wanglab/gogpt-training-data huggingface dataset:
Protein: Aryl-alcohol dehydrogenase [NADP(+)] (AAD) (EC 1.1.1.91) (Q01752)
Organism: Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum)
Interaction partners:
Sequence:
MNIWAPAPEPPTKLGRHRQLAPGCGLHVSPIQLGAMSIGDKWHPYGMGTMDKEASFKLLDAFYNAGGNFIDTANVYQDETSEEFIGEWMEARGNRDQMVVATKYSLVYKRGASFEEIPQKTQYVGNSLKSMHISVHDSLRKLRTSYIDIFYVHFWDYTCTIEEVMNGLHNLVAQGKVLYLGVSDTPAWVVSKANNYARMAGKTPFVIYEGEWNITMRDMERDIIPMCIHEGMAIAPWNVLCAGKIRTDAEEERRLKSGEGGRTLLQFDGWLRNETERKVSKALEKVAEEIGAKSITSVAIAYLMQKFPYVFPIVGGRKVEHLYANLEALDISLSPEQMQFLNDTVPFNKGFPYLLFGDGSDYNIVHKAAGHYDKWPAQQAIRPQK
Protein: tRNA methyltransferase 10 homolog A (EC 2.1.1.221) (RNA (guanine-9-)-methyltransferase domain-containing protein 2) (tRNA (guanine(9)-N(1))-methyltransferase TRMT10A) (Q8C1Z8)
Organism: Mus musculus (Mouse)
Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in tRNAs. Probably not able to catalyze formation of N(1)-methyladenine at position 9 (m1A9) in tRNAs.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8TBZ6}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8TBZ6}.
Interaction partners:
- tRNA
Sequence:
MSSEMLPASIESPNVEEKLGTSDGEEERQEPRVDAGAEPISKRQLKKLMKQKQWEEQREQRKEKRKEKRKRKKLERRQLESNSDGNDRKRVRRDVARSSLRLVIDCSFDDLMVLKDIKKLHKQIQRCYAENRRASHPVQFYLTSHGGQLKKNMDENDQGWVNWKDIHIKSEHYSELIKKEDLVYLTSDSPNVLKDLDESKAYVIGGLVDHSHHKGLTFKQATSYGIEHAQLPLADFVKMNSRKVLAVNHVFEIILEFLETRDWQEAFFTILPQRKGAVPAHKACESSPQDHQSLPEGWDSASEGESCRDNPDSPQKDEQGQQSSPVLQ
Protein: Lamin-B2 (Q03252)
Organism: Homo sapiens (Human)
Function: Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin.
Subcellular location: Nucleus lamina {ECO:0000305|PubMed:33033404}.
Interaction partners:
- Lamin-B1
- Delta
- Prelamin-A/C
- Caspase-6
- Granzyme B
- Emerin
- Mitochondrial import inner membrane translocase subunit Tim13
- SUN domain-containing protein 1
- Barrier-to-autointegration factor
- Inner nuclear membrane protein Man1
Sequence:
MSPPSPGRRREQRRPRAAATMATPLPGRAGGPATPLSPTRLSRLQEKEELRELNDRLAHYIDRVRALELENDRLLLKISEKEEVTTREVSGIKALYESELADARRVLDETARERARLQIEIGKLRAELDEVNKSAKKREGELTVAQGRVKDLESLFHRSEVELAAALSDKRGLESDVAELRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEELDFRKSVFEEEVRETRRRHERRLVEVDSSRQQEYDFKMAQALEELRSQHDEQVRLYKLELEQTYQAKLDSAKLSSDQNDKAASAAREELKEARMRLESLSYQLSGLQKQASAAEDRIRELEEAMAGERDKFRKMLDAKEQEMTEMRDVMQQQLAEYQELLDVKLALDMEINAYRKLLEGEEERLKLSPSPSSRVTVSRATSSSSGSLSATGRLGRSKRKRLEVEEPLGSGPSVLGTGTGGSGGFHLAQQASASGSVSIEEIDLEGKFVQLKNNSDKDQSLGNWRIKRQVLEGEEIAYKFTPKYILRAGQMVTVWAAGAGVAHSPPSTLVWKGQSSWGTGESFRTVLVNADGEEVAMRTVKKSSVMRENENGEEEEEEAEFGEEDLFHQQGDPRTTSRGCYVM
Protein: mRNA export factor ICP27 homolog (52 kDa immediate-early phosphoprotein) (EB2 protein homolog) (P13199)
Organism: Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri)
Function: Probably acts as a viral splicing factor that regulates viral RNA splicing. Functions as a multifunctional regulator of the expression of viral lytic genes (By similarity). Early protein that promotes the accumulation and nuclear export of viral intronless RNA transcripts by interacting with mRNAs and cellular export proteins.
