wanglab/gogpt-training-data huggingface dataset:
Protein: Protein FAM83A (Tumor antigen BJ-TSA-9) (Tumor-specific gene expressed in prostate protein) (Q86UY5)
Organism: Homo sapiens (Human)
Function: Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both RAS/MAPK and PI3K/AKT/TOR signaling cascades downstream of EGFR. Required for the RAS/MAPK signaling cascade activation upon EGFR stimulation, it also activates both signaling cascades independently of EGFR activation.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:22886303}.
Interaction partners:
Sequence:
MSRSRHLGKIRKRLEDVKSQWVRPARADFSDNESARLATDALLDGGSEAYWRVLSQEGEVDFLSSVEAQYIQAQAREPPCPPDTLGGAEAGPKGLDSSSLQSGTYFPVASEGSEPALLHSWASAEKPYLKEKSSATVYFQTVKHNNIRDLVRRCITRTSQVLVILMDVFTDVEIFCDILEAANKRGVFVCVLLDQGGVKLFQEMCDKVQISDSHLKNISIRSVEGEIYCAKSGRKFAGQIREKFIISDWRFVLSGSYSFTWLCGHVHRNILSKFTGQAVELFDEEFRHLYASSKPVMGLKSPRLVAPVPPGAAPANGRLSSSSGSASDRTSSNPFSGRSAGSHPGTRSVSASSGPCSPAAPHPPPPPRFQPHQGPWGAPSPQAHLSPRPHDGPPAAVYSNLGAYRPTRLQLEQLGLVPRLTPTWRPFLQASPHF
Protein: ATP-binding cassette sub-family C member 5 isoform X1 (ATP-binding cassette, sub-family C (CFTR/MRP), member 5) (Multidrug resistance-associated protein 5 isoform X1) (E7EYG0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MKGHDLGKDCLAAGSAYRAVPSRETLPGPDGDHYELSKVQDAFETAARAEGGLSLDRGNAADAKELEEDAAGRSKYHHSVCVLKPIRSTSKYQHPVDNAGLFSFMTFNWLTSLAVLAHKKGQLFLEDIWAVSQFESCEINRRRLAGLWEEEIRSRGDDASLRRVVWHFCRTRLLLSILCLMVTQLAGFSGPAFVVWRLLEYTQRSEPDLPYGLLLVLGLLATELIRSWSLALTWALNYRTGTRLRGAILTMAFHKILRLRSLREKSMGELINMCSGDGQRMFEAAAVGSLLAGGPLVAVLGMAYNLFVLGPTSLLGSAVFILFYPTMMFSSRLTAYFRRKGVAVTDQRVQKMNEILNYIKFIKMYAWVKAFSQAVRRIRDEERQILERTGYFQSITVGVAPIVVVIASVATFSTHMLLGYDLTAAQAFTVVTVFNAMTFALKVTPFSVKSLSEASVAIDRFKSLLLMAEVKMIRELPRNPSVAVEMSGASLAWETGGHSAQPSPRGTPHVGTRGCRKKRRQRDVPKHHAILEEETHGQLLNDVSGEMASSPEDQTLHVPTISQRLQRTLHCIDLSIQKGKLVGVCGSVGSGKTSLISAILGQMTLLEGTVAVDGDFAYVAQQAWILNASFRDNILFGKEMEEERYQAILSACCLRPDLAILPSGDLTEIGERGANLSGGQRQRISLARALYSNRGIYILDDPLSALDAHVGNHIFNNAIKKQLRGKTVIFVTHQLQYLVDCDDVIVMRDGSITEQGSHEDLMNVNGDYAAMFNNLQLGETPIIEVPNKKSGSSLKKPLEKSKAGSVKKEKSTTQGDGQLMQVEERGKGSVPWAVYKVYIQALGGWPVFLFILALFILNVGSTAFSNWWLSYWIKQGSGNTTVQVGNSSVLSESMRDNPLMQHYAAVYTMSMGVMLLLKLLRGIVFVKGTLRASSRLHDELFQKILRSPMKFFDTTPTARILNRFSKDMDEVDTRLPFQAEMFIQNVILVLFCLAVIGSVFPWFLVAVGPLVLLFTVLHVVSRVFIRELKRLDNVTQSPFLSHIASSIQGLTTVHAYGKEDEFLHRYQELLDQNQAPFYLFSCAMRWLAVRLDVISVALISITALMIVLMHGQIPPAYAGLAISYAVQLTGLFQFTVRLASETEARFTSVERIHHYIKSLSLEAPARVKNKAPPSDWPQEGEIVFDQTEMKYRDNLPLILKKVSFTVRPKEKIGIVGRTGSGKSSLGVVLYRLVEPCGGSIKIDGVNICDIGLADVRSKLSIIPQEPVLFSGTVRSNLDPFSQYSEAQIWDALERTHMKECVSQLPLKLESEVVENGENFSVGERQLLCVARVLLRQCKILILDEATAAMDTETDCLIQETIRNAFQDCTTLTIAHRVHTVLSCDRIMVLNQGQVVEFDEPSKLLANENSRFCAMLAAVENKISVRG
