wanglab/gogpt-training-data huggingface dataset:
Protein: Spastin (A0A2R8YGN6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKMQPVLPFSKSQTDVYNDSTNLACRNGHLQSESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPEVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
Protein: Histone H4 transcription factor (Histone nuclear factor P) (HiNF-P) (MBD2-interacting zinc finger protein) (Methyl-CpG-binding protein 2-interacting zinc finger protein) (Q9BQA5)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor that binds to the consensus sequence 5'-CGGACGTT-3' and to the RB1 promoter. Transcriptional activator that promotes histone H4 gene transcription at the G1/S phase transition in conjunction with NPAT. Also activates transcription of the ATM and PRKDC genes. Autoregulates its expression by associating with its own promoter.
Subcellular location: Nucleus {ECO:0000269|PubMed:11553631, ECO:0000269|PubMed:14585971, ECO:0000269|PubMed:15988025, ECO:0000269|PubMed:18850719}. Note=Associated with discrete nuclear foci.
Interaction partners:
- Homeobox protein goosecoid
- Protein NPAT
- Homeobox protein HMX3
- Transcription initiation factor TFIID subunit 8
- Leucine-rich repeat-containing protein 57
- Zinc finger protein 766
Sequence:
MPPPGKVPRKENLWLQCEWGSCSFVCSTMEKFFEHVTQHLQQHLHGSGEEEEEEEEDDPLEEEFSCLWQECGFCSLDSSADLIRHVYFHCYHTKLKQWGLQALQSQADLGPCILDFQSRNVIPDIPDHFLCLWEHCENSFDNPEWFYRHVEAHSLCCEYEAVGKDNPVVLCGWKGCTCTFKDRSKLREHLRSHTQEKVVACPTCGGMFANNTKFLDHIRRQTSLDQQHFQCSHCSKRFATERLLRDHMRNHVNHYKCPLCDMTCPLPSSLRNHMRFRHSEDRPFKCDCCDYSCKNLIDLQKHLDTHSEEPAYRCDFENCTFSARSLCSIKSHYRKVHEGDSEPRYKCHVCDKCFTRGNNLTVHLRKKHQFKWPSGHPRFRYKEHEDGYMRLQLVRYESVELTQQLLRQPQEGSGLGTSLNESSLQGIILETVPGEPGRKEEEEEGKGSEGTALSASQDNPSSVIHVVNQTNAQGQQEIVYYVLSEAPGEPPPAPEPPSGGIMEKLQGIAEEPEIQMV
Protein: Developmental pluripotency-associated protein 3 (Compaction-associated protein 1) (Primordial germ cell protein 7) (Stella) (Q8QZY3)
Organism: Mus musculus (Mouse)
Function: Primordial germ cell (PGCs)-specific protein involved in epigenetic chromatin reprogramming in the zygote following fertilization. In zygotes, DNA demethylation occurs selectively in the paternal pronucleus before the first cell division, while the adjacent maternal pronucleus and certain paternally-imprinted loci are protected from this process. Participates in protection of DNA methylation in the maternal pronucleus by preventing conversion of 5mC to 5hmC: specifically recognizes and binds histone H3 dimethylated at 'Lys-9' (H3K9me2) on maternal genome, and protects maternal genome from TET3-mediated conversion to 5hmC and subsequent DNA demethylation. Does not bind paternal chromatin, which is mainly packed into protamine and does not contain much H3K9me2 mark. Also protects imprinted loci that are marked with H3K9me2 in mature sperm from DNA demethylation in early embryogenesis. May be important for the totipotent/pluripotent states continuing through preimplantation development. Also involved in chromatin condensation in oocytogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:11900980, ECO:0000269|PubMed:12124616, ECO:0000269|PubMed:17143267, ECO:0000269|PubMed:22722204}. Cytoplasm {ECO:0000269|PubMed:11900980, ECO:0000269|PubMed:12124616, ECO:0000269|PubMed:17143267}. Note=Localized in the cytoplasm at the primary oocyte stage and in oocytes within mono-laminar follicles. Expressed in the nucleus and cytoplasm of oocytes in bi-laminar and Graafian follicles and during the 2-cell and morula stages. In 3.5 dpc blastocysts localization is mainly nuclear. Mainly localizes in the female pronucleus, localization to the male pronucleus in much weaker. {ECO:0000269|PubMed:22722204}.
