wanglab/gogpt-training-data huggingface dataset:
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (G9CU32)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MEGGGPPQAADTEMAEQPNPQHHQQQPPQMGIGLENIPATLSHGGRFIQYNIFGNIFEVTAKYKPPIMPIGKGAYGIVCSALNSETNEQVALKKIANAFDNKIDAKRTLREIKLLRHMDHENVVAIRDIIPPPKRECFNDVYIAYELMDTDLHQIIRSNQALSEEHCQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARVTSESDFMTEYVVTRWYRAPELLLNSSDYTAAIDVWSVGCIFMELMDRKPLFPGRDHVHQLRLLIELIGTPSEAELGFLNANARRYIQQLPLYHRQSFTEKFPTVHPLAIDLVEKMLTFDPRLRITVEDALAHPYLSSLHDLSDEPVCMTPFNFDFEQHALTEEQMKELIYREALTFNPEYVQP
Protein: Protein smoothened (Protein Gx) (Q99835)
Organism: Homo sapiens (Human)
Function: G protein-coupled receptor that probably associates with the patched protein (PTCH) to transduce the hedgehog's proteins signal. Binding of sonic hedgehog (SHH) to its receptor patched is thought to prevent normal inhibition by patched of smoothened (SMO). Required for the accumulation of KIF7, GLI2 and GLI3 in the cilia. Interacts with DLG5 at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P56726}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium {ECO:0000269|PubMed:22072986}. Note=Cilium localization is promoted by SHH and is required for activity. {ECO:0000250|UniProtKB:P56726}.
Interaction partners:
- Sonic hedgehog protein
- Protein patched homolog 1
- Suppressor of fused homolog
- Indian hedgehog protein
- Beta-arrestin-2
- Beta-arrestin-1
- Protein patched homolog 2
- Kinesin-like protein KIF3A
- Beta-adrenergic receptor kinase 1
- Zinc finger protein GLI1
Sequence:
MAAARPARGPELPLLGLLLLLLLGDPGRGAASSGNATGPGPRSAGGSARRSAAVTGPPPPLSHCGRAAPCEPLRYNVCLGSVLPYGATSTLLAGDSDSQEEAHGKLVLWSGLRNAPRCWAVIQPLLCAVYMPKCENDRVELPSRTLCQATRGPCAIVERERGWPDFLRCTPDRFPEGCTNEVQNIKFNSSGQCEVPLVRTDNPKSWYEDVEGCGIQCQNPLFTEAEHQDMHSYIAAFGAVTGLCTLFTLATFVADWRNSNRYPAVILFYVNACFFVGSIGWLAQFMDGARREIVCRADGTMRLGEPTSNETLSCVIIFVIVYYALMAGVVWFVVLTYAWHTSFKALGTTYQPLSGKTSYFHLLTWSLPFVLTVAILAVAQVDGDSVSGICFVGYKNYRYRAGFVLAPIGLVLIVGGYFLIRGVMTLFSIKSNHPGLLSEKAASKINETMLRLGIFGFLAFGFVLITFSCHFYDFFNQAEWERSFRDYVLCQANVTIGLPTKQPIPDCEIKNRPSLLVEKINLFAMFGTGIAMSTWVWTKATLLIWRRTWCRLTGQSDDEPKRIKKSKMIAKAFSKRHELLQNPGQELSFSMHTVSHDGPVAGLAFDLNEPSADVSSAWAQHVTKMVARRGAILPQDISVTPVATPVPPEEQANLWLVEAEISPELQKRLGRKKKRRKRKKEVCPLAPPPELHPPAPAPSTIPRLPQLPRQKCLVAAGAWGAGDSCRQGAWTLVSNPFCPEPSPPQDPFLPSAPAPVAWAHGRRQGLGPIHSRTNLMDTELMDADSDF
Protein: Immunoglobulin heavy variable 3-30 (Ig heavy chain V-III region BUR) (Ig heavy chain V-III region CAM) (Ig heavy chain V-III region GA) (Ig heavy chain V-III region NIE) (P01768)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MEFGLSWVFLVALLRGVQCQVQLVESGGGVVQPGRSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVAVISYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAK
Protein: Serine-arginine protein 55 (SRP55) (52 kDa bracketing protein) (B52 protein) (Protein enhancer of deformed) (P26686)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for development. May have a critical role in splicing or in controlling alternative splice site use of at least some pre-mRNA in vivo. Not required for all splicing. May play a general role in the condensation or decondensation of chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:1717489, ECO:0000269|PubMed:1741384, ECO:0000269|PubMed:1885003}. Note=Associated with boundaries of transcriptionally active chromatin.
