wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein (Q57WH2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEDEWNTDGGLVSLTLEVPSAIQLPGSIRFRSFTETSYEDNESGDSATITAWKATRWNDLGIHKRRRLDDAPGYECGDVVQPLLHVVKDSFDVAQRRMETLHWFQKPRSAEEISARFALDRRLGVTPSLAATHQALTRLQQLNRTEAIIDLAEDLVMDSPTISLWTLLRIVDGLKGQPQCAARIVFSLSPLVTNGAVPPSAWTSLCDGLDKVARQLPAPLERPLVELFGEVLYRARDDGPVDGKFVVYYGQALLKSRAPIGSIMGFVRAELLSGRNAPSADGTSAIRLGAFLSDLIQVMCSASGGAEEREERVPLSAADRLMHCGDLVKHAYAGRLQLTQGAFDAFLRFCDESQDYHRLCIVFLAMCTLSTPTLSSVARVAEVLCDVKQMSDYLADVLHQSTPSLMLYLLLRHGSVSLFPQINNNNIRTRGGNVSNNERDKLEMHFCTCLARLCVRDGDEFVCMALFSAIIDIGRPVGASAFISEVANSLRCPVKLFGGRATPAGVAASVEPFNVEALYYALRPAVASSGSGGIGDGTSLDALRTIPQSRPLASLLGGRDLAEKTCGTTVEQALAGLLTSPHVYCTVVCESAISSLVKSPPLAEAFAKMMDGYATKMGAIAFVPFDVCTAEQLTDDGRKFLFEWISRYAWFVVLPLSLTMQLAMNPAAVTVGKWKTEERLNESRCIRLFHAIQAAKHTKVAFITAEPNVAEDAKASGVHPVITLTDLAKRLGIN
Protein: Enkurin domain-containing protein (Q4GZB9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Cilia- and flagella-associated protein 45
- Uncharacterized protein
- Uncharacterized protein
- CFA20 domain-containing protein
- Uncharacterized protein
Sequence:
MSGENIKNLLAPQPTVDQGPYSGKYEKRMVDLPKPTYSTFYNKNKEFDSTHPRYFKQRDAVIGPIVNDTVDPKNFLRTGQGIKHIVPPVPHKKQHRKDFLDCGDIRKRTQGAMEPADQQQKESSGMGGMGSLANTNGVGGQAGDGIREHDMSSNDPERKGEQANGGDTGLRGTGNVESAVGSCDNKNNFQGAATGDNGRCHLNSLDRSRCKKDFVTSNIIDVDNMVPKRRKDQPEDPTRRKTFGRVPGYIGRVKEVIEKERMQLKAIGEARTNNRLERVGKFVYRLDEQERLNMISKLRAKLTEKGAELNRMPFAKDTYIQMKRKSDLEKRIKEIESSLEKLEKDAVFIYSDDPRVVHWTKDAAFEEARLFASD
Protein: Kelch-like protein 5 (Q96PQ7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Cullin-3
Sequence:
MNVIYFPLHIFVVYSRAYTSLVLVGCTNLCAVLFARCLDDHLVSLRMSGSRKEFDVKQILKIRWRWFGHQASSPNSTVDSQQGEFWNRGQTGANGGRKFLDPCSLQLPLASIGYRRSSQLDFQNSPSWPMASTSEVPAFEFTAEDCGGAHWLDRPEVDDGTSEEENESDSSSCRTSNSSQTLSSCHTMEPCTSDEFFQALNHAEQTFKKMENYLRHKQLCDVILVAGDRRIPAHRLVLSSVSDYFAAMFTNDVREARQEEIKMEGVEPNSLWSLIQYAYTGRLELKEDNIECLLSTACLLQLSQVVEACCKFLMKQLHPSNCLGIRSFADAQGCTDLHKVAHNYTMEHFMEVIRNQEFVLLPASEIAKLLASDDMNIPNEETILNALLTWVRHDLEQRRKDLSKLLAYIRLPLLAPQFLADMENNVLFRDDIECQKLIMEAMKYHLLPERRPMLQSPRTKPRKSTVGTLFAVGGMDSTKGATSIEKYDLRTNMWTPVANMNGRRLQFGVAVLDDKLYVVGGRDGLKTLNTVECYNPKTKTWSVMPPMSTHRHGLGVAVLEGPMYAVGGHDGWSYLNTVERWDPQARQWNFVATMSTPRSTVGVAVLSGKLYAVGGRDGSSCLKSVECFDPHTNKWTLCAQMSKRRGGVGVTTWNGLLYAIGGHDAPASNLTSRLSDCVERYDPKTDMWTAVASMSISRDAVGVCLLGDKLYAVGGYDGQAYLNTVEAYDPQTNEWTQVAPLCLGRAGACVVTVKL
Protein: Vacuolar protein sorting-associated protein 36 (AtVPS36) (ESCRT-II complex subunit VPS36) (Q9FF81)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex (By similarity).