Interaction partners:
- Developmental pluripotency-associated protein 5A
- POU domain, class 5, transcription factor 1
- Growth/differentiation factor 3
- Undifferentiated embryonic cell transcription factor 1
- Zinc finger protein 57
- E3 ubiquitin-protein ligase UHRF1
- PR domain zinc finger protein 14
- Transcription factor CP2-like protein 1
- Homeobox protein NANOG
- Zinc finger protein 42
Sequence:
MEEPSEKVDPMKDPETPQKKDEEDALDDTDVLQPETLVKVMKKLTLNPGVKRSARRRSLRNRIAAVPVENKSEKIRREVQSAFPKRRVRTLLSVLKDPIAKMRRLVRIEQRQKRLEGNEFERDSEPFRCLCTFCHYQRWDPSENAKIGKN
Protein: Serine/threonine-protein kinase (EC 2.7.11.1) (D3ZMG0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Autophagy related 13
- RB1-inducible coiled-coil protein 1
- Autophagy-related protein 101
- Beclin 1-associated autophagy-related key regulator
- Serine/threonine-protein kinase mTOR
- Beclin-1
- Autophagy related 2A
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Regulatory-associated protein of mTOR
- Activating molecule in BECN1-regulated autophagy protein 1
Sequence:
MEPGRGGVETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHTMRTLSEDTVRLFLQQIAGAMQLLHSKGIIHRDLKPQNILLSNPGGRRANPSNIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPAIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASTPIKKSPPVPVPSYPSSGSGSSSSSSSASHLASPPSLGEMPQLQKTLTSPADAAGFLQGSRDSGGSSKDSCDTDDFVMVPAQFPGDLVPEAASAKPPPDSLLCSGSSLVASAGLESHGRTPSPSPTCSSSPSPSGRPGPFSSNRYGASVPIPVPTQVHNYQRIEQNLQSPTQQQTARSSAIRRSGSTSPLGFGRASPSPPSHTDGAMLARKLSLGGGRPYTPSPQATLFLPVGTIPERPSWSRVPSPQGADVRAGRSPRPGSSVPEHSPRTTGLGCRLHSAPNLSDFHVVRPKLPKPPTDPLGATFSPPQTSAPQPCPGLQSCRPLRGSPKLPDFLQRSPLPPILGSPTKAGPSFDFPKAPSSQSLLTLLARQGVVMTPPRNRTLPDLSEAGPFQGQQLGSGLRPAEDTRGPFGRSFSTSRLTDLLLKAAFGTQASDSGSTDSLQEKPMEIAPSAGFGGTLHPGARAGGASSPAPVVFTVGSPPSGTTPPQSTRTRMFSVGSSSSLGSTGSSSARHLVPGACAEAPELSAPGYCCSLADPLAANLEGAVTFEAPDLPEETLMEQEHTETLHSLRFTLAFAQQVLEIAALKGSASEAAGGPEYQLQESVVADQISQLSREWGFAEQLVLYLKVAELLSSGLQTAIDQIRAGKLCLSSTVKQVVRRLNELYKASVVSCQGLSLRLQRFFLDKQRLLDGIHGVTAERLILSHAVQMVQSAALDEMFQHRESCVPRYHKALLLLEGLQHTLTDQADIENIAKCKLCIERRLSALLSGVYA
Protein: Farnesyl pyrophosphate synthase (FPP synthase) (FPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Cholesterol-regulated 39 kDa protein) (CR 39) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Geranyltranstransferase) (P05369)
Organism: Rattus norvegicus (Rat)
Function: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Squalene synthase
- Diphosphomevalonate decarboxylase
- Geranylgeranyl pyrophosphate synthase
- Squalene monooxygenase
- Lanosterol synthase
- Lanosterol 14-alpha demethylase
- Isopentenyl-diphosphate Delta-isomerase 1
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Methylsterol monooxygenase 1
Sequence:
MNGDQKLDVHNQEKQNFIQHFSQIVKVLTEDELGHPEKGDAITRIKEVLEYNTVGGKYNRGLTVVQTFQELVEPRKQDAESLQRALTVGWCVELLQAFFLVLDDIMDSSYTRRGQICWYQKPGIGLDAINDALLLEAAIYRLLKFYCREQPYYLNLLELFLQSSYQTEIGQTLDLITAPQGQVDLGRYTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANALKILLEMGEFFQIQDDYLDLFGDPSVTGKVGTDIQDNKCSWLVVQCLLRATPQQRQILEENYGQKDPEKVARVKALYEELDLRSVFFKYEEDSYNRLKSLIEQCSAPLPPSIFLELANKIYKRRK
Protein: C-terminal-binding protein (CtBP protein) (dCtBP) (O46036)
Organism: Drosophila melanogaster (Fruit fly)
Function: Corepressor targeting diverse transcription regulators. Hairy-interacting protein required for embryonic segmentation and hairy-mediated transcriptional repression.