Interaction partners:
- Cell division cycle 5, isoform A
- BcDNA.LD23634
- Nuclear cap-binding protein subunit 2
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Transportin-3
- tRNA selenocysteine-associated protein 1
- Serine/arginine repetitive matrix protein 1
- Putative RNA-binding protein Alsin2
Sequence:
MVGSRVYVGGLPYGVRERDLERFFKGYGRTRDILIKNGYGFVEFEDYRDADDAVYELNGKELLGERVVVEPARGTARGSNRDRYDDRYGGRRGGGGGRYNEKNKNSRSSSRYGPPLRTEYRLIVENLSSRVSWQDLKDYMRQAGEVTYADAHKQRRNEGVVEFASLSDMKTAIEKLDDTELNGRRIHLVEDRRGGRSGGGGGSGRGRSRSSSSRSRSRSRRRSRSRRSSHSRSKSRSRSKSRGGRSKSKSPVKSRSRSRSRSNKSRDVSKSKSKSHSRTRSRSPKRERDSRSRSRSVSKRESRSRSRSKSIHRDSRSRPPTVSFKSSFYKFTTMPFFCSDRSASAENKSRSRSRSRSASPKNGNASPDRNNESMDD
Protein: LD07342p (Myb-interacting protein 130) (Q9W542)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- LD06557p
- Protein lin-54 homolog
- Lin-52, isoform A
- Transcription factor E2F2
- Myb protein
- Chromatin assembly factor 1 p55 subunit
- RE32990p
- Retinoblastoma family protein
- Transcription factor Dp
- LD05287p
Sequence:
MLTGRPVRMSVAVNQKGWGKKAGASVSDSAIRTQSALSEGGGAIDVRPMEHDEEINREDLNLDEDDEMEEEEEEEHADEEDDDEEPDSNENSAPEEQVEPPAFSLATLGLQRVGSAPPPKPKVQKAPIPTLNARGMPARIRKRNRLFYDENIINDDKPLRMSLAPKKTPGRPPQSAGGGSSQKIPLTPSKVLKKRKGVVSRYMRSSEQGTNSVSASNQPQLLGKHKKATPSKSQSVGSKLGSGGPKTGRGAHFIGKGTAAAVAAVAAAEEEANQAEAAALANKRLGQSIGLRLRNLLKLPKAHKWAIAEWFYSYVDKPLFECRDEFMNHVNELAPRLGTRSLIRHEWVNIRRRMGRPRRCSAKFFSEERKELDRKRQVIRTLQSRKPGEFKDSVSMLSDMPEKIPMTLPLGTKVTARLRSPQDGIFAGTVAAYDSLNAMYRVTFERIGLGTHAIPDYEIVSENFHEMLPLHSFTKDFRPNLMSIYQTNNLGFTTNLGFTANLTNNYLQKKEKIDGGAGAAAGAGSLYFKPQKHLATNNAAARNALSMKLNKSDPLLGQDSVGVSPIRQQLTRNRGYSTSLLEHLVRLEKYIAVKADRIQRLNKMNGTAELAMGDMISHDENGDRHRRQIAVNFQRQYAFNIVTIERINAELMFELTKVQELSSSLTRNPNVQAMISPTYLREECRAKASQTVDDINKGMVKNTRMIKLLKDLTTLLIVTQNLGGDCEVSEVNEVLEGCLEEVRSNLICSENREVFQMSVQGRLEYIAMDISRRLEEKSLSRVADGDDDIKSLKSEDETDEDHVQDHKHGADEEPAADTSKTKAKGSPKQVEGKENSEVDKMDHSSHPMDTDTEKEEKLESGGSENAGYASQQRQDEDQDTEEQHLDLEEQHLDPEEHHLDLEEQHLDPEEQHLDLEEHHLELEEQHLDPEEQSLNPAVTEDTQITIESMKESDEEFQSAAETEEDDMVGLIMEEEEEEEFVYDKDL