Protein: Eukaryotic translation initiation factor 3 subunit M (eIF3m) (Q5B5C1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit D
Sequence:
MPAPSTTLLIEGSFSELAEEFAAYLDALNKPDDTTVQTEVAPLLQPLREQEQNDTQLDQSKRDEVLKKLVSAATVLNTAPEKEITPAYNLLIHLVQQASDPDMFLSRICSYLAKPIPSSPQFGASLSIAILSTIFNTLAPTDSSRFHVLLAIVTVIRQSGSSAAFDALKPQLTAQLPNWRSTWELDDEEARRLHLAIADAAQAAGDLDWAQTHVVDALQTIPPAEASSPAARDLAVRALTSALTHPAVFDFTPLTAADAVQALRSSDAPLFELLEIFTADTLDAYEDFISATPVENILPDNALAPHAEALQTKIRLLTLASLAAAATTTTGPSARSLSYETIASALRVPQEEVEKWVIDTIRAGLVEGKLSQLRSEFLVHRATYRVFGEKQWAEVQGRLMVWRRSLENVLGVIRSERERFVREAAAAAAAAAAEGEKGDKNNKGPSERRRAPQEIAAAE
Protein: Probable xyloglucan galactosyltransferase GT11 (EC 2.4.1.-) (Glycosyltransferase 11) (AtGT11) (O81072)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions in xyloglucan synthesis by adding side chains to the xylosylated glucan backbone. Involved in the galactosylation of hemicellulose xyloglucan.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q7XJ98}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q7XJ98}.
Interaction partners:
- O-fucosyltransferase 14
- O-fucosyltransferase 5
- O-fucosyltransferase 36
- O-fucosyltransferase 23
- O-fucosyltransferase 27
- O-fucosyltransferase 29
- O-fucosyltransferase 15
- Probable apyrase 7
- O-fucosyltransferase 1
- Rhamnogalacturonan I rhamnosyltransferase 4
Sequence:
MAMEKSSSKYRTQFWYVAMASFLLWLVLLYLFSSSAKTVHNHERLFRQENIIDLPVENVPQNHEPDEAPVVNVVSEDISVDNSSLPVSVDSPPDDQMSEDKKVVTDLVEELEKERVENEKKRVDSVVIGRSSKARRGHREPRKARSSGRLEAEKKRVRRNDADESNAENSDENHQALDKEPNFFEAKKDVEPKKALVDDNDDDLETKRGKELPNDSSSNVVEDDNDDDLETKKGKDNISKSEPKTQRNFVLNKNNTSKAKNRVISKRNQPSRVGKVMLRPRETRSNDPCKGKYVYMHEVPALFNEELLKNCWTLSRWTDMCELTSNFGLGPRLPNMEGVSGWYATNQFTLEVIFHNRMKQYKCLTKDSSLASAVYVPYYPGLDLMRFLWGPFPFMRDAAALDLMKWLRESQEWKRMDGRDHFMVAGRTTWDFMRTPENESDWGNRLMILPEVRNMTMLLIESSPWNYHGFAVPYPTYFHPSTYAEIIQWQMRMRRINRRYLFSFVGAPRPNLGDSIRTEIMDQCKASKRKCKLLECISGSQKCYKPDQIMKFFLSSTFCLQPPGDSYTRRSTFDSILAGCIPVFFHPGSAYAQYIWHLPKDIAKYSVFIPEKNVKEGKVSIENVLSRIPRTKVFAMREQVIRLIPRLMYFHPSSKSEDTGRFEDAFDVAVEGVLERVEGLRKRIEEGKEEIFDFPEQYSWKYNVFGNVERHEWDPYFDRP