Subcellular location: Endosome {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 28 homolog 2
- Vacuolar protein sorting-associated protein 22 homolog 1
- Vacuolar protein sorting-associated protein 28 homolog 1
- Protein ELC-like
- Vacuolar protein sorting-associated protein 20 homolog 2
- Protein ELC
- Vacuolar protein sorting-associated protein 32 homolog 2
- Vacuolar protein sorting-associated protein 32 homolog 1
- Putative vacuolar protein sorting-associated protein 22 homolog 2
- Vacuolar protein sorting-associated protein 20 homolog 1
Sequence:
MASGSSSIAIGGLFENAEVTTSGRPVLRRNEVECFLLSSIDIDSEDDPPRFTALRSGNLILTTHRLIWIPSQSNESVPSSIPLSAVTHIYSHKKSIKSMFHSPRIRFQADPGSIVVTIVFRGKGDFDGFLSKLWECWRGRAWEEEEKSESETSKSGSGTVAQGLYGNDGTVRMVGLAGILRKEQEQWESTDKSLQDAFQDLNALMSKAKEMVSLAEKMRQKLLSAPSSQNGSTDDEEMGSKEEMQQWMLSVGIISPVTKESAGALYHQELSRQLADFVRIPLEKAGGMISLTDMYYHFNRARGTELISPDDLWQACTLWEKFDVPVMLRKFDSGVMVIQNKSHSDEEVMSRIRMLVTKTETLRVGVTASDAALTLKIAPAMAKEHLLSAETKGLLCRDMSPDGLRFYFNLFPEIDPTNLHIVKEFGTYGEWIKATSLLSV
Protein: Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60) (HIP-70) (Q-2) (P11598)
Organism: Rattus norvegicus (Rat)
Function: Disulfide isomerase which catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds (By similarity). Associates with calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (By similarity). Association with calcitriol does not affect its enzymatic activity (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P30101}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:9399589}. Melanosome {ECO:0000250|UniProtKB:P30101}.
Interaction partners:
- Calreticulin
- Calnexin
- TAP binding protein
- Calreticulin
- Calreticulin
- Endoplasmic reticulum chaperone BiP
- Beta-2-microglobulin
- Endoplasmin
- Antigen peptide transporter 2
- Antigen peptide transporter 1
Sequence:
MRFSCLALLPGVALLLASALLASASDVLELTDENFESRVSDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAGAYDGPRTADGIVSHLKKQAGPASVPLRTEDEFKKFISDKDASVVGFFRDLFSDGHSEFLKAASNLRDNYRFAHTNVESLVKEYDDNGEGITIFRPLHLANKFEDKIVAYTEKKMTSGKIKKFIQESIFGLCPHMTEDNKDLIQGKDLLTAYYDVDYEKNTKGSNYWRNRVMMVAKTFLDAGHKLNFAVASRKTFSHELSDFGLESTTGEIPVVAIRTAKGEKFVMQEEFSRDGKALERFLQEYFDGNLKRYLKSEPIPETNEGPVKVVVAESFDDIVNAEDKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVKGFPTIYFSPANKKLTPKKYEGGRELNDFISYLQREATNPPIIQEEKPKKKKKAQEDL
Protein: Pre-mRNA-splicing factor prp1 (Q12381)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in pre-mRNA splicing. Interacts with prp6 and prp13. May also be involved in the regulation of the G0-G1/G2 transition. Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U5. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pre-mRNA-splicing factor sap62