Protein: TLE family member 3, transcriptional corepressor (H0YKT5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPPPPPLSCLRGLQAPHQPGQPGFKFTVAESCDRIKDEFQFLQAQYHSLKVEYDKLANEKTEMQRHYVMYYEMSYGLNIEMHKQTEIAKRLNTILAQIMPFLSQEHQQQVAQAVERAKQVTMTELNAIIGQQLQAQHLSHATHGPPVQLPPHPSGLQPPGIPPVTGSSSGLLALGALGSQAHLTVKDEKNHHELDHRERESSANNSVSPSESLRASEKHRGSADYSMEAKKRKAEEKDSLSRYDSDGDKSDDLVVDVSNEDPATPRVSPAHSPPENGLDKARSLKKDAPTSPASVASSSSTPSSKTKDLGHNDKSSTPGLKSNTPTPRNDAPTPGTSTTPGLRSMPGKPPGMDPIASALRTPISITSSYAAPFAMMSHHEMNGSLTSPGAYAGLHNIPPQMSAAAAAAAAAYGRSPMVSFGAVGFDPHPPMRATGLPSSLASIPGGKPAYSFHVSADGQMQPVPFPHDALAGPGIPRHARQINTLSHGEVVCAVTISNPTRHVYTGGKGCVKIWDISQPGSKSPISQLDCLNRDNYIRSCKLLPDGRTLIVGGEASTLTIWDLASPTPRIKAELTSSAPACYALAISPDAKVCFSCCSDGNIAVWDLHNQTLVRQFQGHTDGASCIDISHDGTKLWTGGLDNTVRSWDLREGRQLQQHDFTSQIFSLGYCPTGEWLAVGMESSNVEVLHHTKPDKYQLHLHESCVLSLKFAYCGKWFVSTGKDNLLNAWRTPYGASIFQSKESSSVLSCDISADDKYIVTGSGDKKATVYEVIY
Protein: Dynein axonemal intermediate chain 1 (A0A286ZPL5)
Organism: Sus scrofa (Pig)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}.
Interaction partners:
- Dynein axonemal heavy chain 11
- Dynein axonemal heavy chain 5
- Dynein regulatory complex subunit 2
- Dynein axonemal heavy chain 10
- Dynein axonemal intermediate chain 2
- Coiled-coil domain containing 103
- Radial spoke head component 4A
- Dynein axonemal heavy chain 9
- Dynein axonemal light intermediate chain 1.
- Dynein axonemal heavy chain 12
Sequence:
VLPASLKMPHKQPPHKQSFTMGRGARKKDEDSGTDVGEGTDEWAQSKATVRPPDQLDLTDAELKEEFTRILTANNPHAPQNIVRYSFKEGTYKLIGFVDQLAVHFSQVGNLIPKDSDEGRRQHYRDELAAVSYQGSQESVKVVISETEILEEEEEPKEAEAGSQTDVPTAEASEKVAEEELITPKQPKERKLTNKFNFSERASQTFNNPLRDRECQMEPPPRTNFSATANQWEIYDAYVEELEKQEKTKEKEKTKTPVAKKMGKMAMRKMTSMESQSDDITKVTQAAKIVERMVNQNTYDDVAQDFKYYEDVADEYRDQEGTLLPLWKFQNDKAKRLAVTALCWNPKYNDLFAVGYGSYDFMKQSRGMLLLYSMKNPSFPEYIFSSESGIMCLDIHVDHPYLVVVGHYDGNVAIYNLKKPHSQPAFRSSAKSGKHTDPVWQVRWQKDDMDNNLNFFSVSSDGRIVSWTLVKSELVHTEVIKLKVEGSSSESLEGLQIHTVGCGTAFDFHKEIDYMFLVGTEEGKIYKCSKSYSSQFLDTYDAHNMAVDAVSWNPYHTKVFISCSSDWTVKIWDHTVKTPMFIYDLNSAVGDVAWAPYSSTVFAAVTTNGKTHVFDLSINKYEAICSQAVVAKKKNKITHVQFNPIHPIIIVGDDRGHVTCLKLSPNLRKMPKEKKGQEVQKGPAVEIAKLDKLLNLVREVKTKT
Protein: Somatostatin receptor type 2 (SS-2-R) (SS2-R) (SS2R) (SRIF-1) (P30680)
Organism: Rattus norvegicus (Rat)
Function: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate in neuron development and maturation during brain development. Mediates negative regulation of insulin receptor signaling through PTPN6. Inactivates SSTR3 receptor function following heterodimerization.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cytoplasm. Note=Located mainly at the cell surface under basal conditions. Agonist stimulation results in internalization to the cytoplasm.
