wanglab/gogpt-training-data huggingface dataset:
Protein: Paralemmin A kinase anchor protein (A2API9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MERISKPPSSTWPECASSPTHWRQKPPQLSEDANQLRSKQDNCGDSRLEPAASSLSPDHKNMEIGVSVAECKSVPGVTSTPHSKDHSSPFYSPSHNGLLADHHESLDNDVAREIQYLDEVLEANCCDSSVDGTYNGISSPEPGAAILVSSLGSPAHSVTEAEPTEKASGRQVPPHIELSRSPSDRM
Protein: Small ribosomal subunit protein eS17z (40S ribosomal protein S17-1) (P49205)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS26z
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS19z
- Small ribosomal subunit protein uS2z
- Small ribosomal subunit protein eS10z
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein eS8z
- Large ribosomal subunit protein eL42z/eL42y
Sequence:
MGRVRTKTVKKSSRQVIEKYYSRMTLDFHTNKKILEEVAIIPSKRLRNKIAGFSTHLMKRIQKGPVRGISLKLQEEERERRMDFVPDESAIKTDEIKVDKETLEMLASLGMSDTLGISAVDPQQAMAPIPAFGGGRAPRRY
Protein: Vesicle-associated membrane protein 713 (AtVAMP713) (Q9LFP1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q12255}. Prevacuolar compartment membrane {ECO:0000269|PubMed:15342965}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q12255}. Note=Strong colocalization with VAMP713 at the contact sites of two vacuoles. {ECO:0000269|PubMed:29463724}.
Interaction partners:
- Vacuolar protein-sorting-associated protein 33 homolog
- Protein VACUOLELESS1
- Vacuolar sorting protein 18
- Vacuolar protein-sorting-associated protein 11 homolog
- Vacuolar sorting protein 39
- Vacuolar protein sorting-associated protein 41 homolog
- Syntaxin-22
- Putative SNAP25 homologous protein SNAP30
- SNAP25 homologous protein SNAP29
- Syntaxin-23
Sequence:
MAIIFALVARGTVVLSEFSATSTNASSISKQILEKLPGNDSDSHMSYSQDRYIFHVKRTDGLTVLCMADETAGRNIPFAFLDDIHQRFVKTYGRAIHSAQAYSMNDEFSRVLSQQMEFYSNDPNADRMSRIKGEMSQVRNVMIENIDKVLDRGERLELLVDKTENMQGNTFRFRKQARRYRTIMWWRNVKLTIALILVLALVVYIAMAFVCHGPSLPSCFK
Protein: At2g28710 (C2H2-type zinc finger family protein) (Putative C2H2-type zinc finger protein) (Q9SI97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ac-like transposase
- HAT family dimerization domain-containing protein
Sequence:
MERGRSDMEMINNMANCLILLSKAHQNDTKSRVFACKTCNKEFPSFQALGGHRASHRRSAALEGHAPPSPKRVKPVKHECPICGAEFAVGQALGGHMRKHRGGSGGGGGRSLAPATAPVTMKKSGGGNGKRVLCLDLNLTPLENEDLKLELGRFIF
Protein: Large ribosomal subunit protein uL10 (60S acidic ribosomal protein P0) (F8VPE8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAFEQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKV
Protein: tRNA nucleotidyltransferase cca2 (EC 2.7.7.-) (A-adding enzyme cca2) (tRNA adenylyltransferase cca2) (Q9Y7U9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: tRNA nucleotidyltransferase involved in the synthesis of the tRNA CCA terminus. In contrast to what is usually observed in eukaryotes for which one enzyme synthesizes the whole tRNA CCA terminus, in S.pombe, cca1 specifically adds two cytidine residues to a tRNA substrate lacking this sequence while cca2 specifically adds the terminal adenosine residue thereby completing the CCA sequence.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable proteasome subunit alpha type-5