- U4/U6.U5 tri-snRNP-associated protein snu66
- U4/U5/U6 small nuclear ribonucleoprotein prp3
- U2 snRNP component prp10
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein Sm D3
- Pre-mRNA-splicing factor spp42
- Mitosis protein dim1
- Pre-mRNA-processing factor 31
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MANFYPDFLNMQPPPNYVAGLGRGATGFTTRSDLGPAQELPSQESIKAAIEQRKSEIEEEEDIDPRYQDPDNEVALFATAPYDHEDEEADKIYQSVEEHLSKRRKSQREKQEQLQKEKYEKENPKVSSQFADLKRGLSTLTDEDWNNIPEPGDLTRKKRTKQPRRERFYATSDFVLASARNENQAISNFAVDTQAGTETPDMNGTKTNFVEIGAARDKVLGIKLAQASSNLTSPSTIDPKGYLTSLNSMVPKNANDLGDIRKARKLLQSVIETNPKHASGWVAAARLEEVANKLSQAQSLILKGCENCSRSEDVWLEAIRLHPAAEAKVIIANAVKKLPKSVTLWLEAEKLENQAQHKKRIIKKALEFNPTSVSLWKEAVNLEEEVDNARILLARAVELIPMSIDLWLALARLETYENAKKVLNKARQTIRTSHEVWIAAARLEEQQGNVSRVEKIMARGVSELQATGGMLQRDQWLSEAEKCETEGAVITAQAIINTCLGVGLDEEDQFDTWLDDAQSFIARKCIDCARAVFAFSLRVYPKSEKLWLRAVELEKLYGTTESVCSILEKAVESCPKAEILWLLYAKERKNVNDIAGARNILGRAFEYNSNSEEIWLAAVRIEFVNNENERARKLLARARIESGTERIWTKSISLERILDEKDRALQLLENALKIYPHYDKLYMMKGQIFEDKEQIELARDAYLAGTKVCPYSIPLWLLLAKLEEKQSVIRARVVFDRAKVKNPKNEFLWLELIKMELRAGNISQVRAALAKALQECPSSGLLWTEAIWLEPRAQRKTRATDALRKCEGNAHLLCTIARMLWLEKKADKARSWFLKAVKADQDNGDVWCWFYKYSLEAGNEDQQKEVLTSFETADPHHGYFWPSITKDIKNSRKTPQELLHLAINVL
Protein: Translationally controlled tumor protein (TCTP), putative (Q57TT8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GST N-terminal domain-containing protein
- 60S acidic ribosomal protein P0
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S8
- Translation elongation factor 1-beta, putative
- Translation elongation factor 1-beta, putative
- Translation elongation factor 1-beta, putative
- 60S ribosomal subunit protein L31, putative
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S4
Sequence:
MKIFRDILTNAEVVCDNDKPMDLLDEIVYAVQGRYIEIGGEDYGISANADEDAGEGAAGDVDDGKQRVIDVVHNNRYTETNYDKGSYMAHIRGYMKQLLEKIEDEGAKKAFQTNAAAFVKKVIKEIDEYQFFIPEGNEEDPDNGMIVLCKWDGETPTFYFWKDGLKGERV
Protein: Cytochrome P450 27C1 (EC 1.14.19.53) (All-trans retinol 3,4-desaturase) (Q4G0S4)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase that catalyzes the 3,4 desaturation of all-trans-retinol (also called vitamin A1) to all-trans-3,4-didehydroretinol (also called vitamin A2) in the skin. Desaturates with lower efficiency all-trans retinal and all-trans retinoic acid. Forms minor amounts of 3-hydroxy and 4-hydroxy all-trans-retinol derivatives. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin).
Subcellular location: [Isoform 2]: Mitochondrion membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14137}.