Subcellular location: Nucleus.
Interaction partners:
- Histone deacetylase HDAC1
- Protein groucho
- Protein hairless
- Suppressor of hairless protein
- Chromatin-remodeling complex ATPase chain Iswi
- Protein pangolin, isoform J
- Protein snail
- Phosphoserine aminotransferase
- CoRest, isoform G
- ATP-dependent chromatin assembly factor large subunit
Sequence:
MDKNLMMPKRSRIDVKGNFANGPLQARPLVALLDGRDCSIEMPILKDVATVAFCDAQSTSEIHEKVLNEAVGALMWHTIILTKEDLEKFKALRIIVRIGSGTDNIDVKAAGELGIAVCNVPGYGVEEVADTTMCLILNLYRRTYWLANMVREGKKFTGPEQVREAAHGCARIRGDTLGLVGLGRIGSAVALRAKAFGFNVIFYDPYLPDGIDKSLGLTRVYTLQDLLFQSDCVSLHCTLNEHNHHLINEFTIKQMRPGAFLVNTARGGLVDDETLALALKQGRIRAAALDVHENEPYNVFQGALKDAPNLICTPHAAFFSDASATELREMAATEIRRAIVGNIPDVLRNCVNKEYFMRTPPAAAAGGVAAAVYPEGALHHRAHSTTPHDGPHSTTNLGSTVGGGPTTVAQAAAAAVAAAAAAALLPSPVPSHLSPQVGGLPLGIVSSQSPLSAPDPNNHLSSSIKTEVKAESTEAP
Protein: Cation channel sperm-associated auxiliary subunit TMEM249 (Transmembrane protein 249) (A0A2R8VHF7)
Organism: Mus musculus (Mouse)
Function: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:34225353}; Multi-pass membrane protein {ECO:0000269|PubMed:34225353}. Note=Predominantly located in the principal piece of the sperm tail. {ECO:0000269|PubMed:34225353}.
Interaction partners:
- Cation channel sperm-associated protein 4
- Cation channel sperm-associated auxiliary subunit TMEM262
- Cation channel sperm-associated auxiliary subunit epsilon
- Cation channel sperm-associated auxiliary subunit beta
- EF-hand calcium-binding domain-containing protein 9
- Cation channel sperm-associated auxiliary subunit zeta
- Cation channel sperm-associated auxiliary subunit gamma 2
- Solute carrier organic anion transporter family member 6C1
- Cation channel sperm-associated protein 2
- Cation channel sperm-associated auxiliary subunit delta
Sequence:
MLFIICLVFISCNVLREVKYQETWCFPAYGMVIGLWLMLSSIPQRRLVLNHTRGMYHFSIQGRTVCQGPMHLVYVRLALSSDAYGGRFFQLVLCGHKLEPLVLVQLSERYEQMEFLGRHLARKLNINYFDYLASSYRHVVRHWPLGASFSPGIVQRKTQVYTKSSVNDLDV
Protein: AMP-dependent synthetase/ligase domain-containing protein (Q54NV9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Nuclear pore protein
- Uncharacterized protein
- Malonyl-CoA:ACP transacylase
- Malonyl-CoA:ACP transacylase
- Malonyl-CoA:ACP transacylase
- 50S ribosomal protein L13
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL11m
- Small ribosomal subunit protein uS17m
- Ribosomal protein L15
Sequence:
MLSKSNNIRKVFARGFTTYVQPGKFNAETNETIGNRISNVCEKFSYNDAISIPDHENYTLTYNDVLQNTRGLAGGFIEHSIKDDQTIVSNSFGVDSTMTHIAASFAGLNYVSIPPTSTFSEIGTHLNNQKASSFVMADSNQRVMVDEALEFFPNLKTIYNDEYHRDNRFPELKHIFSTGASQQPGISLLRDIILDTKTSPNKNVTNTQISATYPVADGKYVSFTQKSLLNTADALAEFFNIKTAQRFSFAAPLFEGNATAFNLACLSKGALIALISQINPANILNSIIKDKCDNLFISSSVLNTLVSSPEFARVENFELKKLIVVGEIDNSVVKQFESKCKGVESSIIPFVHAGQISGVVFNSSGVGKLLPNVEAKIVDSNGKELDFDNKGSLMTKGFHVGSNPAHWLKTNIKASMSKDGTIKL
Protein: aspartyl aminopeptidase (EC 3.4.11.21) (C8VJ09)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MTSNLTKNLKQPALDFLSFVNASPTPFHAVNSARNLLANAGFQEIKEKDSWASTCRPGGKYYLTRNQSTIVAFAVGKKWKPGNAIAMIGAHTDSPVLRIKPVSNKRGEGYIQVGVETYGGGIWHTWFDRDLGVAGRAMVRTDDGSIVQKLIKIDRPILRIPTLAIHLERQETFSFNKETQLFPIAGMIAAELNRTGQAEGASDKSNTAAESENAEFSPLKAITERHHPHIVELIAAEAGVEPADVLDFEMILFDTQKSCLGGLMEEFIFSPRLDNLNSSFCATAGLIESVADESALDDESTIRLIALFDHEEIGSRTAQGADSNVLPGIIRRLSVLPSTAGDVDTSTAYEQTLSTSFLLSADMAHAVHPNWSAKYENDHRPEINKGPVIKINANARYATNSPGIVLLQEVARKAVETEGEGVPLQLFVVRNDSSCGSTIGPMLSAALGARTLDLGNPQLSMHSIRETGGTYDVAHSIRLFKSFFQHYASTSQSIFVD
Protein: Probable ATP-binding component of ABC dipeptide transporter (Q9HVR5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable binding protein component of ABC transporter
- Probable permease of ABC transporter
- Probable permease of ABC transporter
- ABC-type dipeptide transporter
- Dipeptide-binding protein
- Probable binding protein component of ABC transporter
- Glycine-glutamate dipeptide porin OpdP
- Tripeptide-binding protein
- Probable binding protein component of ABC dipeptide transporter
- Probable ATP-binding/permease fusion ABC transporter
Sequence:
METVLTARDLTRHYEVSRGLFKGHAQVRALNGVSFELEAGKTLAVVGESGCGKSTLARALTLIEEPTSGSLKIAGQEVKGASKDQRRQLRRDVQMVFQNPYASLNPRQKIGDQLAEPLLINTALSREERREKVQQMMRQVGLRPEHYQRYPHMFSGGQRQRIALARAMMLQPKVLVADEPTSALDVSIQAQVLNLFMDLQQQFRTAYVFISHNLAVVRHVADDVLVMYLGRPAEMGPADKLYENPLHPYTRALLSATPAIHPDPTKPKIRIQGELPNPLNPPEGCAFHKRCPYATERCRSEVPELRLLDQRQVACHHAEQFLG
Protein: AB hydrolase-1 domain-containing protein (Q54T91)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MENIKTIKEYIEIGKDRSGNNSPIFKLYYESYGEIEAPIKIIFIAGFMSSGKNDYYKQVEYFMKQELVNKCYQIVIFDNRGSGNSGTPNKFSTFDMALDMIELMDHLGWDSAHVIGASMGGMIALELATVIPPQRIRSLTLAVTHAGHTITPIKGTKAVTKSIFTSDPIKKSQITIDSLYSKEYLSKLSIEDPSRSNKDVLTDIFVDRLKTSKKPSLNAIMGHFKSVLTHYISETKLKYISNQEFPIQIITGTNDHLVDPKNSFYLKSKLNPCEFTVFQGCGHAVNTERLNDFNNLIQSHINRFIPDHNILNQYLKK
Protein: Ral GTPase-activating protein subunit beta (p170) (Q86X10)
Organism: Homo sapiens (Human)
Function: Non-catalytic subunit of the heterodimeric RalGAP1 and RalGAP2 complexes which act as GTPase activators for the Ras-like small GTPases RALA and RALB.