Protein: Triacylglycerol lipase (EC 3.1.1.3) (Esterase/lipase) (Triolein hydrolase) [Cleaved into: Cytosolic triacylglycerol lipase; Extracellular triacylglycerol lipase] (I6Y2J4)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the hydrolysis of both intracellular and extracellular triacylglycerol (TAG). In vitro, can also hydrolyze p-nitrophenyl (pNP) esters with various chain lengths, including pNP-acetate (C2), pNP-butyrate (C4), pNP-caproate (C6), pNP-caprylate (C8), pNP-laurate (C12), pNP-myristate (C14), pNP-palmitate (C16) and pNP-stearate (C18). Also hydrolyzes monobutyrin, tributyrin and trioctanoin. Overexpression results in increase of virulence characterized by reduced survival of infected mouse and increased burden of bacilli in the lungs. Hydrolyzes internal or host-derived TAG depending on its localization.
Subcellular location: [Cytosolic triacylglycerol lipase]: Cytoplasm {ECO:0000269|PubMed:29986895}.; SUBCELLULAR LOCATION: [Extracellular triacylglycerol lipase]: Secreted {ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693, ECO:0000269|PubMed:31662454}. Secreted, cell wall {ECO:0000269|PubMed:17938218, ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693}. Cell surface {ECO:0000269|PubMed:17938218, ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:29986895, ECO:0000269|PubMed:31034693, ECO:0000269|PubMed:31662454}. Note=Exported to the cell surface via the ESX-5 / type VII secretion system (T7SS). {ECO:0000269|PubMed:21471225, ECO:0000269|PubMed:31034693, ECO:0000269|PubMed:31662454}.
Interaction partners:
- Probable diacyglycerol O-acyltransferase Tgs4
- Putative diacyglycerol O-acyltransferase Rv3480c
- Probable diacyglycerol O-acyltransferase tgs1
- Putative diacyglycerol O-acyltransferase Rv3087
- Putative diacyglycerol O-acyltransferase Rv2285
- Putative diacyglycerol O-acyltransferase Rv0895
- Putative diacyglycerol O-acyltransferase Rv3740c
- Probable diacyglycerol O-acyltransferase tgs2
- Putative diacyglycerol O-acyltransferase Rv1425
- Putative diacyglycerol O-acyltransferase Rv1760
Sequence:
MVSYVVALPEVMSAAATDVASIGSVVATASQGVAGATTTVLAAAEDEVSAAIAALFSGHGQDYQALSAQLAVFHERFVQALTGAAKGYAAAELANASLLQSEFASGIGNGFATIHQEIQRAPTALAAGFTQVPPFAAAQAGIFTGTPSGAAGFDIASLWPVKPLLSLSALETHFAIPNNPLLALIASDIPPLSWFLGNSPPPLLNSLLGQTVQYTTYDGMSVVQITPAHPTGEYVVAIHGGAFILPPSIFHWLNYSVTAYQTGATVQVPIYPLVQEGGTAGTVVPAMAGLISTQIAQHGVSNVSVVGDSAGGNLALAAAQYMVSQGNPVPSSMVLLSPWLDVGTWQISQAWAGNLAVNDPLVSPLYGSLNGLPPTYVYSGSLDPLAQQAVVLEHTAVVQGAPFSFVLAPWQIHDWILLTPWGLLSWPQINQQLGIAA
Protein: Beta-hexosaminidase A (EC 3.2.1.52) (Beta-N-acetylhexosaminidase) (N-acetyl-beta-glucosaminidase) (Q22492)
Organism: Caenorhabditis elegans
Function: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines. Degrades chitotriose.
Subcellular location: Lysosome {ECO:0000305}.