Interaction partners:
- Retinol dehydrogenase 10
- Cytochrome P450 26A1
- All-trans-retinol 13,14-reductase
- Short-chain dehydrogenase/reductase 3
- Retinol dehydrogenase 12
- Retinol dehydrogenase 8
- Retinol dehydrogenase 11
- Dehydrogenase/reductase SDR family member 9
- Lecithin retinol acyltransferase
- Dehydrogenase/reductase SDR family member 4
Sequence:
MQTSAMALLARILRAGLRPAPERGGLLGGGAPRRPQPAGARLPAGARAEDKGAGRPGSPPGGGRAEGPRSLAAMPGPRTLANLAEFFCRDGFSRIHEIQQKHTREYGKIFKSHFGPQFVVSIADRDMVAQVLRAEGAAPQRANMESWREYRDLRGRATGLISAEGEQWLKMRSVLRQRILKPKDVAIYSGEVNQVIADLIKRIYLLRSQAEDGETVTNVNDLFFKYSMEGVATILYESRLGCLENSIPQLTVEYIEALELMFSMFKTSMYAGAIPRWLRPFIPKPWREFCRSWDGLFKFSQIHVDNKLRDIQYQMDRGRRVSGGLLTYLFLSQALTLQEIYANVTEMLLAGVDTTSFTLSWTVYLLARHPEVQQTVYREIVKNLGERHVPTAADVPKVPLVRALLKETLRLFPVLPGNGRVTQEDLVIGGYLIPKGTQLALCHYATSYQDENFPRAKEFRPERWLRKGDLDRVDNFGSIPFGHGVRSCIGRRIAELEIHLVVIQLLQHFEIKTSSQTNAVHAKTHGLLTPGGPIHVRFVNRK
Protein: Protein farnesyltransferase subunit beta (FTase-beta) (PFTase beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Ras proteins prenyltransferase subunit beta) (P22007)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X where X is Ser, Ala, Met, Cys, or Gln. Required for the membrane localization of proteins such as a-factor, Ras proteins and other membrane proteins containing the C-terminal CAAX motif. The beta subunit is responsible for isoprenoid and peptide-binding.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- CAAX prenyl protease 2
- CAAX prenyl protease 1
- Farnesyl pyrophosphate synthase
- Geranylgeranyl pyrophosphate synthase BTS1
- Hexaprenyl pyrophosphate synthase, mitochondrial
- Dehydrodolichyl diphosphate synthase complex subunit SRT1-farnesyl diphosphate specific))
- Protein-S-isoprenylcysteine O-methyltransferase
- Dehydrodolichyl diphosphate synthase complex subunit RER2
- Dehydrodolichyl diphosphate synthase complex subunit NUS1
Sequence:
MRQRVGRSIARAKFINTALLGRKRPVMERVVDIAHVDSSKAIQPLMKELETDTTEARYKVLQSVLEIYDDEKNIEPALTKEFHKMYLDVAFEISLPPQMTALDASQPWMLYWIANSLKVMDRDWLSDDTKRKIVDKLFTISPSGGPFGGGPGQLSHLASTYAAINALSLCDNIDGCWDRIDRKGIYQWLISLKEPNGGFKTCLEVGEVDTRGIYCALSIATLLNILTEELTEGVLNYLKNCQNYEGGFGSCPHVDEAHGGYTFCATASLAILRSMDQINVEKLLEWSSARQLQEERGFCGRSNKLVDGCYSFWVGGSAAILEAFGYGQCFNKHALRDYILYCCQEKEQPGLRDKPGAHSDFYHTNYCLLGLAVAESSYSCTPNDSPHNIKCTPDRLIGSSKLTDVNPVYGLPIENVRKIIHYFKSNLSSPS
Protein: Formyl peptide receptor-related sequence 1 (FMLP-related receptor I) (FMLP-R-I) (Formyl peptide receptor related sequence 1) (Formyl peptide receptor-like 1) (Lipoxin A4 receptor) (LXA4 receptor) (N-formyl peptide receptor 2) (N-formyl peptide receptor 3) (O08790)
Organism: Mus musculus (Mouse)
Function: Low affinity receptor for N-formyl-methionyl peptides. Receptor for lipoxin A4. May have an olfactory function associated with the identification of pathogens or of pathogenic states.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Annexin A1
- Amyloid-beta precursor protein
- Heme-binding protein 1
- Polyunsaturated fatty acid lipoxygenase ALOX15
Sequence:
METNYSIPLNGSDVVIYDSTISRVLWILSMVVVSITFFLGVLGNGLVIWVAGFRMPHTVTTIWYLNLALADFSFTATLPFLLVEMAMKEKWPFGWFLCKLVHIAVDVNLFGSVFLIAVIALDRCICVLHPVWAQNHRTVSLARNVVVGSWIFALILTLPLFLFLTTVRDARGDVHCRLSFVSWGNSVEERLNTAITFVTTRGIIRFIVSFSLPMSFVAICYGLITTKIHKKAFVNSSRPFRVLTGVVASFFICWFPFQLVALLGTVWLKEMQFSGSYKIIGRLVNPTSSLAFFNSCLNPILYVFMGQDFQERLIHSLSSRLQRALSEDSGHISDTRTNLASLPEDIEIKAI