Sequence:
MYSRIVLNDVEKKVVNLLKKTADFIESKSSSSSSLEVRLAGGWVRDKLLGLSSDDLDVTLNKVTGVDFANSIFEYVHSLDSDSVIPYKDALGKLTVNPDQSKHLETATLSLFDLDIDFVGLRAESYDDKSRIPSVTPGTVETDALRRDFTVNTLFFNIRTEKIEDITKRGYKDLQTKVLVTPISPLQSFLEDPLRILRGIRFASRFEFTIDPSVVSAIQDPKVCKAFEKKVSKERVGEEIEKMLKGANAKLALQLLYSTNTYQFTFDTLPAEKEFQIPKALEATESLFQSLALTFPKLMKLSEDEKIGLWLYVALIPWSSQTVMVKKKQFYIPAIIAKDKLKLRSTYVNQLNQCCTFNPIFDELVNDTSTKNCSSIGSLIRQLNKSWEVVFLTSVIYSCCKTPAASVSNTFSSYKSLYDFIYDKNLQNAYNMKPLLDGKQIMKNVGVKPGPQLKETMDNMISWQFKHPEGSVEDCVAYLQSLKI
Protein: Phosphodiesterase (EC 3.1.4.-) (A0A8I6A416)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGSTDTDIEELENATYKYLIGEQTEKMWQRLKGILRCLVKQLEKGDVNVVDLKKNIEYAASVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRSIVHAVQAGIFVERMYRKNYHMVGLTYPAAVIVTLKEVDKWSFDVFALNEASGEHSLKFMIYELFTRYDLINRFKIPVSCLIAFAEALEVGYSKHKNPYHNLVHAADVTQTVHYIMLHTGIMHWLTELEILAMVFAAAVHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLMQEEEMNILVNLSKDDWRDLRNLVIEMVLATDMSGHFQQIKNIRSSLQQPEGIDRAKTMSLILHAADISHPAKTWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGFIDFIVEPTFSLLTDSTEKIVIPLIEEASKPESSNYGASSSSTMIGFHVADALRRSNTKGCMSDGTYAPDYSLSAVDLKSFKNNLVDIIQQNKERWKELAAQGELDLHKNSEDLEEKHADTHP
Protein: Alpha-1,2-mannosyltransferase ALG9 (EC 2.4.1.259) (EC 2.4.1.261) (Asparagine-linked glycosylation protein 9 homolog) (Disrupted in bipolar disorder protein 1) (Dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase) (Dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase) (Q9H6U8)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of mannose from Dol-P-Man to lipid-linked oligosaccharides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:15148656}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P53868}.
Interaction partners:
- Dol-P-Man:Man
- Dol-P-Man:Man
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Phosphomannomutase 2
Sequence:
MASRGARQRLKGSGASSGDTAPAADKLRELLGSREAGGAEHRTELSGNKAGQVWAPEGSTAFKCLLSARLCAALLSNISDCDETFNYWEPTHYLIYGEGFQTWEYSPAYAIRSYAYLLLHAWPAAFHARILQTNKILVFYFLRCLLAFVSCICELYFYKAVCKKFGLHVSRMMLAFLVLSTGMFCSSSAFLPSSFCMYTTLIAMTGWYMDKTSIAVLGVAAGAILGWPFSAALGLPIAFDLLVMKHRWKSFFHWSLMALILFLVPVVVIDSYYYGKLVIAPLNIVLYNVFTPHGPDLYGTEPWYFYLINGFLNFNVAFALALLVLPLTSLMEYLLQRFHVQNLGHPYWLTLAPMYIWFIIFFIQPHKEERFLFPVYPLICLCGAVALSALQKCYHFVFQRYRLEHYTVTSNWLALGTVFLFGLLSFSRSVALFRGYHGPLDLYPEFYRIATDPTIHTVPEGRPVNVCVGKEWYRFPSSFLLPDNWQLQFIPSEFRGQLPKPFAEGPLATRIVPTDMNDQNLEEPSRYIDISKCHYLVDLDTMRETPREPKYSSNKEEWISLAYRPFLDASRSSKLLRAFYVPFLSDQYTVYVNYTILKPRKAKQIRKKSGG
Protein: Formate dehydrogenase (FDH) (EC 1.17.1.9) (NAD-dependent formate dehydrogenase) (O13437)
Organism: Candida boidinii (Yeast)
Function: Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03210}.