Subcellular location: Host cytoplasm {ECO:0000250}. Host nucleus {ECO:0000269|PubMed:21253573}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}.
Interaction partners:
Sequence:
MEDIIEGGISSDDDFDSSDSSSDEEESDTSPQIMKSDVTMASPPSTPEPSPDVSASTSNLKRERQRSPITWEHQSPLSRVYRSPSPMRFGKRPRISSNSTSRSCKTSWADRVREAAAQRRPSRPFRKPYSHPRNGPLRNGPPRAPPLLKLFDISILPKSGEPKLFLPVPSLPCQEAEKTNDKYVLAMAQRAMHDVPISSKQLTANLLPVKFKPLLSIVRYTPNYYYWVSMRKETIASANLCTVAAFLDESLCWGQQYLKNDFIFSENGKDIILDTSSALLSQLVHKIKMLPFCHCLMQTTPQDHIVKQVCYLIASNNRILDAVRYLQTSVIKSPIVLLLAYAVCLPAAIICTKNETQLYSHCMRILKEYRPGDVMNILHESLTQHLNKCPSSTCAYTTRAIVGTKANTTGLFFLPTQ
Protein: GTP-binding protein Rit1 (EC 3.6.5.2) (Ras-like without CAAX 1) (Si:ch211-93a2.3) (B3DJU3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MESSRSTVGHSREYKLVMLGEGGVGKSAIIMQFISHRFPEDHDPTIEDAYKTQIRIDDEPANLDILDTAGQAEFTAMRDQYMRAGEGFIISYSITDRRSFQEARHFKQLIYRVRRTVDTPVVLVGNKSDLVHLRQVSVEEGKQLAREFQCPFFETSAAFRYYIDEVFAALVRQIRQHEAEMVRDSERKTRRSHSFWSRLKAPFHRKQQSEH
Protein: Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase PHS1) (HACD) (PTPLA homolog involved in sphingolipid biosynthesis protein 1) (P40857)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18272525}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase
- Very-long-chain enoyl-CoA reductase
- Fatty acid elongase 2
- Fatty acid elongase 1
- Fatty acid elongase 3
- Acyl-CoA desaturase 1
- Sphingosine-1-phosphate lyase
- Sphingoid long chain base kinase 4
Sequence:
MSKKLASPLSFLPLYNLLSAVGWSYLLYLVISLYPKVGQPAFFYQTKNVATLVQCGAIIEIINSFLGVVRSPLLTTVAQVSSRLLVVLGIFQLLPNTSGVQSVVYISLLLAWSITEIVRYLYYFFMLVFKNGAPKILILLRYNLFWILYPTGVASELRIIYCALNAAESQYSLLYKRILIAAMLAYIPGFPMLFLHMVAQRKKVMKSLRSSFGKKLI
Protein: LD22957p (Q9VXM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MADIMDLLCSEIIVYESDPSLYRLNKRQQQMSSPAIIRDQSSICSSLGDAESDSHPDAQNNAVVCNMKELVYIYASVDSAAKNPEQLEPPPPPPPPPPPPPTATQSIQSYPRYISQEPPTSHCQRLDERLTTTADPPATDNVNTAIGDPTLYSDRCLENFLKVEEKHHKIPDTYFSIQKDITPPMRKIVAEWMMEVCAEENCQEEVVLLALNYMDRFLSSKSVRKTQLQILAAACLLLASKLREPSCRALSVDLLVVYTDNSIYKDDLIKWELYVLSRLGWDLSSVTPLDFLELLMMRLPIGSKNFPDINIGKVRGHAQAFISLAAKEHKFAKFSASTIAASSIAASMNGLKWHLRSGHNLHFLLSLMTDLTSVEQAQVRDCMLHMEDIFKEHSRNLEPFLVNIDPKEMSTLYYKRRFQIHQSQHLSQISIRPLPLPKAPAECVEQHQQQHNFGSAAPHRTHTCKMQAQAQAQNEIQDVTF