Protein: DNA-directed RNA polymerase subunit (EC 2.7.7.6) (A8JUY3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA-directed RNA polymerases I and III subunit RPAC1
- FI04119p
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase III subunit RPC6
Sequence:
MPKEQFRASALNKKISHVQFGISGADEIQQEALVRIISKNLYQAQRQPVPYGVLDRRMGISTKDAMCETCGQGLNECIGHFGYLDLALPVFHIGHFRSTINILQMICKVCAHVMLKPEDRQLYEKKLHNPNFSYLGKKALHVQMLAKAKKVTKCPHCGSPNGGVKKGPGLLKILHDPYKGRKMDSLFTSNMNEMLRSTQTNRDLNSTLGNYSTAEELTPLMVLDLFEQIPQRDVALLGMCSHDAHPKHLIVTRVFVPPACIRPSVLSEVKAGTTEDDLTMKQSEILLINDVIQRHMATGGKIELIHEDWDFLQLHVALYFHSEISGIPINMAPKKTTRGIVQRLKGKQGRFRCNLSGKRVDFSGRTVISPDPNLMINQVGVPVRVAKILTYPERVNPANIRHMRELVRNGPSMHPGANYVQQRGSSFKKYLAYGNREKVAQELKCGDVVERHLRDGDIVLFNRQPSLHKMSIMCHRAKVQPQRTFRFNECACTPYNADFDGDEMNLHLPQTEEARAEALILMGNQSNLVTPKNGEILIAATQDFITGGYLLTQKEVFLTKEEAMQLAACFLANEDSTMHIKLPPPALLKPRRLWTGKQMFSLLMRPNDDSQVRLNMVNKGRNYTRNKDLCSNDSWIHIRNSELMCGVMDKATMGSGTKQCIFYLLLRDFGESHATKAMWRLARIASYFLQNRGFSFGISDVTPSKKLLQHKELLLNNGYAKCNEYIELLKAGTLQCQPGCTPEETLESVMLRELSAIREQAAKTCFAELHPTNSALIMALSGSKGSNINISQMIACVGQQAISGKRVPNGFENRALPHFERHSAIPAARGFVQNSFYSGLTPTEFFFHTMAGREGLVDTAVKTAETGYLQRRLVKCLEDLVVHYDGTVRNAVNEMVDTIYGGDGLDPVSMETRNKPVDLVHQYDNLRAQHPQGKDRPLNAEEMSEALETLLRTPEFAEARDDFKLDVRNHINTVSKRIGQLQKRYEKCIDLCHQIECLTTEQLLQFVRRINDRYNRAVTEPGTAVGAIAAQSIGEPGTQMTLKTFHFAGVASMNITQGVPRIVEIINATKTISTPIITAELENCHSMEFARQVKARIEKTTLAELSSYVEVVCGPYSCYLAIGVDMARIKLLGLHIDLDTIVFSILKSRMRVKPTQVEVVASQSRIVVRVEATRTSTINAELARLALSLQNVVVAGLPNINRAVIAVDDARQPPTYKLCIEGYGLRDVIATYGVVGKRTRSNNICEIYQTLGIEAARTIIMSEITEVMEGHGMSVDWRHIMLLASQMTARGEVLGITRHGLAKMRESVFNLASFEKTADHLFDAAYYGQTDAINGVSERIILGMPACIGTGIFKLLQQHEDKQVPPIEPTICSSLNLLPSKTT
Protein: Polyadenylate-binding protein (Q08212)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDESQPKTLYVGNLDSSVSEDLLIALFSTMGPVKSCKIIREPGNDPYAFIEYSNYQAATTALTAMNKRLFLEKEIKVNWATSPGNQPKTDISSHHHIFVGDLSPEIETETLREAFAPFGEISNCRIVRDPHTMKSKGYAFVSFVKKAEAENAIQAMNRQWIASRSIRTNWSTRKLPPPREPSKGGGQGGGMGGGPGNGSGVKGSQRHTFEEVYNQSSPTNTTVYCGGFPPNVISDDLMHKHFVQFGPIQDVRVFKDKGFSFIKFVTKEAAAHAIEHTHNSEVHGNLVKCFWGKENGGDNSANNLNAAAAAAAASANVAAAVAANAAVAAGAGMPGQMMTQQQIAAATGAAIPGQMMTPQQIAAQYPYAYQQMGYWYPPATYPTTQMQTQYMQQGYYPYAYPTSAQQAGGVPAGYRMVPPNVAWGVPGTVVPGVTAAAASAAAAAANGSLPPQMMYSAAMPQYQTQ
Protein: Annexin A13 (Annexin XIII) (Annexin-13) (Intestine-specific annexin) (ISA) (P27216)
Organism: Homo sapiens (Human)
Function: Binds to membranes enriched in phosphatidylserine or phosphatidylglycerol in a calcium-dependent manner. Half-maximal membrane binding requires about 60 uM calcium. Does not bind to membranes that lack phospholipids with an acidic headgroup.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:1530946}. Cell membrane {ECO:0000269|PubMed:30610115}; Lipid-anchor {ECO:0000269|PubMed:30610115}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99JG3}. Note=Myristoylation anchors the protein to the membrane, but the protein also displays calcium-dependent, reversible binding to lipid membranes (PubMed:30610115). Associated with the plasma membrane of undifferentiated, proliferating crypt epithelial cells as well as differentiated villus enterocytes (PubMed:1530946). {ECO:0000269|PubMed:1530946, ECO:0000269|PubMed:30610115}.