Interaction partners:
Sequence:
MKIVLVLYDAGKHAADEEKLYGCTENKLGIANWLKDQGHELITTSDKEGETSELDKHIPDADIIITTPFHPAYITKERLDKAKNLKLVVVAGVGSDHIDLDYINQTGKKISVLEVTGSNVVSVAEHVVMTMLVLVRNFVPAHEQIINHDWEVAAIAKDAYDIEGKTIATIGAGRIGYRVLERLLPFNPKELLYYDYQALPKEAEEKVGARRVENIEELVAQADIVTVNAPLHAGTKGLINKELLSKFKKGAWLVNTARGAICVAEDVAAALESGQLRGYGGDVWFPQPAPKDHPWRDMRNKYGAGNAMTPHYSGTTLDAQTRYAEGTKNILESFFTGKFDYRPQDIILLNGEYVTKAYGKHDKK
Protein: Cytosolic 5'-nucleotidase 3A (EC 3.1.3.5) (7-methylguanosine phosphate-specific 5'-nucleotidase) (7-methylguanosine nucleotidase) (EC 3.1.3.91) (Cytosolic 5'-nucleotidase 3) (Cytosolic 5'-nucleotidase III) (cN-III) (Pyrimidine 5'-nucleotidase 1) (P5'N-1) (P5N-1) (PN-I) (Uridine 5'-monophosphate hydrolase 1) (p36) (Q9H0P0)
Organism: Homo sapiens (Human)
Function: Nucleotidase which shows specific activity towards cytidine monophosphate (CMP) and 7-methylguanosine monophosphate (m(7)GMP). CMP seems to be the preferred substrate.
Subcellular location: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum.
Interaction partners:
- 5'
- 5'
- Cytosolic purine 5'-nucleotidase
- Cytosolic 5'-nucleotidase 1A
- Deoxycytidine kinase
- Cytosolic 5'-nucleotidase 1B
- UMP-CMP kinase 2, mitochondrial
- Cytidine deaminase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Deoxycytidylate deaminase
Sequence:
MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSVRIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDECRKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVMLKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLKGFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYLNDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
Protein: Interleukin 17 isoform A (Interleukin 17A) (Q70I21)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Interleukin-17 receptor C/E N-terminal domain-containing protein
- SEFIR domain-containing protein
- Interleukin-17 receptor fibronectin-III-like domain-containing protein
- SEFIR domain-containing protein
- Interleukin-17 receptor D
- Interleukin-17 receptor D
- SEFIR domain-containing protein
- Interleukin 17a/f1
- protein disulfide-isomerase
- EGF-like domain-containing protein
Sequence:
MELKSNVSKYLVVCCVSMLLGLTMAKGMKVTKERCNETLIIPSDFYKIPTEESEGNGNIHTRSLSPWTWKSTTVENRIPQTMWEAECSSMYCVYPTNRSQYMRYRQNSVPIYQQVVVLYTSATRKCYSASFLSVAVGCTCAWARTT
Protein: Pre-mRNA processing factor 40 homolog A (H0YG38)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCSGSGRRRSSLSPTMRPGTGAERGGLMVSEMESHPPSQGPGDGERRLSGSSLCSGSWVSADGFLRRRPSMGHPGMHYAPMGMHPMGQRANMPPVPHGMMPQMMPPMGGPPMGQMPGMMSSVMPGMMMSHMSQASMQPALPPGVNSMDVAAGTASGAKSMWTEHKSPDGRTYYYNTETKQSTWEKPDDLKTPAEQLLSKCPWKEYKSDSGKPYYYNSQTKESRWAKPKELEDLEAMIKAEESSKQEECTTTSTAPVPTTEIPTTMSTMAAAEAAAAVVAAAAAAAAAAAAANANASTSASNTVSGTVPVVPEPEVTSIVATVVDNENTVTISTEEQAQLTSTPAIQDQSVEVSSNTGEETSKQETVA