Interaction partners:
- Somatostatin
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Interleukin-33
- Appetite-regulating hormone
- Pro-neuropeptide Y
- Interleukin-1 receptor-like 1
- D
- Endothelin-1
Sequence:
MELTSEQFNGSQVWIPSPFDLNGSLGPSNGSNQTEPYYDMTSNAVLTFIYFVVCVVGLCGNTLVIYVILRYAKMKTITNIYILNLAIADELFMLGLPFLAMQVALVHWPFGKAICRVVMTVDGINQFTSIFCLTVMSIDRYLAVVHPIKSAKWRRPRTAKMINVAVWGVSLLVILPIMIYAGLRSNQWGRSSCTINWPGESGAWYTGFIIYAFILGFLVPLTIICLCYLFIIIKVKSSGIRVGSSKRKKSEKKVTRMVSIVVAVFIFCWLPFYIFNVSSVSVAISPTPALKGMFDFVVILTYANSCANPILYAFLSDNFKKSFQNVLCLVKVSGAEDGERSDSKQDKSRLNETTETQRTLLNGDLQTSI
Protein: Lysophosphatidic acid receptor 6 (LPA receptor 6) (LPA-6) (Oleoyl-L-alpha-lysophosphatidic acid receptor) (P2Y purinoceptor 5) (P2Y5) (Purinergic receptor 5) (Q8BMC0)
Organism: Mus musculus (Mouse)
Function: Binds to oleoyl-L-alpha-lysophosphatidic acid (LPA). Intracellular cAMP is involved in the receptor activation. Important for the maintenance of hair growth and texture (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Lysophosphatidic acid receptor 3
- Lysophosphatidic acid receptor 1
- Lysophosphatidic acid receptor 2
- Guanine nucleotide-binding protein subunit alpha-12
- Muscarinic acetylcholine receptor M1
- Lysophosphatidic acid receptor 5
- Prothrombin
- Lysophosphatidic acid receptor 4
- Proteinase-activated receptor 1
- Angiotensinogen
Sequence:
MVSSNGSQCPYDDSFKYTLYGCMFSMVFVLGLISNCVAIYIFICALKVRNETTTYMINLAMSDLLFVFTLPFRIFYFATRNWPFGDLLCKISVMLFYTNMYGSILFLTCISVDRFLAIVYPFKSKTLRTKRNAKIVCIAVWFTVMGGSAPAVFFQSTHSQGNNTSEACFENFPAATWKTYLSRIVIFIEIVGFFIPLILNVTCSSMVLRTLNKPVTLSRSKMNKTKVLKMIFVHLVIFCFCFVPYNINLILYSLMRTQTFVNCSVVAAVRTMYPITLCIAVSNCCFDPIVYYFTSDTIQNSIKMKNWSVRRSDSRFSEVQGTENFIQHNLQTLKNKIFDNESAI
Protein: Trace amine-associated receptor 13a (Q5QNP9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDLSSQEYDPSQFCFPAVNNSCLKGTHHVSTQTVVYLILASAMTVTILGNSVVIISIAHFKQLQTPTNILVMSLALADLLLGLVVMPFSMIRSVDGCWYYGETFCMLHSTFDLFLTSVSILHLVCIAVDRHQAVCYPLQYPTRITISVAWVMVMISWTLIAIYSYGLVYSKANVEGLEEYIESIYCMGHCSLLFSKLWSVLDTFITFFFPSCIMVGLYIRIFVVANKHARVITEANPNENENVFKSSRRSERKAAKTLGIVVGAFIICWLPFFINSLMDPYINFSTPVALFDAFVWLGYINSTINPIIYGFFYPWFRKTLYLIITRRIFEPNSSDINVFTV
Protein: Putative elongation factor 1-delta-like protein (Putative EF-1-delta-like pseudogene 3 protein) (Q658K8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATNFLVGEKIWFHKFKYGDAERRFYEQMNGPVAGASLQEASMILHDIARARENIPKSLAGSLGPGASSGPSGDHSELVVRIASLEVDNQRDLAERAGEELARPLGHSPADPAHVSHAPSGAPGQEASHTSRG
Protein: Transcription factor RelB (Q04863)
Organism: Mus musculus (Mouse)
Function: NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49 (By similarity). As a member of the NUPR1/RELB/IER3 survival pathway, may allow the development of pancreatic intraepithelial neoplasias. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a CRY1/CRY2 independent manner. Increased repression of the heterodimer is seen in the presence of NFKB2/p52. Is required for both T and B lymphocyte maturation and function (By similarity).