Interaction partners:
- CUB and sushi domain-containing protein 3
- Exostosin-1
- Zinc finger transcription factor Trps1
Sequence:
MGNRHAKASSPQGFDVDRDAKKLNKACKGMGTNEAAIIEILSGRTSDERQQIKQKYKATYGKELEEVLKSELSGNFEKTALALLDRPSEYAARQLQKAMKGLGTDESVLIEVLCTRTNKEIIAIKEAYQRLFDRSLESDVKGDTSGNLKKILVSLLQANRNEGDDVDKDLAGQDAKDLYDAGEGRWGTDELAFNEVLAKRSYKQLRATFQAYQILIGKDIEEAIEEETSGDLQKAYLTLVRCAQDCEDYFAERLYKSMKGAGTDEETLIRIVVTRAEVDLQGIKAKFQEKYQKSLSDMVRSDTSGDFRKLLVALLH
Protein: APC regulator of WNT signaling pathway 2 (A0A0G2JZW4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Axin-2
- Catenin beta-1
- Rho guanine nucleotide exchange factor 4
- Glycogen synthase kinase-3 beta
- Spermatogenesis associated 13
- Segment polarity protein dishevelled homolog DVL-1
- Dishevelled segment polarity protein 2
- Junction plakoglobin
- Dishevelled segment polarity protein 3
- Lymphoid enhancer-binding factor 1
Sequence:
MASSVASYEQLVRQVEALKAENTHLRQELRDNSSHLSKLETETSGMKEVLKHLQGKLEQEARVLVSSGQTEVLEQLKALQTDISSLYNLKFHAPALGPEPAAQTPEGSPVHGPAPSKDSFGELSRATIRLLEELDQERCFLLSEIEKEEKEKLWYYSQLQGLSKRLDELPHVDTQFSMQMDLIRQQLEFEAQHIRSLMEERFGTSDEMVQRAQIRASRLEQIDKELLEAQDRVQQTEPQALLAVKPVAVEEQEAEVPTHPEDVTPQPGNSKVEVVFWLLSMLATRDQEDTARTLLAMSSSPESCVAMRRSGCLPLLLQILHGTEAGSVGRTGTPGAPGAKDARMRANAALHNIVFSQPDQGLARKEMRVLHVLEQIRAYCETCWDWLQARDSGTESGTGDTPVPIEPQICQAACAVMKLSFDEEYRRAMNELGGLQAVAELLQVDYEMHKMTQDPLNLALRRYAGMTLTNLTFGDVANKATLCARRGCMEAIVAQLASESEELHQVVSSILRNLSWRADINSKKVLREVGSMTALMECVLRASKESTLKSVLSALWNLSAHSTENKAAICQVDGALGFLVSTLTYRCQGNSLAVIESGGGILRNVSSLIATREDYRQVLRDHNCLQTLLQHLTSHSLTIVSNACGTLWNLSARSPRDQELLWDLGAVGMLRNLVHSKHKMIAMGSAAALRNLLAHRPAKYQAAAMAVSPGTCVPSLYVRKQRALEAELDTRHLVHALGHLEKQGLPEAETTSKKPLPPLRHLDGLVQDYASDSGCFDDDDAPSLAAAATTAEPASPAVMSMFLGGPFLQGQALARTPPARQGGLEAEKETGGEAAVAAKAKAKLALAVARIDRLVEDISALHTSSDDSFSLSSGDPGQEAPREGRAQSCSPCRGTEGGRREAGSRAHPLLRLKAAHTSLSNDSLNSGSTSDGYCTREHMTPCPLAVLTEHRDGPVCGQTRPSRLDLDLPSRAELPARDTAATDARVRTIKLSPTYQHVPLLDGAPGAGVRPLVGLGTSPGTRKQAWIPADSLSKVPEKLVASPLPVTSKVLQKLVAQDGPMSLSRCSSLSSLSSTGHAVPSQVENLDDSDSSLEELEEAGPGEAELDRAWRASGSTSLPVSIPAPQRGRSRGLGVEDATPSSSSENCVQETPLVLSRCSSVSSLGSFESRSIASSIPSDPCSALGSGTVSPSELPDSPGQTMPPSRSRTPPAPPGQPEASQFSLQWESYVKRFLDIADCRERCQPPSELDAGSVRFTVEKPDENFSCASSLSALALHELYVQQDVELRLRPPACPERAVGGGGGHRRRDEATSRLDGPAPAGSRARSAADKELEALRECLGAAMPARLRKVASALVPGRRALPVPVYMLVPAPARGDDSGTDSAEGTPVNFSSAASLSDETLQGPSRDKPARPGDRQKPTGRAAPARQTRGHRPKAAGAGAGKSTEHTRGANRNRAGLELPLSRPQSARSNRDGSCQTRTRGDGALQSLCLTTPTEEAVYCFYDSDEEPPATAPPTRRASAIPRALKREKPAGRKETPTRATQPATLPVRAQPRLIVDETPPCYSLTSSASSLSEPEASEQPACHPRVEEQGSKQDSSPRAEEELLQRCISLAMPRRRTQVPSSRRRKPRAVRSDIRPTELPQKCREEVPGSDPASDLDSVEWQAIQEGANSIVTWLHQAAAKASLEASSESDSLLSLVSGLSASSTLQPSKLRKGRKPVAEAGGAWRPEKRGTTSTKGSGSPRFPSGPEKAKGTQKTMAGESAMLRGRTVIYTASPASRAQSKGISGPCSAPKKMGTSGTTQPETATKTPSPEQQRSRSLHRPGKISELAALSHPPRSATPPARLTKTPSSSSSQTSPASQSLPRRSPLATPTGGPLPGPGGSPVPKSPARALLAKQHKTQKSPVRIPFMQRPARRVPPPLARPSPEPGSRGRAGAEGTPGARGSRLGLVRVASTRSSGSESSDRSGFRRQLTFIKESPGLLRRRRSELSSADSTVSTSQTASPCRGRPALPAVFLCSSRCDELRASPRQPLAAQRVPQAKPGLAPRAPRRTSSESPSRLPVRATPGRPETVKRYASLPHISVSRRPDSAVSVPTTQANATRRGSDGEARPLPRVAAPGTTWRRIKDEDVPHILRSTLPATALPLRGSSPEDSPAGTPHRKTSDAVVQTEDVATSKTNSSTSPSLESRDPPQAPISGPVAPLGSDVDGPVLAKPPASAPFTHEGLSVVTGGFPTSRHGSPSRAARVPPFNYVPSPMVVATMTSDSAVEKAPVTSPASLLE
Protein: 25S rRNA (adenine(645)-N(1))-methyltransferase (EC 2.1.1.287) (Ribosomal RNA-processing protein 8) (Q10257)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine in helix 25.1 in 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis. Required for efficient pre-rRNA cleavage at site A2 (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 18S rRNA
- Probable nucleolar GTP-binding protein 1
- Importin subunit beta-1
- 25S rRNA
- 25S rRNA
- Ribosome production factor 2 homolog
- rRNA biogenesis protein rrp5
- Uncharacterized RNA-binding protein C4F6.14
- Uncharacterized RNA-binding protein C1827.05c
- KRR1 small subunit processome component homolog
Sequence:
MFKVDWDLGPVSKSASDQTKESRKEKKRKKGERKNVGDKGEKLNEKVLKKAKSVTTNNSLKSEIKKEKSVPSIKEKNKGDAKHTKLTSLQQKMKDKLDGANFRWINEQLYTTESDKAVQMFKENPDLFDIYHAGFRYQVEGWPENPVDIFIQHLKIRFEHSNAKKKNNIVIADLGCGEAKIASTFRKSRSLQVHSFDLVAPNEHVVACDIANVPMADETVDIAVFCLSLMGTNWQSFLKEAYRILKVGGLLWVAEIKSRFSDKSGEVFAKELPKLGFETKSIQLQNKMFTLFEFKKVPVHGKCEELPPILSACIYKRR
Protein: DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.-.-) (Q57X31)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Endonuclease III homolog lyase)
- Protein artemis
- Proliferating cell nuclear antigen
- DNA-
- Flap endonuclease 1
- Adenine DNA glycosylase
- Uracil-DNA glycosylase
- Sm protein F