Protein: Ankyrin repeat protein (Q385S7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
- C2H2-type domain-containing protein
- Uncharacterized protein
- Intraflagellar transport protein component, putative
- Intraflagellar transport protein 57/55
- IFT80/172/WDR35 TPR domain-containing protein
- Intraflagellar transport protein A1
- Intraflagellar transport protein 56 homolog
- BTB domain-containing protein
- Intraflagellar transport protein 22
Sequence:
MDNGKRIAEDVEVFLRAARAKDVLKCSEMLKQKPSLIDSVEAGGFSALHFAAFNGDLDMLYMLLEYKPTLSLKNYDGNTPLIMAAKVRQHEAIKVLVDAGADVNFRTPTGGTAAHFAASMGHVDTVRYLVGLGADVMHVDCETGSLLHWAAHSGDVDCLGAMIYEFRVPIDIKDSNGGSPLFTALFMKKVEAVEFLLEHGADPHTVVEGDLSTPLHIAVEHSNTECVKLLLSYGANPNSKNKSGDTPVAIAEREKKQSALKELLKLPVSEEKRKEEANRFKMQGNKVFEDGENVKAAKYYTLAIRMDNTNHVFFSNRAAAYFNQRHYSGAYWDSLRCITLAPQWAKGYFRKAATELAMKKRDEALRTCEEGLRLDPQNKDLLTIREETRRSK
Protein: ATP synthase assembly factor FMC1, mitochondrial (Formation of mitochondrial complexes protein 1) (P40491)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Needed for the assembly of the mitochondrial F1-F0 complex at high temperature.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11096112, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Protein ATP12
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- Acyl carrier protein, mitochondrial
- Protein ATP11
- Mitochondrial zinc maintenance protein 1, mitochondrial
- Urea amidolyase
- Mitochondrial ATPase complex subunit ATP10
- Succinate dehydrogenase assembly factor 3, mitochondrial
Sequence:
MDRPRTLRTYRGLIRAILKYERPSKIVNWGNLRKAMITKLEYAKKQNQRDSHENINRQLEKWKKLDPVSDRSLNLFIADSKSLRSILQNDIKWEKKVAQGQNVDEIFEHALDIIKFLDNQREYEELVDRYNPGNKLTQDEKVKRTANVVGLDVPT
Protein: Putative trans-acting enoyl reductase Rv2449c (EC 1.3.1.-) (O53176)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTATPREFDIVLYGATGFVGKLTAEYLARAGGDARIALAGRSTQRVLAVREALGESAQTWPILTADASLPSTLQAMAARAQVVVTTVGPYTRYGLPLVAACAAAGTDYADLTGEPMFMRNSIDLYHKQAADTGARIVHACGFDSVPSDLSVYALYHAAREDGAGELTDTNCVVRSFKGGFSGGTIASMLEVLSTASNDPDARRQLSDPYMLSPDRGAEPELGPQPDLPSRRGRRLAPELAGVWTAGFIMAPTNTRIVRRSNALLDWAYGRRFRYSETMSVGSTVLAPVVSVVGGGVGNAMFGLASRYIRLLPRGLVKRVVPKPGTGPSAAARERGYYRIETYTTTTTGARYLARMAQDGDPGYKATSVLLGECGLALALDRDKLSDMRGVLTPAAAMGDALLERLPAAGVSLQTTRLAS
Protein: Aldehyde dehydrogenase family 3 member B2 (ALDH3B2) (EC 1.2.1.3) (Aldehyde dehydrogenase 8) (Long-chain fatty aldehyde dehydrogenase) (EC 1.2.1.48) (P48448)
Organism: Homo sapiens (Human)
Function: Oxidizes medium and long chain aldehydes into non-toxic fatty acids.
