associated endoribonuclease Cas2
- Carbon storage regulator
- Phenylalanine--tRNA ligase alpha subunit
Sequence:
MALTKAEMSEYLFDKLGLSKRDAKELVELFFEEIRRALENGEQVKLSGFGNFDLRDKNQRPGRNPKTGEDIPITARRVVTFRPGQKLKSRVENASPKDE
Protein: Protein GOLM2 (Golgi membrane protein 2) (H0YMR0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MADIHHLKEQLAELRQEFLRQEDQLQDYRKNNTYLVKRLEYESFQCGQQMKELRAQHEENIKKLADQFLEEQKQETQKIQSNDGKELDINNQVVPKNIPKVAENVADKNEEP
Protein: Major facilitator superfamily multidrug transporter FLU1 (Fluconazole resistance protein 1) (G1UB37)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Major facilitator superfamily transporter that mediates resistance to structurally and functionally unrelated compounds including cycloheximide but also azoles such as fuconazole, ketoconazole and itraconazole. Mediates also efflux of histatin 5, a salivary human antimicrobial peptide, and is responsible for reduction of its toxicity in C.albicans.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pleiotropic ABC efflux transporter of multiple drugs CDR1
- Multidrug resistance protein CDR2
- Lanosterol 14-alpha demethylase
Sequence:
MNNNTNSNHNDIAPEATITQNTTTSVSNDELQHITNNNNVNVQSYVGPTDSVESSSNTADEENEINSFNAQNVKDYEANVGGELPPDDELSRIESNTELSRRATRSIMNTESLLRTASQSSKPLPPMGGGKEYPPMLGSRDPYVVAFDGPDDPDHPHNYPTWKKILYCASVGLAALSVSMGSAMFSQASADIMQIYHIGWTPATLTTSLFVFGFASGPVIYGPLSELFGRKLVMVPSCLGYVCFSFAVATAKDIQTIMICRFFAGFIGAAPLVVAPAVMADMFNNRYRGTAIAIFSMLLFGGPMLAPILGAFTVKNSALGWRWTSYFCGIIGSLALFMNTFLLQETHHPLILTRRAEELRRRTGNWGIYAPHEELKLSMKEIVENNIARPLKMLFTEPILFLVSLYNAFIYGMLYLFLTAIPLIFLGEYHFVQGVAELPYLAMLIGILIGGGMIMLFEKRYIKAMEDNGGKIIPEKRLEPMMVGGFTFVIGIFWLGWTGNYPQHVHWIVPVIGAAFVGNGLMLIFLPCFNYIIDCYLLYAATALAGNTFIRSAFGAVFPLFARQMFTNLTIKWASTLLGCIGILLLPMPFVFYYYGKSLRHKSKFAFVLE