Interaction partners:
- Alpha-galactosidase
- Beta-galactosidase
- Probable endochitinase
- GH18 domain-containing protein
- beta-N-acetylhexosaminidase
- Fucosyltransferase
- N-acetyl-D-glucosamine kinase
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- Alpha-
Sequence:
MRLLIPILIFALITTAVTWFYGRDDPDRWSVGGVWPLPKKIVYGSKNRTITYDKIGIDLGDKKDCDILLSMADNYMNKWLFPFPVEMKTGGTEDFIITVTVKDECPSGPPVHGASEEYLLRVSLTEAVINAQTVWGALRAMESLSHLVFYDHKSQEYQIRTVEIFDKPRFPVRGIMIDSSRHFLSVNVIKRQLEIMSMNKLNVLHWHLVDSESFPYTSVKFPELHGVGAYSPRHVYSREDIADVIAFARLRGIRVIPEFDLPGHTSSWRGRKGFLTECFDEKGVETFLPNLVDPMNEANFDFISEFLEEVTETFPDQFLHLGGDEVSDYIVECWERNKKIRKFMEEKGFGNDTVLLENYFFEKLYKIVENLKLKRKPIFWQEVFDNNIPDPNAVIHIWKGNTHEEIYEQVKNITSQNFPVIVSACWYLNYIKYGADWRDEIRGTAPSNSRYYYCDPTNFNGTVAQKELVWGGIAAIWGELVDNTNIEARLWPRASAAAERLWSPAEKTQRAEDAWPRMHELRCRLVSRGYRIQPNNNPDYCPFEFDEPPATKTEL
Protein: Gag polyprotein (Core polyprotein) (Pr78) [Cleaved into: Matrix protein p10; Phosphorylated protein pp24; Phosphorylated protein pp18; p12; Capsid protein p27; Nucleocapsid protein p14; p4] (P07567)
Organism: Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus)
Function: Matrix protein.
Subcellular location: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKSNSQTDLTKTSQNPDLDLISLDSDDEGAKSSSLQDKGLSSTKKPKRFPVLLTAQTSKDPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTHPDTAGGLSRTPHWPGQHIPKGKCCASREKEEQIPKDIFPVTETVDGQGQAWRHHNGFDFAVIKELKTAASQYGATAPYTLAIVESVADNWLTPTDWNTLVRAVLSGGDHLLWKSEFFENCRDTAKRNQQAGNGWDFDMLTGSGNYSSTDAQMQYDPGLFAQIQAAATKAWRKLPVKGDPGASLTGVKQGPDEPFADFVHRLITTAGRIFGSAEAGVDYVKQLAYENANPACQAAIRPYRKKTDLTGYIRLCSDIGPSYQQGLAMAAAFSGQTVKDFLNNKNKEKGGCCFKCGKKGHFAKNCHEHAHNNAEPKVPGLCPRCKRGKHWANECKSKTDNQGNPIPPHQGNGWRGQPQAPKQAYGAVSFVPANKNNPFQSLPEPPQEVQDWTSVPPPTQY
Protein: Peroxisomal membrane protein PEX16 (A0A8I6A5Q8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Peroxisome membrane {ECO:0000256|RuleBase:RU365003}.