Subcellular location: Lipid droplet {ECO:0000250|UniProtKB:E9Q3E1}.
Interaction partners:
- Aldehyde dehydrogenase family 3 member B1
- Acetyl-coenzyme A synthetase, cytoplasmic
- 4-aminobutyrate aminotransferase, mitochondrial
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Amine oxidase [flavin-containing] A
- Aldo-keto reductase family 1 member A1
- Amine oxidase [flavin-containing] B
- Amine oxidase [copper-containing] 3
- Cytochrome P450 2E1
- Amine oxidase [copper-containing] 2
Sequence:
MKDEPRSTNLFMKLDSVFIWKEPFGLVLIIAPWNYPLNLTLVLLVGALAAGSCVVLKPSEISQGTEKVLAEVLPQYLDQSCFAVVLGGPQETGQLLEHKLDYIFFTGSPRVGKIVMTAATKHLTPVTLELGGKNPCYVDDNCDPQTVANRVAWFCYFNAGQTCVAPDYVLCSPEMQERLLPALQSTITRFYGDDPQSSPNLGHIINQKQFQRLRALLGCSRVAIGGQSNESDRYIAPTVLVDVQETEPVMQEEIFGPILPIVNVQSVDEAIKFINRQEKPLALYAFSNSSQVVNQMLERTSSGSFGGNEGFTYISLLSVPFGGVGHSGMGRYHGKFTFDTFSHHRTCLLAPSGLEKLKEIHYPPYTDWNQQLLRWGMGSQSCTLL
Protein: Non-structural protein ORF5 (ORF5) (K9N7D2)
Organism: Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1)
Function: Seems to play a role in the inhibition of host innate immune repsonse.
Subcellular location: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Host Golgi apparatus {ECO:0000269|PubMed:24318862}. Note=Also localizes in the host perinuclear area.
Interaction partners:
Sequence:
MAFSASLFKPVQLVPVSPAFHRIESTDSIVFTYIPASGYVAALAVNVCLIPLLLLLRQDTCRRSIIRTMVLYFLVLYNFLLAIVLVNGVHYPTGSCLIAFLVILIILWFVDRIRFCLMLNSYIPLFDMRSHFIRVSTVSSHGMVPVIHTKPLFIRNFDQRCSCSRCFYLHSSTYIECTYISRFSKISLVSVTDFSLNGNVSTVFVPATRDSVPLHIIAPSSLIV
Protein: Peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (Cyclophilin B) (Cyclophilin-related protein) (Rotamase B) (P23285)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Secreted.
Interaction partners:
- FK506-binding protein 1
- Peptidyl-prolyl cis-trans isomerase FPR2
- Ran-specific GTPase-activating protein 1
- Cytochrome b5
Sequence:
MKFSGLWCWLLLFLSVNVIASDVGELIDQDDEVITQKVFFDIEHGEEKVGRIVIGLYGKVCPKTAKNFYKLSTTTNSKKGFIGSTFHRVIPNFMVQGGDFTDGTGVGGKSIYGDTFPDENFTLKHDRKGRLSMANRGKDTNGSQFFITTTEEASWLDGKHVVFGQVVDGMDVVNYIQHVSRDANDKPLEAVKIAKCGEWTPELSS
Protein: Zinc finger protein ZIC 1 (Zinc finger protein 201) (Zinc finger protein of the cerebellum 1) (Q15915)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional activator. Involved in neurogenesis. Plays important roles in the early stage of organogenesis of the CNS, as well as during dorsal spinal cord development and maturation of the cerebellum. Involved in the spatial distribution of mossy fiber (MF) neurons within the pontine gray nucleus (PGN). Plays a role in the regulation of MF axon pathway choice. Promotes MF migration towards ipsilaterally-located cerebellar territories. May have a role in shear flow mechanotransduction in osteocytes. Retains nuclear GLI1 and GLI3 in the cytoplasm. Binds to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3' (By similarity).