Interaction partners:
- Ral GTPase-activating protein subunit alpha-2
- Ras-related protein Ral-A
- Ral GTPase-activating protein subunit alpha-1
- RAC-beta serine/threonine-protein kinase
- E3 ubiquitin-protein ligase Arkadia
- Disco-interacting protein 2 homolog B
- Transmembrane protein 131
Sequence:
MYSEWRSLHLVIQNDQGHTSVLHSYPESVGREVANAVVRPLGQVLGTPSVAGSENLLKTDKEVKWTMEVICYGLTLPLDGETVKYCVDVYTDWIMALVLPKDSIPLPVIKEPNQYVQTILKHLQNLFVPRQEQGSSQIRLCLQVLRAIQKLARESSLMARETWEVLLLFLLQINDILLAPPTVQGGIAENLAEKLIGVLFEVWLLACTRCFPTPPYWKTAKEMVANWRHHPAVVEQWSKVICALTSRLLRFTYGPSFPAFKVPDEDASLIPPEMDNECVAQTWFRFLHMLSNPVDLSNPAIISSTPKFQEQFLNVSGMPQELNQYPCLKHLPQIFFRAMRGISCLVDAFLGISRPRSDSAPPTPVNRLSMPQSAAVSTTPPHNRRHRAVTVNKATMKTSTVSTAHASKVQHQTSSTSPLSSPNQTSSEPRPLPAPRRPKVNSILNLFGSWLFDAAFVHCKLHNGINRDSSMTAITTQASMEFRRKGSQMSTDTMVSNPMFDASEFPDNYEAGRAEACGTLCRIFCSKKTGEEILPAYLSRFYMLLIQGLQINDYVCHPVLASVILNSPPLFCCDLKGIDVVVPYFISALETILPDRELSKFKSYVNPTELRRSSINILLSLLPLPHHFGTVKSEVVLEGKFSNDDSSSYDKPITFLSLKLRLVNILIGALQTETDPNNTQMILGAMLNIVQDSALLEAIGCQMEMGGGENNLKSHSRTNSGISSASGGSTEPTTPDSERPAQALLRDYALNTDSAAGLLIRSIHLVTQRLNSQWRQDMSISLAALELLSGLAKVKVMVDSGDRKRAISSVCTYIVYQCSRPAPLHSRDLHSMIVAAFQCLCVWLTEHPDMLDEKDCLKEVLEIVELGISGSKSKNNEQEVKYKGDKEPNPASMRVKDAAEATLTCIMQLLGAFPSPSGPASPCSLVNETTLIKYSRLPTINKHSFRYFVLDNSVILAMLEQPLGNEQNDFFPSVTVLVRGMSGRLAWAQQLCLLPRGAKANQKLFVPEPRPVPKNDVGFKYSVKHRPFPEEVDKIPFVKADLSIPDLHEIVTEELEERHEKLRSGMAQQIAYEIHLEQQSEEELQKRSFPDPVTDCKPPPPAQEFQTARLFLSHFGFLSLEALKEPANSRLPPHLIALDSTIPGFFDDIGYLDLLPCRPFDTVFIFYMKPGQKTNQEILKNVESSRTVQPHFLEFLLSLGWSVDVGRHPGWTGHVSTSWSINCCDDGEGSQQEVISSEDIGASIFNGQKKVLYYADALTEIAFVVPSPVESLTDSLESNISDQDSDSNMDLMPGILKQPSLTLELFPNHTDNLNSSQRLSPSSRMRKLPQGRPVPPLGPETRVSVVWVERYDDIENFPLSELMTEISTGVETTANSSTSLRSTTLEKEVPVIFIHPLNTGLFRIKIQGATGKFNMVIPLVDGMIVSRRALGFLVRQTVINICRRKRLESDSYSPPHVRRKQKITDIVNKYRNKQLEPEFYTSLFQEVGLKNCSS
Protein: Neuronal acetylcholine receptor subunit alpha-9 (Nicotinic acetylcholine receptor subunit alpha-9) (NACHR alpha-9) (Q9PTS8)
Organism: Gallus gallus (Chicken)
Function: Ionotropic receptor that may play a role in the modulation of auditory stimuli. Agonist binding induces a conformation change that leads to the opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:Q9UGM1}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9UGM1}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein.