Protein: Zn(2)-C6 fungal-type domain-containing protein (G5EAX1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MDPADTIDAFASDADGAALNIPPLPVAQLSASDADRESDVSIKKRKRVRTGCFTCRDRHLKCDEALGQCQNCRKSGRLCRRGVRLNFVDTQVVAPPTCVTPPAGTGVTFRDDSRIIASEYVGGFERYPPPEQDAPVEDVRQTSIPVQPGINPFLNTQYQISRHGCLDDPTELSLLQVFVNQIGPWMDIVDEAKHFTRILPLYAVEQPLLRAVMAACVELYVSIHLFKEASERMRHYDAAALMLSECIASPHRDPSLCATAALIIEIAEMLILGPIESGMRIRAGNSARSLIRDCQWTTRTQGLGGTCSWLSILMELFDCIAFRQTVVWDPDTWGIDMGFVVEPSIAGNEEFWMQRIIYICAKVSDLRSSNLKGIGNSTRYAEAQRLEQWSLYNEWCARWLDSIPRSMLPLGNVQPWQRNPQSVFPQVWLLGRSAIVAQMLYHITRIMLLETDPLQQDHLPELQEEQQRHAYSVCGIVSNDKNNGIPVFSAHLLAVAAGYLVDRKAQEEVVAILDQLRRTSGLSTEHIRDKLRETWGWHSHAHQSFPDTVDTSTVSIGIHTSDHGHEFSQVGITDPFTYSLVETHQYLDHHLIYDQSHQSL
Protein: L-rhamnono-gamma-lactonase (EC 3.1.1.65) (A3LZU8)
Organism: Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545) (Yeast) (Pichia stipitis)
Function: Hydrolase with high substrate specificity for L-rhamnono-1,4-lactone. Catalyzes the second step in an alternative pathway for rhamnose utilization that does not involve phosphorylated intermediates.
Interaction partners:
- L-rhamnonate dehydratase
- V-type proton ATPase subunit F
- L-rhamnose-1-dehydrogenase
- V-type proton ATPase subunit D
- Vacuolar ATP synthase subunit E
- Vacuolar proton pump subunit B
- V-type proton ATPase subunit C
- V-type proton ATPase subunit H
- Vacuolar ATPase V0 domain subunit c
- V-type proton ATPase subunit
Sequence:
MSKYKILDSHIHLYSLANIPLLHWDEGNPLHGNRRLDEYIENSQSTQFDVEGVVWIECDAKIDLTQGLKGLENPIEEYLYICRNINGKLLPEEGVSTPFKRRLIKAMIPFAPMPLGSAGVEEYVKALKTRNSSEFHLVKGFRYLIQDKPPLTISDPHFVSSFQWLDSNGYVFDLGIDMRSGGLWQFKETLEVFKKVPNLKYIINHLTKPCLDFDPETIDSNPDFLSWKRLVTEMYITTPNSYMKLSGGFSEVEQDVALDVTSTSRHVYPWFKVVYELWGPERTIFASNWPVCAIPAGQNLTEKWFQVCETLFDSIGMDEDTRRKIYYSNAFKAYNI
Protein: Long-chain-fatty-acid--[acyl-carrier-protein] ligase AEE15, chloroplastic (EC 6.2.1.20) (Acyl-[acyl-carrier-protein] synthetase) (Acyl-activating enzyme 15) (Q8W471)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in the activation of fatty acids to acyl-carrier-protein prior to fatty acid elongation in plastids. Acts on medium- to long-chain fatty acids.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Peroxisomal acyl-coenzyme A oxidase 1
- Acyl-coenzyme A oxidase 2, peroxisomal
- Acyl-coenzyme A oxidase 3, peroxisomal
- Acyl-coenzyme A oxidase 4, peroxisomal
- Putative acyl-coenzyme A oxidase At3g06690
- Putative acyl-coenzyme A oxidase 3.2, peroxisomal
Sequence:
MQIRLKPDYSFFIASSSTMASTSSLGPSTLLSYGSPSRQFPDFGFRLISGHESVRIPSFRRFRVHCESKEKEVKPSSPFLESSSFSGDAALRSSEWKAVPDIWRSSAEKYGDRVALVDPYHDPPLKLTYKQLEQEILDFAEGLRVLGVKADEKIALFADNSCRWLVSDQGIMATGAVNVVRGSRSSVEELLQIYRHSESVAIVVDNPEFFNRIAESFTSKASLRFLILLWGEKSSLVTQGMQIPVYSYAEIINQGQESRAKLSASNDTRSYRNQFIDSDDTAAIMYTSGTTGNPKGVMLTHRNLLHQIKHLSKYVPAQAGDKFLSMLPSWHAYERASEYFIFTCGVEQMYTSIRYLKDDLKRYQPNYIVSVPLVYETLYSGIQKQISASSAGRKFLALTLIKVSMAYMEMKRIYEGMCLTKEQKPPMYIVAFVDWLWARVIAALLWPLHMLAKKLIYKKIHSSIGISKAGISGGGSLPIHVDKFFEAIGVILQNGYGLTETSPVVCARTLSCNVLGSAGHPMHGTEFKIVDPETNNVLPPGSKGIIKVRGPQVMKGYYKNPSTTKQVLNESGWFNTGDTGWIAPHHSKGRSRHCGGVIVLEGRAKDTIVLSTGENVEPLEIEEAAMRSRVIEQIVVIGQDRRRLGAIIIPNKEEAQRVDPETSKETLKSLVYQELRKWTSECSFQVGPVLIVDDPFTIDNGLMTPTMKIRRDMVVAKYKEEIDQLYS
Protein: Slc4a9 protein (Q14CH2)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDECKAQSTEDILSVPGLVNASFLPPPECIRQGGHPLGPSCHTVPDIAFFSLLLFFTSFLCAIALKHIKNSRFFPSVVRKVLGDFSSVLAILLGCGLDAFLGLATPKLLVPTEFKPTLSGRGWLVSPFGANPWWLSVAAALPALLLSILIFMDQQITAVILNRAEYRLQKGAGFHLDLFCVAVLMLFTSALGLPWEQRLTGLVVFVLTGVSIFLAPVLKFIPMPVLYGIFLYMGVAALSSIQFVKRVQLLLMPRKHQPDMLLLRHVPLSRVHLFTAIQLACLGLLWVVKSTPAAIVFPLMLLGLVAIRKALEWVFSPQELLWLDELMPEEEETIPENRSEPEHLFSGNDSEDSELMYQPKAPEINISVN
Protein: Insulin-like growth factor-binding protein 5 (IBP-5) (IGF-binding protein 5) (IGFBP-5) (Q05717)
Organism: Bos taurus (Bovine)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P24593}. Cytoplasm {ECO:0000250|UniProtKB:P24593}. Nucleus {ECO:0000250|UniProtKB:P24593}.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Pappalysin 1.
- Pappalysin 2
- Insulin-like growth factor-binding protein complex acid labile subunit
- Insulin-like growth factor-binding protein 3
- Insulin-like growth factor 1 receptor
- Insulin
Sequence:
MVLTAVLLLLAACAGSAQGLGSFVHCEPCDEKALSMCPPSPLGCELVKEPGCGCCMTCALAEGQSCGVYTERCAQGLRCLPRQDEEKPLHALLHGRGVCLNEKSYREQAKIERDSREHEEPTTSEMAEETYSPKIFRPKHTRISELKAEAVKKDRRKKLTQSKFVGGAENTAHPRVISAPEMRQKSEQGPCRRHMEASLQELKASPRMVPRAVYLPNCDRKGFYKRKQCKPSRGRKRGICWCVDKYGMKLPGMEYVDGDFQCHTFDSSNVE
Protein: Peroxisomal biogenesis factor 5 (F5GZ41)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDDLLAEMQQIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVTQDYNETDWSQEFISEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGTATDRWYDEYHPEEDLQHTA
Protein: Protein OS-9 homolog (Q99220)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. The recognition of targets is N-glycan specific. Functions in recruiting misfolded protein substrates in conjunction with HRD3.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12077121, ECO:0000269|PubMed:16168371}; Peripheral membrane protein {ECO:0000269|PubMed:12077121, ECO:0000269|PubMed:16168371}; Lumenal side {ECO:0000269|PubMed:12077121, ECO:0000269|PubMed:16168371}.