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Colocalizes with NEK6 in the centrosome. {ECO:0000250}.
Interaction partners:
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor p65
- Nuclear factor NF-kappa-B p100 subunit
- Targeting protein for Xklp2
- Proto-oncogene c-Rel
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- NF-kappa-B inhibitor epsilon
- NF-kappa-B inhibitor alpha
- NF-kappa-B inhibitor beta
- B-cell lymphoma 3 protein homolog
Sequence:
MPSRRAARESAPELGALGSSDLSSLSLTVSRTTDELEIIDEYIKENGFGLDGTQLSEMPRLVPRGPASLSSVTLGPAAPPPPATPSWSCTLGRLVSPGPCPRPYLVITEQPKQRGMRFRYECEGRSAGSILGESSTEASKTLPAIELRDCGGLREVEVTACLVWKDWPHRVHPHSLVGKDCTDGVCRVRLRPHVSPRHSFNNLGIQCVRKKEIEAAIERKIQLGIDPYNAGSLKNHQEVDMNVVRICFQASYRDQQGHLHRMDPILSEPVYDKKSTNTSELRICRINKESGPCTGGEELYLLCDKVQKEDISVVFSTASWEGRADFSQADVHRQIAIVFKTPPYEDLEISEPVTVNVFLQRLTDGVCSEPLPFTYLPRDHDSYGVDKKRKRGLPDVLGELSSSDPHGIESKRRKKKPVFLDHFLPGHSSGLFLPPSALQPADSDFFPASISLPGLEPPGGPDLLDDGFAYDPSAPTLFTMLDLLPPAPPLASAVVGSGGAGATVVESSGPEPLSLDSFAAPGPGDVGTASLVGSNMFPNQYREAAFGGGLLSPGPEAT
Protein: Leucine-rich repeat-containing protein 59 (Ribosome-binding protein p34) (p34) [Cleaved into: Leucine-rich repeat-containing protein 59, N-terminally processed] (Q96AG4)
Organism: Homo sapiens (Human)
Function: Required for nuclear import of FGF1, but not that of FGF2. Might regulate nuclear import of exogenous FGF1 by facilitating interaction with the nuclear import machinery and by transporting cytosolic FGF1 to, and possibly through, the nuclear pores.
Subcellular location: Microsome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane; Single-pass type II membrane protein. Nucleus envelope. Note=Localization in the nuclear envelope depends upon the nuclear import machinery, including KPNB1.
Interaction partners:
Sequence:
MTKAGSKGGNLRDKLDGNELDLSLSDLNEVPVKELAALPKATILDLSCNKLTTLPSDFCGLTHLVKLDLSKNKLQQLPADFGRLVNLQHLDLLNNKLVTLPVSFAQLKNLKWLDLKDNPLDPVLAKVAGDCLDEKQCKQCANKVLQHMKAVQADQERERQRRLEVEREAEKKREAKQRAKEAQERELRKREKAEEKERRRKEYDALKAAKREQEKKPKKEANQAPKSKSGSRPRKPPPRKHTRSWAVLKLLLLLLLFGVAGGLVACRVTELQQQPLCTSVNTIYDNAVQGLRRHEILQWVLQTDSQQ
Protein: N-acyl homoserine lactonase (AHL-lactonase) (EC 3.1.1.81) (Homoserine lactone lactonase) (A3FJ64)
Organism: Bacillus thuringiensis
Function: Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone, but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3, has maximum activity on C10-AHL.