- Acetylcholine receptor subunit alpha
- Uncharacterized protein
Sequence:
MKRNNLSSFYVSLWLLFTATMLQAVESAKGKYAQMLFNELFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQSWYDAYLKWDKDKYDGLDSIRIPSNLVWRPDIVLYNKADDDFSEPVNTNVVLRYDGKITWDAPAITKSSCVVDVSYFPFDSQQCNLTFGSWTYNGNQVDIINSLDSGDLSDFVEDVEWEIHGMPAVKNVITYGCCSEPYPDVTFTLILKRKSSFYIFNLLLPCILISFLAPLGFYLPADSGEKVSLGVTVLLALTVFQLMVAEIMPPSENVPLIGKYYIATMTMITASTALTIIIMNVHHCGSEAKPVPQWARVVILDYMSKIFFVYDVGENCTSPRREKEQEHRLEGGDMCRGGDGKSHLSSRNDDSDLKENLNGNWNKSFGVHGENVRENVNCCSCYKMLIKNIEYIANCVRDHKANRAKGIEWKKVAKVMDRFFMWIFFIMVFFMSVLIIGKAA
Protein: Keratin-associated protein 2-4 (High sulfur keratin-associated protein 2.4) (Keratin-associated protein 2.4) (Q9BYR9)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity).
Interaction partners:
Sequence:
MTGSCCGSTLSSLSYGGGCCQPCCCRDPCCCRPVTCQTTVCRPVTCVPRCTRPICEPCRRPVCCDPCSLQEGCCRPITCCPSSCTAVVCRPCCWATTCCQPVSVQSPCCRPPCGQPTPCSTTCRTSSC
Protein: GRB10 interacting GYF protein 2 (I1E4Y6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAETQTLNFGPEWLRALSSGGSITSPPLSPALPKYKLADYRYGREEMLALFLKDNKIPSDLLDKEFLPILQEEPLPPLALVPFTEEEQRNFSMSVNSAAVLRLTGRGGGGTVVGAPRGRSSSRGRGRGRGECGFYQRSFDEVEGVFGRGGGREMHRSQSWEERGDRRFEKPGRKDVGKKNGYYCMYSPVLLLGQPLCQGRPNFEEGGPTSVGRKHEFIRSESENWRIFREEQNGEDEDGGWRLAGSRRDGERWRPHSPDGPRSAGWREHMERRRRFEFDFRDRDDERGYRRVRSGSGSIDDDRDSLPEWCLEDAEEEMGTFDSSGAFLSLKKVQKEPIPEEQEMDFRPVDEGEECSDSEGSHNEEAKEPDKTNKKEGEKTDRVGVEASEETPQTSSSSARPGTPSDHQSQEASQFERKDEPKTEQTEKAEEETRMENSLPAKVPSRGDEMVADVQQPLSQIPSDTASPLLILPPPVPNPSPTLRPVETPVVGAPGMGSVSTEPDDEEGLKHLEQQAEKMVAYLQDSALDDERLASKLQEHRAKGVSIPLMHEAMQKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPLGDIMKMWGRVPFSPGPAPPPHMGELDQERLTRQQELTALYQMQHLQYQQFLIQQQYAQVLAQQQKAALSSQQQQQLALLLQQFQTLKMRISDQNIIPSVTRSVSVPDTGSIWELQPTASQPTVWEGGSVWDLPLDTTTPGPALEQLQQLEKAKAAKLEQERREAEMRAKREEEERKRQEELRRQQEEILRRQQEEERKRREEEELARRKQEEALRRQREQEIALRRQREEEERQQQEEALRRLEERRREEEERRKQEELLRKQEEEAAKWAREEEEAQRRLEENRLRMEEEAARLRHEEEERKRKELEVQRQKELMRQRQQQQEALRRLQQQQQQQQLAQMKLPSSSTWGQQSNTTACQSQATLSLAEIQKLEEERERQLREEQRRQQRELMKALQQQQQQQQQKLSGWGNVSKPSGTTKSLLEIQQEEARQMQKQQQQQQQHQQPNRARNNTHSNLHTSIGNSVWGSINTGPPNQWASDLVSSIWSNADTKNSNMGFWDDAVKEVGPRNSTNKNKNNASLSKSVGVSNRQNKKVEEEEKLLKLFQGVNKAQDGFTQWCEQMLHALNTANNLDVPTFVSFLKEVESPYEVHDYIRAYLGDTSEAKEFAKQFLERRAKQKANQQRQQQQLPQQQQQQPPQQPPQQPQQQDSVWGMNHSTLHSVFQTNQSNNQQSNFEAVQSGKKKKKQKMVRADPSLLGFSVNASSERLNMGEIETLDDY
Protein: Neuroligin 1 (Neuroligin-1 isoform X1) (D2X2F9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- Neurexin-3a.