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MPPKKLSKLPLNTRMKRSRSRSPSATLPSKETKETDRSKAQSPVRSVSLPVGSGSASPVRGDDLKKTEKSIWSQVEPFKRKTEAKDFKPREMLKFITWNVAGLRGLLKKDSEAIKKLLEEEHPDALCLQETKLNVGDKGNEALGVVQGYDFVDHPCHAKKGYSGTRTYIKKEVAEKWNAVFVKGFGGPNGVDDDKQENGDDEGRVLTTYFGGDQGCENTFRLALVNTYVPNSGMDLARLPYRHKTFDVKMRNYLCKLDAAAMKVNGTCNNVKDAQPPTGVIWAGDLNVAERDYDRYFAGTFAAMQKCSGFTPEERTSFRETLRAVNAVDTFRELYPRAAPVYTFWSARINGRARGLGWRLDYFVVSAALAGRVVDCFTMPMIMGSDHCPVQMWLRK
Protein: Small COPII coat GTPase SAR1B (EC 3.6.5.2) (GTP-binding protein SAR1B) (Q01474)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in transport from the endoplasmic reticulum to the Golgi apparatus.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y6B6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9QVY3}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9QVY3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9QVY3}. Note=Active at endoplasmic reticulum exit sites (ERES) where it inserts into the membrane and recruits the remainder of the coat protein complex II/COPII. {ECO:0000250|UniProtKB:Q9Y6B6}.
Interaction partners:
- SEC12-like protein 2
- Protein transport protein SEC13 homolog B
- Protein transport protein SEC31 homolog A
- SEC12-like protein
- Protein transport protein SEC31 homolog B
- Protein transport protein SEC24 A
- SEC12-like protein 1
- Protein transport protein SEC13 homolog A
- Protein transport protein SEC23 B
- Protein transport protein SEC23 D
Sequence:
MFLFDWFYGILASLGLWQKEAKILFLGLDNAGKTTLLHMLKDERLVQHQPTQHPTSEELSIGKIKFKAFDLGGHQIARRVWKDYYAKVDAVVYLVDAYDKERFAESKRELDALLSDEALATVPFLILGNKIDIPYAASEDELRYHLGLTNFTTGKGKVTLGDSGVRPLEVFMCSIVRKMGYGEGFKWLSQYIN
Protein: F-box only protein 15 (Q8NCQ5)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Interaction partners:
- S-phase kinase-associated protein 1
- Homeobox protein NANOG
- Krueppel-like factor 4
- POU domain, class 5, transcription factor 1
- Transcription factor SOX-2
- Protein lin-28 homolog A
- Cullin-1
Sequence:
MATGRGRILQQHWLGLQTLRGPSRGGGAARGRARAFGCRKGPGVKLSAGSAALRCHAGGGQHWESSFSCCSGFLDGMPSEILLKIFSYLDAVSLLCTGCVSRRFYHLANDNFIWIGIYSTAFSPARSNWKFNSVEKIAMSMSFLSVQDKEAGYWKKEYITKQIASVKAALADILKPVNPYTGLPVKTKEALRIFGLGWAIILKEKGGKEYIMEHVDLSINDTSVTVIWYGKKWPCLASLSTLDLCGMTPVFTDWYKTPTKHRLRWHSLIAKYNLSHLTISTMIGCDRLIRIFCLHPGLLVGVWKKEEELAFVMANLHFHHLVERSTLGSATIPYELPPHSPFLDDSPEYGLHGYQLHVDLHSGGVFYLCGTFRNLFTKRGNIENGHVKLIVIHLKNNREHLPLIGKVGLSWKTDIFDGCIKSCSMMDVTLLDEHGKPFWCFSSPVCLRSPATPSDSSSFLGQTYNVDYVDAEGRVHVELVWIRETEEYLIVNLVLYLSIAKINHWFGTEY