Subcellular location: Nucleus. Cytoplasm {ECO:0000250}. Note=Localizes in the cytoplasm in presence of MDFIC overexpression. {ECO:0000250}.
Interaction partners:
- Zinc finger protein ZIC 4
- Paired box protein Pax-3
- Zinc finger protein GLI1
- Catenin beta-1
Sequence:
MLLDAGPQYPAIGVTTFGASRHHSAGDVAERDVGLGINPFADGMGAFKLNPSSHELASAGQTAFTSQAPGYAAAAALGHHHHPGHVGSYSSAAFNSTRDFLFRNRGFGDAAAAASAQHSLFAASAGGFGGPHGHTDAAGHLLFPGLHEQAAGHASPNVVNGQMRLGFSGDMYPRPEQYGQVTSPRSEHYAAPQLHGYGPMNVNMAAHHGAGAFFRYMRQPIKQELICKWIEPEQLANPKKSCNKTFSTMHELVTHVTVEHVGGPEQSNHICFWEECPREGKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHESSSQGSQPSPAASSGYESSTPPTIVSPSTDNPTTSSLSPSSSAVHHTAGHSALSSNFNEWYV
Protein: Protein shisa-3 homolog (A0PJX4)
Organism: Homo sapiens (Human)
Function: Plays an essential role in the maturation of presomitic mesoderm cells by individual attenuation of both FGF and WNT signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250, ECO:0000250|UniProtKB:Q7T0Z7}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q7T0Z7}.
Interaction partners:
Sequence:
MRALLALCLLLGWLRWGPAGAQQSGEYCHGWVDVQGNYHEGFQCPEDFDTLDATICCGSCALRYCCAAADARLEQGGCTNDRRELEHPGITAQPVYVPFLIVGSIFIAFIILGSVVAIYCCTCLRPKEPSQQPIRFSLRSYQTETLPMILTSTSPRAPSRQSSTATSSSSTGGSIRRFSFARAEPGCLVPSPPPPYTTSHSIHLAQPSGFLVSPQYFAYPLQQEPPLPGKSCPDFSSS
Protein: Coiled-coil domain-containing 141 (Q9D003)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSCKESPHVGASTTTVSSVAVHAGDSKIVIAVVKCGKWVRLQLAESQPNLLEIGSSQDETKKLLHDHELLLAKLKALEDRVWELLREADRTAEANKAQSQVYDAMAQTLGEAWATLVSMLERRRELLGLTSEFFQSALEFAIKIDQAEAFLQNPHEFESTEALQSLLLLHDRHAKELLERSLDLLNKSQQLTDFIEKFKCEGSTMNSELIQGAQSSCLKIDSLLELLQDRGRQLDKYLQQQRQELSQVLQLCLWDQQENQVSSWFQKAIRDLQEQSLGASLSDNRELICKHEDLIVKAKEWDSAVEKLKSQALGILLSKDLAGKEHLQLSNQKLNRLQEEFGRLMVERKAWLSMANDFFTSANKSFDVLGKVEAYLKLLKSEGLSLPVLAAKHEELHREIKDSTATALQKGRTLISQVDSCR
Protein: Mitochondrial glycine transporter (Appoptosin) (Mitochondrial glycine transporter GlyC) (Solute carrier family 25 member 38) (Q96DW6)
Organism: Homo sapiens (Human)
Function: Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix. Required during erythropoiesis.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03064}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03064}.