- Neurexin-1a-beta
- Neurexin 2a
- Disks large homolog 4
- Neurexin 2.
- SH3 and multiple ankyrin repeat domains 2b
- Leucine-rich repeat transmembrane neuronal 1
- Leucine-rich repeat transmembrane neuronal 2
Sequence:
MPFQQPNRLSSIWKAMCPRLGLSASLDLPFLCWIVGLALHAQLAASEKLDETDPIVTTTYGKVRGFKKELNNEILGPVIQFLGVPYAAPPTGERRFQPPEPPISWSEIRNATQFAPVCPQTLLEGRLPDVMLPVWFTNSIEVVSSYVQDQSEDCLFLNIYVPTEDVKRISKECARKPGKKICRKGGPLSKKQNDDLADNDGAEDEDIRESGSPKPVMVFVHGGSYMEGTGNMFDGSILASYGNVIVITVNYRLGVLGFLSTGDQAAKGNYGLLDLIQALRWTSENIAFFGGDPLRITVFGSGAGASCVNLLTLSHYSEGNRWSNSTKGLFQRAIAQSGTALSSWAVSFQPAKYARMLAKKVGCNLKDTVEMVECLQKKHYKELVEQDIQPARYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGLKFVELIVDNENGVQANDFDYAVSSFVDDLYGYPEGKDILRETIKFMYTDWADRHNPETRRKTLLALFTDHQWVAPAVATADLHSSFGSPTYFYAFYHHCQTEQVPPWADAAHGDEIPYVFGLPMIGPTELFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVAWTRYNQKDQLYLHIGLKPRVKEHYRANKVNLWLELVPHLHSLNEVSQIISTTKLPPPEVTPRTPKKIPVNTKRPYPTPFPTETQDSHNQNQNQPFLVDQRDYSTELSVTIAVGASLLFLNILAFAALYYKKDKRRHEVHRRCSPQRTTANELPHTQEEEIMSLQMKHSDLERECREAMHPHEVVLRTACPPDYTLAMRRSPDDIPLMTPNTITMIPNSMPGLTSLHPFNSYSSGQNNTLPHPHPHSHSTTRV
Protein: HTH-type transcriptional regulator PtxS (Q88HH7)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Negatively regulates glucose metabolism by binding directly to the promoter region of the kgu and gad operons. It also negatively regulates its own synthesis.
Interaction partners:
- 2-ketogluconokinase
- Epimerase
- 2-ketogluconate transporter, putative
- phosphoenolpyruvate--protein phosphotransferase
- HTH-type transcriptional regulator HexR
- Gluconokinase
- Glutamate synthase large chain
- Mannose/glucose ABC transporter, permease protein
- Glucokinase
- Sodium/glutamate symporter
Sequence:
MTDAPAHTRERVTISEVARVAGVSKATVSRYIGGDRQLLAEATAKRLEEVIERLGYRPNQMARGLKRGQTRLIGMLVADILNPYSVAVMHGVETACRQHGYSLVVCNTNRDDEQERHHLVALQSYNVEGLIVNTLGHHPGELLNLQRDIPMVLVDRQLPELNVDLVGLDNADAVEQALDHLQAQGYRDILAVSEPLDGTSSRLERVQAFGASISRRPGMRQQVLEIGAGLQGQLASFLAHSGHGPQAIFTFNGVATLAVTRALLEAGRNLVADVGLIALDDLDWYPLVGKGITALAQPTERIGVAAFESLLGRLRGDSGAARRIDFKANLIIRGSTQPQ
Protein: Serine protease/ABC transporter B family protein tagC (EC 3.4.21.-) (Prestalk-specific protein tagC) (Q23868)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May be directly involved in maturation and export of SDF-2. The exposure of the protease domain of tagC on the surface of the prestalk cells were it can convert acbA to SDF-2 is induced by GABA. Intercellular communication via tagC may mediate integration of cellular differentiation with morphogenesis.