Interaction partners:
- ERAD-associated E3 ubiquitin-protein ligase component HRD3
- UBX domain-containing protein 2
- U1 SNP1-associating protein 1
- ERAD-associated E3 ubiquitin-protein ligase HRD1
- Degradation in the endoplasmic reticulum protein 1
- Endoplasmic reticulum chaperone BiP
- DER1-like family member protein 1
- Cell division control protein 48
- ERAD-associated E3 ubiquitin-protein ligase DOA10
- Ubiquitin-conjugating enzyme E2 7
Sequence:
MQAKIIYALSAISALIPLGSSLLAPIEDPIVSNKYLISYIDEDDWSDRILQNQSVMNSGYIVNMGDDLECFIQNASTQLNDVLEDSNEHSNSEKTALLTKTLNQGVKTIFDKLNERCIFYQAGFWIYEYCPGIEFVQFHGRVNTKTGEIVNRDESLVYRLGKPKANVEEREFELLYDDVGYYISEIIGSGDICDVTGAERMVEIQYVCGGSNSGPSTIQWVRETKICVYEAQVTIPELCNLELLAKNEDQKNASPILCRMPAKSKIGSNSIDLITKYEPIFLGSGIYFLRPFNTDERDKLMVTDNAMSNWDEITETYYQKFGNAINKMLSLRLVSLPNGHILQPGDSCVWLAEVVDMKDRFQTTLSLNILNSQRAEIFFNKTFTFNEDNGNFLSYKIGDHGESTELGQITHSNKADINTAEIRSDEYLINTDNELFLRISKEIAEVKELLNEIVSPHEMEVIFENMRNQPNNDFELALMNKLKSSLNDDNKVEQINNARMDDDESTSHTTRDIGEAGSQTTGNTESEVTNVAAGVFIEHDEL
Protein: Uncharacterized protein, isoform C (Q0E8E6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRLLLVHIITICVLITIVKCGVPIGTGGPSIILESKDALLTCVVSDNSSNNTVIWKKGDEILTAGTVRVTKDHRVRILHDENPKGKNLETGGEVWVLLIKTLKPNDSGAYICELNSDPVLRSIHILTVKELHSSTGGPGNSTDTSTAESSDVFLLPPPLDAQDNRSFWRPSQVPPLVTHDFTECCERANVSTQCMGFCNVHNILDGTTGIDPEACERDFPGIVRCMADGRNHVPCCVDKQIPDLCQDMCRGEYTPFTDKLKTRVSCVQHTLSGLQCILKGVQLIPSSPTFVTIENVSETSVTIGWTAPDKLADRVSGYTINLTTLHSFDEDELSGEIVHRTASDSPESISLYSVPTNQTQLTLSNLSPLTMYAVIVTATNEFGSSLPTERLRFFTHTSASAAESKAGTTDKQAMPQLPDTRQCCEDNGMTHRMCLDKMCDPQKTDQANLPDFMVCAPWSNITFNCLANNIDHTPCCRARGIPSACFPLCAGKLTSLDFSLFKCLRFMSEYNSCLFQGYGVLADPPSKLRTVAKTDSFVILDWNKPKRLADTVSTYHVKFRRLGVGDDYLTVEKVLLHWTFWKKNSL
Protein: Protein LLP homolog (Protein LAPS18-like) (Q9BRT6)
Organism: Homo sapiens (Human)
Function: In hippocampal neurons, regulates dendritic and spine growth and synaptic transmission.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9D945}. Chromosome {ECO:0000269|PubMed:20813266}. Note=Cell-permeable protein. 22 hours after injection in the hippocampal area CA1, internalized by most cells at the injection site (By similarity). Localizes at the chromosome periphery during mitosis (PubMed:20813266). {ECO:0000250|UniProtKB:Q9D945, ECO:0000269|PubMed:20813266}.