Interaction partners:
Sequence:
MEKLRLLGLRYQEYVTRHPAATAQLETAVRGLSYLLAGRFSDSHELSELVYSASNLLVLLNDGILRKELRKKLPVSLSQQKLLTWLSVLECVEVFMEMGAAKVWGEVGRWLVIALIQLAKAVLRMFLLIWFKTGIQTSPPIVPLDRETQAQPLDGDHNLGSPEPSYVGKRSNRVVRTLQNSPSLHSRHWGAPQQREIRQKQQQEELSTPPTPLGLQETIAESLYIARPLLHLLSLGLWGQRSWAPWLLSGVVDMTSLSLLSDRKNLTRRERLELRRRTILLLYYLLRSPFYDRFSEAKILFLLQLLADHIPGIGLVASKCG
Protein: Prolyl 4-hydroxylase subunit alpha-2 (4-PH alpha-2) (EC 1.14.11.2) (Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-2) (Q60716)
Organism: Mus musculus (Mouse)
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
- Protein disulfide-isomerase
- Prolyl 4-hydroxylase subunit alpha-1
- Prolyl 4-hydroxylase subunit alpha-3
- Pyrroline-5-carboxylate reductase 3
- Proline dehydrogenase 1, mitochondrial
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Hydroxyproline dehydrogenase
- Pyrroline-5-carboxylate reductase 2
- Cytosol aminopeptidase
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
Sequence:
MKLQVLVLVLLMSWFGVLSWVQAEFFTSIGHMTDLIYAEKDLVQSLKEYILVEEAKLAKIKSWASKMEALTSRSAADPEGYLAHPVNAYKLVKRLNTDWPALGDLVLQDASAGFVANLSVQRQFFPTDEDESGAARALMRLQDTYKLDPDTISRGELPGTKYQAMLSVDDCFGLGRSAYNEGDYYHTVLWMEQVLKQLDAGEEATVTKSLVLDYLSYAVFQLGDLHRAVELTRRLLSLDPSHERAGGNLRYFERLLEEERGKSLSNQTDAGLATQENLYERPTDYLPERDVYESLCRGEGVKLTPRRQKKLFCRYHHGNRVPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPKLARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVANYGMGGQYEPHFDFSRSDDEDAFKRLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKKGTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGTTEVD
Protein: Tyrosine recombinase XerD-like (P0A4S9)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Putative tyrosine recombinase. Not involved in the cutting and rejoining of the recombining DNA molecules on dif(SL) site.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01817}.
Interaction partners:
Sequence:
MRDRISAFLEEKQGLSVNSKQSYKYDLEQFLDMVGERISETSLKIYQAQLANLKISAQKRKISACNQFLYFLYQKGEVDSFYRLELAKQAEKKTEKPEILYLDSFWQESDHPEGRLLALLILEMGLLPSEILAIKVADINLDFQVLRISKASQQRIVTIPTALLSELEPLMGQTYLFERGEKPYSRQWAFRQLESFVKEKGFPSLSAQVLREQFILRQIENKVDLYEIAKKLGLKTVLTLEKYR
Protein: Mannose-1-phosphate guanylyltransferase (EC 2.7.7.13) (GDP-mannose pyrophosphorylase) (GMP) (GMPP) (P24174)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of the capsular polysaccharide colanic acid.
Interaction partners:
- Phosphomannomutase
- GDP-mannose 4,6-dehydratase
- UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase
- GDP-L-fucose synthase
- Putative colanic acid biosynthesis glycosyl transferase WcaI
- GDP-mannose mannosyl hydrolase
- Putative colanic acid biosynthesis glycosyl transferase WcaA
- Tyrosine-protein kinase wzc
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Low molecular weight protein-tyrosine-phosphatase Wzb
Sequence:
MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILEPAGRNTAPAIALAALAAKRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIRRGEVSAGEQDMVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLNFIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV
Protein: Rho GTPase activating protein 4 (A0A8I5ZY52)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAHGKLRRERGLQPEYEAQVKVMRGQLSEQLHCLELQGELRRDLLLELAEFMRRRAEVELEYSRGLDKLAERFTSRSGRLGGSSREQQSFRKEPTLLSPLHCWAMLLEHTRQQSRESATLSEVLAGPLAQRLSHIAEDVGRIVKKSKDLVQQLQDELLEVVSELQTTKKTYHVYHLESMNAETKLREAERQEEKRSGKSALPTTTAASATTTITIETELHRKGSLKKGGRLVEKRQAKFLEHKLKCTKARNEYLLSLASVNAAVSNYYLHDILDLMDCCDTGFHLALEQALRSYTAAESRTQTSHMQGLGSLEEALEALDPPGDKAKVLEVHAMAFCPPLRFDYQPHEGDEVNKTLKATLQALLEVVASEDGDILDSLQASPSTESLKSTSSDPGTRQAGRRRNQQQETETFYITKLQEYLSGRSILAKLQAKHEKLQEAIQRGNKEEQETSSWTQCTERKFHKSHHPYPGSQCTQRLFGGDLEKFIQSTGQPVPLVVKSCIRFINLNGLQHEGIFRVSGAQARILEIRDAFERGEDPLVEGCTAHDLDSVAGVLKLYFRSLEPPLFPLDMFNELLASAELEVVGERVELVSHLLSRLPRPVLVVLRYLFTFLNHLAQYSDENMMDSYNLAVCFGPTLLPVPAGQDPVALQGRVNQLVQTLILQPAWVFPPTAMLPGPIYEKCMAPPSASCLGDGQLESLAGEPELELKTGTKAQEDDSEGVVEAVACFAYTGRTAQELTFQQGDTLRLYARASSDWWRGEHAGVRGLIPHKYITLSEGDEKQMTGSGLQAMGESLSHPESVLTLEFTNRLELGTPPEALGPSGHRRHCLVPTSPEQHVEMDKAVAQNMDSVFKELLGKAAVRQGHGLASTASPSLGTRNLKPLACSSFSKNKVFSRGPGAPVSPSVSHPQGPDSTRKPV
Protein: Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (Q4Q256)
Organism: Leishmania major
Subcellular location: Endoplasmic reticulum {ECO:0000256|RuleBase:RU365083}.