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- Acyl-CoA-binding protein
- Hybrid signal transduction histidine kinase A
Sequence:
MKFHFSSNKLLLISGLILLVLVIGIKLDIFLSSKSTEYIKFNNNNNHFKRDKRILLHNEIIDTNNKPSIKNNQIFINDNDNNENISPILLRILNNNNNNNNNNGDDKSIYKKNHYIVQFKDRINDETREQLKEFLIGTDIVLDEQPYQSHIVHYIPHDSFLVLMTQEQSVLLSSKEWVSWIGEFEPSNKIHLNYNEKSIGLPVYIILSDSTNSLIQRWENTLNSILKSYNSKVKLTLINQKKLKSIVYCNDESPSPSCSLINSEKLVYQWISEQSESNFIERSEKFQTANRLSPKVVFGTKDTLVNNDRVDIPLRGKGQILSIADTGLDGSHCFFSDSKYPIPLNSVNLNHRKVVTYITTSTSDDSDKVDGHGTHICGSAAGTPEDSSVNISSFSGLATDAKIAFFDLASGSSSLTPPSDLKQLYQPLYDAGARVHCDSWGSVSVEGYTGSYSSDTASIDDFLFTHPDFIILRAAGNNEQYLSLLTQSTAKNVITVGAHQTIHENYLTDGPNYINYQSSVDINQELICDFDSRYCNYTTAQCCLESNATTGLASCCPTLLRKSVIDAANTQPLLYNENNICSFSSKGPTHDGRMKPDLVAPGEYITSARSNGANTTDQCGDGSLPNTNALLAISGTSMATSFAAAATTILRQYLVDGYYPTGSIVESNKLQPTGSLLKALMINNAQLLNGTFQLITSSSITYPSNQVFENFAGASLVQGWGAIRMSNWLHVVNNNNSNNNNKTSDGITKFVGIGGLDLRLVKPNQWKEESLSTGQNTSYCFTYKPSSSSSNSGNNIPRVVATLVWTDPPSYAGAKFNLVNNLDLTMIYYRDNGSTIFYSNQGGSSFLGLAPTQDTLNNVEGIVHNPTEPMTYRFMVAGTNVPMGPQNFSFVFHGENGEFEWADKCPQCSPGQVLACPVENGIGTQLCTSDLQWSSCLIQSCDNNYNYNSIKKRCDKFLSYNYIIMIVAGGTMLLIIFILLLIKYQEYKESKKDSFRRFDDGTGIFVRPKDKDAKVSLADLYNLISPFIIELAISTACSLVSTAASILQPFYIGQIINDIPTAKHIGDFKSQFILIFILAVIEFVFSTISSWISGIVNEKMVMRLQNKVFRALIAQDMGFFQKNNAAILMNVLISDTPMLRSALTGILLSIATGLCKFVGSLVFIFTISWKLSLVFFATVPVLAFITQIQSQFTKRLTRALLFYNSKASQHGQESMVNMHVVTNYCRQDKEIIKYTDNLNNVFQTARRLIINNTLASSIKWLMVESLAFIILYYGAYLAIQKQFTVGLLISFCLYIGYVIDSTTTLFGVYVSYVQSQASATRVFMILRSAPRKRTTLEEEEADRNNGLGGGGGNNNNNDDDDDDDNYNGKGNDNGKGSDDPNNNNNNTTLENIDDNGELTTVQPVELTKKQLKKQKEKEQKEYFKRTGISVVEMSLIPSSYIELTDCKGEIEFKNVSFRYPTRPDVQVLHNINMKFETGKCYGLVGPSGSGKSTLLELISKFYPLRDGGNIIMDDIDIANIRPNNLRGFVTCVHQNPYLFDASIKDNIGYALDNPTIEEVIEAAKLAYAHEFIKDLPQQYDTVLGSAGSLLSGGQKKRIAIARAICAKRKIMLLDEITAELDPESEEAITQSIKVLTQGHTVVMVAHKVAAVRDCDKIFVLDKGYLVEEGTHDELMERKGKYHRMFNNEKDEEELLNNLGLPSNNETNNENNNENNNNNNNNNNNNNNNNDDNNNQVVGEQV