Interaction partners:
- Large ribosomal subunit protein eL30
- Zinc finger protein 593
- Probable ribosome biogenesis protein RLP24
- 60S ribosomal export protein NMD3
- Nucleolar GTP-binding protein 2
- Eukaryotic translation initiation factor 6
- Ribosomal protein eL42-like
- Large ribosomal subunit protein eL8
- GTP-binding protein 4
- Large ribosomal subunit protein eL14
Sequence:
MAKSLRSKWKRKMRAEKRKKNAPKEASRLKSILKLDGDVLMKDVQEIATVVVPKPKHCQEKMQCEVKDEKDDMKMETDIKRNKKTLLDQHGQYPIWMNQRQRKRLKAKREKRKGKSKAKAVKVAKGLAW
Protein: cDNA FLJ13705 fis, clone PLACE2000302 (Q9H8E5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRTSMSEAATRWSCQGSCQKTCFSRVRPWRRRCSCGDSSSRRRRSCCTGSLGPMPRLPSLWPLSLPLRSLSSPHRVQGLGPPRRLKSQLLPRFFWRRQQEPLSSFPGRNEGGSEMEILGVCPVSPGALSYMESPTGFWRPREASSLELAKGISKRRHFLPAPALCPNPRSSEAFPGQSVSRWPFDIKETAPGPSLSALLPTC
Protein: Beta1,4-N-acetylgalactosaminyltransferase B (EC 2.4.-.-, EC 2.4.1.244) (RE31995p) (Q9VAQ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
- Palmitoyltransferase
- Beta-1,3-galactosyltransferase brn
- Beta1,4-N-acetylgalactosaminyltransferase A
- Beta-1,4-mannosyltransferase egh
- Alpha1,4-galactosyltransferase 1
Sequence:
MFVRLWVRSFHKYDLLIAIGLITLIVYLCLPFRFASHYDYIEESKIEGALVPQVTRNVSQQEVFECTYSEIIAENRFVYHLAHYHDAVQRGAEIRPGGEFRPEGCQARYSTAIIVPYRQREEQLHAFLTYMHNYLPQQLIHYRIFLVEQFDHKPFNRAMLFNIGAQVAAEYGFPCLILHDVDLLPLNSGQIYACSERPRHMSSALDHWRFRLPYRGLFGGVVAINTAQYQQINGMSNLYYGWGGEDDDLYERLQALNIDICRFAMEFSKYTMLKHKQEQPNANRVALLRSATLRQHADGLNSLVYTEMERRMHSLFTHILVDT
Protein: Non-receptor protein tyrosine kinase 2-3 (S5RA51)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MMSRSGRFKSTRTGSSTGQCEPPQGPGVHVYLFWTKGGERYLTHTEGKVTAEELSISAAQTVGITPLCHVLFSLYDPESHCWYSPNHFFNSEEQTRLTLHYRMRFYFRNWHGLSEKEPSVVRYAPRSGTEHGGSPLLEMTSLEYLFCQAKFDFVNDVTPMEDAQGKEELSRFKNESLGMAVLHLSHQALRSGCTLQEVAKSVSFLRCIPRSFAKHIARDNFLTKIRIRRVFADFVRTFQEHTVDVGRLGSQEVMYKYLSTLEHLAPRFGTETFLAAHLELRTDGGDGSGSYLNTSRAHGASDPENVGPQVMHEVMVSGTKGIQWRKMTVQKPQANSYFGNDYLGNRKSVKQSPLQQEPTSSDTWTSFCDFPEISHITITGANVSIIKQDNFSMEVQMNSSLEALSFVSLLDGYFRLTADAHHYLCHEVAPPRVVLSATNGLHGPMKD