Interaction partners:
- Glutaredoxin-related protein 5, mitochondrial
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Iron-sulfur clusters transporter ABCB7, mitochondrial
Sequence:
MIQNSRPSLLQPQDVGDTVETLMLHPVIKAFLCGSISGTCSTLLFQPLDLLKTRLQTLQPSDHGSRRVGMLAVLLKVVRTESLLGLWKGMSPSIVRCVPGVGIYFGTLYSLKQYFLRGHPPTALESVMLGVGSRSVAGVCMSPITVIKTRYESGKYGYESIYAALRSIYHSEGHRGLFSGLTATLLRDAPFSGIYLMFYNQTKNIVPHDQVDATLIPITNFSCGIFAGILASLVTQPADVIKTHMQLYPLKFQWIGQAVTLIFKDYGLRGFFQGGIPRALRRTLMAAMAWTVYEEMMAKMGLKS
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FTY8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- 4-aminobutyrate aminotransferase
- Acetyl-coenzyme A synthetase 1
- Acetyl-coenzyme A synthetase 2
- Glutamate decarboxylase
- S-
- alcohol dehydrogenase
- Candida glabrata strain CBS138 chromosome M complete sequence
- Acetyl-CoA hydrolase
- alcohol dehydrogenase
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MPEVFEEINIPQIGRSYKQPIGIFIDNEFVPSSNGEKIETINPATEEVITSFYAATEDDVDKAVKSARESYENVWFKISPAEKRDMLLKLADLIEEEKPLLAALETLDAGKPYHTNAMDDIDQIIHLTKYFAGATDKFTQGKTIPIDHEKLVYTLKSPYGVCGMIIPWNYPLAMASWKMQGCLAAGNTLVIKPAENTSLSLLYLAQLFKKAGFPKGVVNVVPGKGSVVGNSLGLHMDVDKISFTGSTKVGSSILELAGKSNMKDVTLECGGKSPAVVFQDADIDNAIEYIANGIFYNSGQNCTANSRVYVQEDIYDDFIKRFTEHTKENWKFGSKCDPFDKDCTVGPVVSEKQFETVNDYIRHGKEEENLQIHQTVEKCDCKGYFISPTIFTDVPQGSKLMKEEIFGPVVVVAKFKDYKEAIKLANDTNYGLASMVFTKNISVANWFARDIKSGTVWINSSNEEDPTVPFGGFKQSGIGRELGETGVESYMQIKTVHLNMSEKI
Protein: 60S ribosomal protein L18-B (A0A0W0DNM8)
Organism: Candida glabrata (Yeast) (Torulopsis glabrata)
Interaction partners:
Sequence:
MGIDHTSKQHKRVSHRTAPKSENVYLKMLVRLYTFLARRTDAPFNKVVLKSLFLSKINRPPVSISRIARALKQEGAASKTVVVVGTVTDDARLFDLPKTTVAALRFTAGARARIVKAGGECITLDQLAVRAPKGQNTLILRGPRNAREAVRHFGMGPHKNKAPRIMSKGRKFESARGRRRSKGFKV
Protein: Protein Vpr (R ORF protein) (Viral protein R) (P05928)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1)
Function: During virus entry, plays a role in the transport of the viral pre-integration (PIC) complex to the host nucleus. This function is crucial for viral infection of non-dividing macrophages. May act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04080}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04080}. Host extracellular space {ECO:0000255|HAMAP-Rule:MF_04080}. Note=Incorporation into virion is dependent on p6 GAG sequences. Lacks a canonical nuclear localization signal, thus import into nucleus may function independently of the human importin pathway. Detected in high quantity in the serum and cerebrospinal fluid of AIDS patient. {ECO:0000255|HAMAP-Rule:MF_04080}.