Interaction partners:
- Putative dolichyl-P-Man:GDP-Man5GlcNAc2-PP-dolichyl alpha-1,3-mannosyltransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Putative dolichyl-P-Man:GDP-ManGlcNAc2-PP-dolichyl beta-1,4-mannosyltransferase
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- Putative dolichyl pyrophosphate phosphatase
- mannose-1-phosphate guanylyltransferase
- Phosphomannomutase
- Mannosyltransferase
- GDP-Man:Man
- GPI mannosyltransferase 1
Sequence:
MQYSIIVPAYKECGNLEPLIRRVFAAVTEQGFPTQNVEMLIVDDNSRDGSKEVVDRLHEEGFNVHMDVRTTERGLSSAVIHGLRHTSGAYKLVMDADLQHPPECVPALFKALGRDGVEFVCGTRYGVGIEVDKNWPAHRRLISWGARLLARPLTTLSDPMSGFFAIRDGVFKRHAGEVNSIGYKIALELFVKCRVQCFEEVGFNFATRTYGESKLTGKVILHYLEHLYALYLFKLGRLFYVFVVVAVLFAIYLLAFLYHSLF
Protein: Voltage-dependent L-type calcium channel subunit alpha (G5EG02)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
Interaction partners:
Sequence:
MSVLASMMSSGEDEEQAAADEQERTDLWQQTLQAAVAASSSQDATKKRPAQRKPLRQTNVVERSERSLLCLSLNNPIRKLCISIVEWKPFEFLILFMICANCIALAIYQPYPAQDSDYKNTLLETIEYVFIVVFTIECVLKIVAMGFMFHPSAYLRNAWNILDFIIVVIGLVSTILSKMSIQGFDVKALRAFRVLRPLRLVSGVPSLQVVLNAILRAMIPLLHIALLVLFVILIYAIIGLELFCGKLHSTCIDPATGQLAQKDPTPCGTDTEGSAFKCQPSDSLTNMGVRWECSSNTTWPGPNNGITNFDNFGLAMLTVFQCVSLEGWTDVMYWVNDAVGREWPWIYFVTLVILGSFFVLNLVLGVLSGEFSKEREKARARGLFQKFREKQQLEEDLKGYLDWITQAEDIEPVNEDEQEDEPVAQTVVGEEADEEGEERVEDVRPSKWAARMKRLEKLNRRCRRACRRLVKSQTFYWLVILLVLLNTLVLTSEHYGQSEWLDHFQTMANLFFVILFSMEMLLKMYSLGFTTYTTSQFNRFDCFVVISSILEFVLVYFDLMKPLGVSVLRSARLLRIFKVTKYWTSLRNLVSSLLNSLRSIISLLLLLFLFIVIFALLGMQVFGGKFNFNPQQPKPRANFDTFVQALLTVFQILTGEDWNTVMYHGIESFGGVGTLGVIVCIYYIVLFICGNYILLNVFLAIAVDNLADADSLTNAEKEEEQQEIEGEDEEFEEGEDEGEEHGMDEPEGDEEMTSARPRRMSEVPAASTVKPIPKASSLFILSHTNSFRVFCNMVVNHSYFTNAVLFCILVSSAMLAAEDPLQANSTRNMILNYFDYFFTSVFTVEITLKVIVFGLVFHKGSFCRNAFNLLDILVVAVSLTSFVLRTDAMSVVKILRVLRVLRPLRAINRAKGLKHVVQCVIVAVKTIGNIMLVTFMLQFMFAIIGVQLFKGTFFLCNDLSKMTEAECRGEYIHYEDGDPTKPVSKKRVWSNNDFNFDNVGDAMISLFVVSTFEGWPQLLYVAIDSNEEDKGPIHNSRQAVALFFIAFIIVIAFFMMNIFVGFVIVTFQNEGEREYENCELDKNQRKCIEFALKAKPHRRYIPRNRLQYRVWWFVTSRAFEYVIFLIIVMNTVSLACKHYPSSRGFEDFLDVFNLIFTGVFAFEAVLKIVALNPKNYISDRWNVFDLLVVVGSFIDITYGKLNPGGTNLISINFFRLFRVMRLVKLLSRGEGIRTLLWTFMKSFQALPYVALLIVLLFFIYAVIGMQFFGKVALDDSTSIHRNNNFHSFPAAILVLFRSATGEAWQDIMLSCSDREDVRCDPMSDDYHKGGLNESRCGNNFAYPYFISFFMLCSFLVINLFVAVIMDNFDYLTRDWSILGPHHLEEFVRLWSEYDPDAKGRIKHLDVVTLLRKISPPLGFGKLCPHRLACKRLVSMNMPLNSDGTVCFNATLFALVRTNLKIYTEGNIDEANEQLRSAIKRIWKRTHKDLLDEVVPPAGKEDDVTVGKFYATFLIQDYFRRFKKRKEMEAKGVLPAQTPQAMALQAGLRTLHEIGPELKRAISGNLETDFNFDEPEPQHRRPHSLFNNLVHRLSGAGSKSPTEHERIEKGSTLLPFQPRSFSPTHSLAGAEGSPVPSQMHRGAPINQSINLPPVNGSARRLPALPPYANHIHDETDDGPRYRDTGDRAGYDQSSRMVVANRKYADARIVGAARREIEEAYSLGEQEIDLAADSLAPLMQHVGMHDIRDINENSRSALLRPAENSSRQHDSRGGSQEDLLLVTTL
Protein: Mis18-binding protein 1 (Kinetochore-associated protein KNL-2 homolog) (Q80WQ8)
Organism: Mus musculus (Mouse)
Function: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6P0N0}. Chromosome, centromere {ECO:0000250|UniProtKB:Q6P0N0}. Note=Associated with centromeres in interphase cells, from late anaphase to the G1 phase. Not detected on centromeres during earlier phases of mitosis. Associated with chromatin. {ECO:0000250|UniProtKB:Q6P0N0}.
Interaction partners:
- Protein Mis18-alpha
- Protein Mis18-beta
- Centromere protein I
- Holliday junction recognition protein
- Dual specificity protein kinase TTK
- Centromere protein N
- Kinesin-like protein KIF11
- Histone H3-like centromeric protein A
- Kinesin-like protein KIF20B
- Kinesin-like protein KIF18A
Sequence:
MIVTPLKHSGIHLSSGTLQRRNMPLDAVFIDSIPSGTLTPLKDLVKYQKSSLKVNGHKKNQLLEIRTSNNKDLFQSTMLSEATLPNSSLDISVIKPSMDRLRNEMIYESPGKIFQRMKAKVQRDKQEQLTRSSSMLGSPQGEHTKDFPPNTDKKAQLQQTYICEEKQTSVQSNDPSLGDPPILNQEQKNVSASCISKKALTRAQFGGQVLHSKESPVRITVSKKNTFVLGGIDCTYEKFENTDVNTISSLCVPIKNHSQSITSDNDVTTERTAKEDITEPNEEMMSRRTILQDPIKNTSKIKRSSPRPNLTLSGRSQRKCTKLETVVKEVKKYQAVHLQEWMIKVINNNTAICVEGKLVDMTDVYWHSNVIIERIKHNELRTLSGNIYILKGLIDSVSMKEAGYPCYLTRKFMFGFPHNWKEHIDKFLEQLRAEKKNKTRQETARVQEKQKSKKKDAEDKETYVLQKASITYDLNDNSLERTEVPTDPLNSLEQPTSGKERRHPLLSQKRAYVLITPLRNKKLIEQRCIDYSLSIEGISDFFKAKHQEESDSDIHGTPSSTSKSQETFEHRVGFEGNTKEDCNECDIITARHIQIPCPKSKQMLTNDFMKKNKLPSKLQKTENQIGVSQYCRSSSHLSSEENEVEIKSRTRARNTKERLNRERENTNHITKDILLISETEGERACYITPKRPRSCYITPKRPRSSAKESHYKSAVSKDFLTEGKASDRTSRQLLDHLPGLTDDEEWSEQELQKLHCAFTSLPKHKPGFWSDVAMAVGSRTADECQKKYTEEPQGQGSRKHGSKKKQANKVQNGEKDSADAKTIKITAKVGTLKRKRQMRDCLEHLAKDNHDDFFTATPLQKQRIQLPSFQYSQDDDFLLDMDRDPASPSSIITSPLRSTTPQCQHFSPSMLAAIERNNCDRYVYQMQKNAKKYGKSNGGLVWGNIRKKTVKTDLSSPPPTRKALFNKDLGKNTDISKYFIDDTESDEEEKDYYFSNSD
Protein: Larval cuticle protein 65Ab1 (Larval cuticle protein 5) (C0HL62)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the cuticle of the larva.
Interaction partners:
Sequence:
MKFLIVFVALFAMAVARPNLAEIVRQVSDVEPEKWSSDVETSDGTSIKQEGVLKNAGTDNEAAVVHGSFTWVDEKTGEKFTITYVADENGYQPQGAHLPVAPVA
Protein: Serine protease inhibitor A3C (Serpin A3C) (Kallikrein-binding protein) (KBP) (P29621)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Transcription factor PU.1
- Intraflagellar transport protein 122 homolog
Sequence:
MAFIVALGLVITGICPGVLCFPDGTLERDTLFHKDKENGTQLDSLTLASINTDFAFSLYKKLALKNPDTNIVFSPLSISAALAIVSLGAKGNTLEEILEGLNFNLTETPEADIHQGFGHLLQRLSHPGEQVQISTGSALFVEKHLQILAEFQEKARALYQAEAFTADFQQPLEATKLINDYVSNQTQRKIKGLISDLDTDTLMVLVNYIYFKGKWKMPFNPRDTFESEFYLDVKRSVKVPMMKIKTLTTPYFRDEELSCTVVELKYKGNASALFILPDQGRMQQVEASLQPETLRKWKNSLRPRKMGELYLPKFSISTDYSLKNILPELGIKEIFSKQADLSGITGTKDLIVSQMVHKAVLDVAETGTEGVAATGVNFRILSRRTSLWFNRTFLMVISHTDVQTTLFIAKITHPKRA
Protein: GH10162p (Q9W2N5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- WD repeat-containing protein 26 homolog
- Ran-binding proteins 9/10 homolog
- E3 ubiquitin-protein transferase MAEA
- Houki
- FI21269p1
- Ubiquitin-conjugating enzyme E2 H
- RH01588p
- Protein yippee-like
- Protein yippee
Sequence:
MDSESLACSSVEKDLTRVVSKLEQLHENAEADIGDIATQMSELVEVLSRAEQLVTTLNSSTQVSQDDPMGDAVSMQVETEPTAPQRLTERQVESVRNALARCHERVQKLSTEHRDLHGSISKIGKAIDRNFSADFSSTMRVDVLQDEENLMLLNKAIAKHYCRQGMDDVARTLIRECKMSPEHAQDVFDSEREFADIYGIWVKIQKRDLTDALKWAKMYSQQLSDRHSLIEFRLHRMRFMQLVSYGLDSQREAISYARLNFKKFAVRYEHEIANLMASFIYLPSGLENSPYKHFLGQEKWTELSFIFLKDACQLLGISKNSALSVVVNAGCTALPALLNIKQVMQSRQVLGMWNGCDELPIEIDLQPEFRFHSIFACPILRQQTSEDNPPKKLTCGHVISNDALHKLSVGHILKCPYCPVEQNAEEAVRIYF