Protein: Interferon regulatory factor 7 (B6CBU8)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MQSCKPQFADWLIEQVRTEQYTGLFFMDNNKFRVPWKHDSRKDCSEDDRKIFRAWAVVSGKITEHPNDKAKWKTNFRSALNSLCRRFKMVEDHSKDSNDPHKVYLVINEYNYESPLIEEITLENYGIDHALTTTENTPPGMEHDILNFSNLTLNHLDLNQHTENYIPVHTHHPVPPVLIQQPYAQVNPDALLNLPATRSSLWDLEITISYRGSEMLKTQVSGPRVQLHYQCNALEPNTQPLCFPSTDGLPDLKQIEYTNCILRSVQRGLLLEVQNTGIYGYRQDKCHVFSSTSNPREAHPEPRKMPQNEMVQLLNFQQYENELIAFKENRRGSPDYTIHMCFGEKFPDGKPPEKKLIVVKVVPLICRYFHEVAQEEGASSLQNDISLQISHHNSLMELINATWPDGPQHTMGQYF
Protein: Membrane-bound acid phosphatase 2 (Q38AP9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPYACLHGGSLCLLISLLSCLGAQAVQTLHLVQLVHRHGARSPKVKHNQSQICGEVPCGYLNAAGKMMLVNAGEFLRNHYNSNASEPFFPEESYNSCVTYSRSTDVPRTLQSAGCLLRGMFPNASEFFPAIHTADVSTDWLLRYDVIPQAYAFSHLDEHWWRNVCNPKLDTLIDTNTLLSVSREVFSEGFCADPQNRCHCAATLFDIGVAMQSDGRIDKHPLLRENLGRLRDIKFFEDSHRFVYNASDRTHAKMGSLGQHLAQEILKNAENHMNGLTSYKLYHYSAHDTTIAPLAATLGDSTTTGITPPYGQLYAFELLYDHEVKGYIIRIRRGAPGQKPEEGYAFSWGEFQMKCMNENHTVYTAEDNKCPYHDFRRFVKSTKPHDPAGLCYLNRRYRELFHCPGNVGKPPNKQCKVFRRVCPAWSCEEGYTLNSVTLECVCSSRKCMENRDLSISTDTLGRNLFTIFIFVLLALLIPIFSVFVCIGKKLRARTRRTRAKG
Protein: Thylakoid lumenal 15 kDa protein 1, chloroplastic (p15) (O22160)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511}.
Interaction partners:
- Thylakoid lumenal 17.4 kDa protein, chloroplastic
- Probable DNA helicase MCM9
- Bifunctional dTDP-4-dehydrorhamnose 3,5-epimerase/dTDP-4-dehydrorhamnose reductase
Sequence:
MVILSNVSLFSCCNISQKPSLFSPSSRSSHCPIRCSQSQEGKEVVTSPLRSVVWSLGEEVSKRSLFALVSASLFFVDPALAFKGGGPYGQGVTRGQDLSGKDFSGQTLIRQDFKTSILRQANFKGAKLLGASFFDADLTGADLSEADLRGADFSLANVTKVNLTNANLEGATVTGNTSFKGSNITGADFTDVPLRDDQRVYLCKVADGVNATTGNATRDTLLCN
Protein: Peroxisomal membrane protein 11B (Peroxin-11B) (AtPEX11b) (Q9STY0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in peroxisomal proliferation. Promotes peroxisomal duplication, aggregation or elongation without fission.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:17220199, ECO:0000269|PubMed:20179140}; Multi-pass membrane protein {ECO:0000269|PubMed:17220199, ECO:0000269|PubMed:20179140}.