Interaction partners:
Sequence:
MEQAPEDQGPQREPHNEWTLELLEELKNEAVRHFPRIWLHGLGQHIYETYGDTWAGVEAIIRILQQLLFIHFRIGCRHSRIGVTQQRRARNGASRS
Protein: Tegument protein UL47 (Q4VW77)
Organism: bovine alphaherpesvirus 1
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192, ECO:0000256|RuleBase:RU369113}. Host nucleus {ECO:0000256|ARBA:ARBA00004147, ECO:0000256|RuleBase:RU369113}. Virion tegument {ECO:0000256|RuleBase:RU369113}. Note=Major tegument protein of the virion. Undergoes nucleocytoplasmic shuttling during infection. Localizes to the major sites of transcription in the infected cell nucleus. {ECO:0000256|RuleBase:RU369113}.
Interaction partners:
Sequence:
MDAARDGRPERRPRRSGTYRTHPFQRPSARRSLLDALRAADAEAAERPRVRRPRPDFQRPPDEDTSEDENVYDYIDGDSSDSADDYDSDYFTANRGPNHGAGDAMDTDAPPERAPEGGAPQDYLTAHLRAIEALPESAPHRSLLERTARTVYAQQFPPRDLSAGSRAPAQRARRSLRGFPRGGGGGQEPGPDDEGDDAADLREDLVPDEAYAHLERDERLSEGPPLLNMEAAAAAAGERSVVEELFTYAPAQPQVEVPLPRILEGRVRPSAFFAQMPLDALCRTPPNDQRVVRERRAWEMAGTPHGLLITTWSTVDPEFSIGGMYVGAPEGTRPRLVWRRAMKQAMALQYRLGVGGLCRAVDGAAMPPTEALLFLADALLRVVRNCHFLSRPGRAGGAARRLPAAAVGLLAATQFTPPDASPHATLFRGSMGSLIYWHELRVMLTAVPALCARYAGAGLQSAELYLLALAHSEAPGYTANERYALSAYLTLFVALAERALRWLYLAGAHLLGPHPTAAAFREVRAKIPYERLPLGSATLHDAEVETVDSATFQEALAFSALAHVYGEAYVAVRTATTLLMAEYAAHAERRDVREMTAAFLGVGLIAQRLMGSLNLLLNCVAGAAVYGGRRVTVREGTLARYSLLADAALPLVRPVSLVEFWEARDGVMRELRLRPVASPPLAGKRRVMELYLSLDSIEALVGREPLGSRPVLGPLVDIAEALADHPHLVTGDGRGPRLGGR
Protein: Tumor protein D54 (hD54) (Tumor protein D52-like 2) (O43399)
Organism: Homo sapiens (Human)
Interaction partners:
- Protein MAL2
- Tumor protein D53
- Tumor protein D52
- GA-binding protein subunit beta-1
- MAL-like protein
- Tumor protein D55
Sequence:
MDSAGQDINLNSPNKGLLSDSMTDVPVDTGVAARTPAVEGLTEAEEEELRAELTKVEEEIVTLRQVLAAKERHCGELKRRLGLSTLGELKQNLSRSWHDVQVSSAYVKTSEKLGEWNEKVTQSDLYKKTQETLSQAGQKTSAALSTVGSAISRKLGDMRNSATFKSFEDRVGTIKSKVVGDRENGSDNLPSSAGSGDKPLSDPAPF
Protein: TIGR02611 family protein (P95289)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv1526c
- Possible oxygenase
- Conserved protein
- Glycoside hydrolase
- PE_PGRS6
Sequence:
MDPADVINPTSTRDAALARVLAYRQRVRARPLLIRATLAVVGGGLFVVSLPMIVLLPELGIPALLVAFRLLAVEAQWAVRAYAWTDWRFTQLREWFHRQVLVTRAAILVGLFLAAVALVWLLVYEF
Protein: FLYWCH family member 2 (Q96CP2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPLPEPSEQEGESVKASQEPSPKPGTEVIPAAPRKPRKFSKLVLLTASKDSTKVAGAKRKGVHCVMSLGVPGPATLAKALLQTHPEAQRAIEAAPQEPEQKRSRQDPGTDRTEDSGLAAGPPEAAGENFAPCSVAPGKSL