Interaction partners:
- Peroxisomal membrane protein PEX14
- Mitochondrial fission 1 protein B
- Mitochondrial fission 1 protein A
- Peroxisomal membrane protein 11D
- Peroxisomal membrane protein 11C
- Peroxisomal membrane protein 11E
- Peroxisome biogenesis protein 3-1
- Peroxisome biogenesis protein 16
- Peroxisome biogenesis protein 19-2
- Peroxisome biogenesis protein 19-1
Sequence:
MSLDTVDKLVVFLAKRDGIDKLVKTFQYVAKLACWHVEATRPEAADRFKKWEVASGLSRKAFRTGRSLTGFNALRRNPGATPMIRFLAVLANSGEMVYFFFDHFLWLSRIGSIDAKLAKKMSFISAFGESFGYTFFIIIDCIFIKQRLKSLKKLQHSTDEPKEEIGAKISEIRGDIVMRLMGISANVADLLIALAEIHPNPFCNHTITLGISGLVSAWAGWYRNWPS
Protein: DNA-directed RNA polymerase II subunit RPB9 (RNA polymerase II subunit B9) (DNA-directed RNA polymerase II subunit I) (RNA polymerase II 14.5 kDa subunit) (RPB14.5) (P36954)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB9 is part of the upper jaw surrounding the central large cleft and thought to grab the incoming DNA template (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:9852112}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB7
- General transcription factor IIF subunit 1
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II subunit RPB11-a
Sequence:
MEPDGTYEPGFVGIRFCQECNNMLYPKEDKENRILLYACRNCDYQQEADNSCIYVNKITHEVDELTQIIADVSQDPTLPRTEDHPCQKCGHKEAVFFQSHSARAEDAMRLYYVCTAPHCGHRWTE
Protein: C-type lectin domain-containing protein (O45445)
Organism: Caenorhabditis elegans
Interaction partners:
- C-type LECtin
- C-type lectin domain-containing protein
- Sulfhydryl oxidase
- VWFA domain-containing protein
- C-type lectin domain-containing protein
- C-type lectin domain-containing protein
- C-type lectin domain-containing protein
- N-acetyltransferase domain-containing protein
- C-type lectin domain-containing protein
- C-type lectin domain-containing protein
Sequence:
MEIANKRAWREYISYEIIRLQMHQILTLFLLALAASPSQAVTDRSCGSDLSRLWLDIVFVVDNSKNMNLYNVYNTISNLFNPFVQIGTGYDDPRSTRVGFITYNWNATDVADFYKLQSYSDLSSQIQALSVTPLSRADETYIDTGLQAAINMINATGGLRDNYKKVVVLFTSKYNYYHTYPEDLTDYLKSTGVTIITVNTGGDSYTTQSLRDKIASKGMAFAMSDGNTTAELQKAVLAINCFCRPGWMQYHYPLKSDNIYSNYGVCLYRPDSAMTKFAAQSYCHSLTTNGYLVSELDQQKRAFNWDYLNSKGITINAFYNGLTNYNGTWWWDQPSGQPLWPLNPNSGAPPQRSGCVVDMKYSDGSISWTPISCTSFFRFLCESVACDTDNYCEF
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (E9PG73)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGIKVQRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHYKSCLFHRVVKDFMVQGGDFSEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELIPKSKVKKEEKKRHKSSSSSSSSSSDSDSSSDSQSSSDSSDSESATEEKSKKRKKKHRKNSRKHKKEKKKRKKSKKSASSESEAENLEAQPQSTVRPEEIPPIPENRFLMRKSPPKADEKERKNRERERERECNPPNSQPASYQRRLLVTRSGRKIKGRGPRRYRTPSRSRSRDRFRRSETPPHWRQEMQRAQRMRVSSGERWIKGDKSELNEIKENQRSPVRVKERKITDHRNVSESPNRKNEKEKKVKDHKSNSKERDIRRNSEKDDKYKNKVKKRAKSKSRSKSKEKSKSKERDSKHNRNEEKRMRSRSKGRDHENVKEKEKQSDSKGKDQERSRSKEKSKQLESKSNEHDHSKSKEKDRRAQSRSRECDITKGKHSYNSRTRERSRSRDRSRRVRSRTHDRDRSRSKEYHRYREQEYRRRGRSRSRERRTPPGRSRSKDRRRRRRDSRSSEREESQSRNKDKYRNQESKSSHRKENSESEKRMYSKSRDHNSSNNSREKKADRDQSPFSKIKQSSQDNELKSSMLKNKEDEKIRSSVEKENQKSKGQENDHVHEKNKKFDHESSPGTDEDKSG