Interaction partners:
Sequence:
MTVKKLYFIPAGRCMLDHSSVNSALTPGKLLNLPVWCYLLETEEGPILVDTGMPESAVNNEGLFNGTFVEGQILPKMTEEDRIVNILKRVGYEPDDLLYIISSHLHFDHAGGNGAFTNTPIIVQRTEYEAALHREEYMKECILPHLNYKIIEGDYEVVPGVQLLYTPGHSPGHQSLFIETEQSGSVLLTIDASYTKENFEDEVPFAGFDPELALSSIKRLKEVVKKEKPIIFFGHDIEQEKSCRVFPEYI
Protein: Tubulin alpha chain (C9JJQ8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MAPILPGTRRVTSGASPQVPLPFWRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAP
Protein: IRS-type PTB domain-containing protein (Q18820)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLPAEPTSGEPKNDGEYVETMFDATEEKKQETIAPKQEETVKKLSMAAREERIRESRQQGQLKEKRLKNPDSKGDTSHDKPTRETWKPLAVEDLPKDEDPDEFGIPEVYKCGNCLVGFAPVKKKKLMFVTLTERCLELHESEKSYRAGKAAKHMVDLSMSFNVHSEHYDAKLKKCLCLMGPDETICMRPEGGILTIEGWRRAIVKLIHESRRRKMDRVPRPEDIFDAAYDVRVCLFPKNLEKYVESLKTDGFTNICTVAKELLGKKRLCLYPNTLAIVDLCIEPTAYGLPPAGFPPFRASSMFILERNTVAYYGFRENYFYVRIGKGSPYRGFELLFQVDTNEVCKEIYSRLRALADRDLENRKQESIRRPERPRVSTLQSVKPGKEETGLREALLESYGHLRKKNSTQSERGEIVVPEQERKMSDNRPRLRTQDIKTVTKPELKSEEPIRPRLPPLKFNANKPSGEFLLSLQREKELMEEARKNGYDGRTHNPDGTPREIKKDFLDTVCPQAAAPEVVIKEKIINNDTYTLMGPADWGKLEDIVKDDYSDSGDSCYSSRRGTGSQPTRPAASHLACQMQNRTQSFGAKQQTFQNRLPPTVNLPDSERKISAANQGTSNQLDLPQEDPRKRAFSLGSKNFFNLIGLNDFRRLVSKRHRTSSPNHTSTSGISLNSSNASPSASSNFLASSEYLEHARTDSFGSARSSPKSLHTQRTSSPKRRSDEDLISIDFSRLGKNSASDTKRFPFGGGGPGGSFDYDREKREKEDNNRRDREKAAMDLKRKEEWEARELAEKKRELERKIQAKKDRKLEKGRGKDREKDKDHDHDKEFRPKADSGIADCTPSSSFSGKKDHKNDGSSDSAYMDKEGLKYLADIKKRKKEQGAIDTTNSSSSSLSTIVSIEDNKVTRRITETVETKVVTADLAKALGAIDPNRRSSACIEINRKPSICTAIMEEREGEASETDSRGEPSDRKTTAAPVTRKPASTGSSMSPFRRLKFLSFRK
Protein: Transmembrane prolyl 4-hydroxylase (P4H-TM) (EC 1.14.11.29) (Hypoxia-inducible factor prolyl hydroxylase 4) (HIF-PH4) (HIF-prolyl hydroxylase 4) (HPH-4) (Q9NXG6)
Organism: Homo sapiens (Human)
Function: Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12163023, ECO:0000269|PubMed:17726031}; Single-pass type II membrane protein {ECO:0000269|PubMed:12163023, ECO:0000269|PubMed:17726031}.
Interaction partners:
- Paired box protein Pax-6
- Polyhomeotic-like protein 3
Sequence:
MAAAAVTGQRPETAAAEEASRPQWAPPDHCQAQAAAGLGDGEDAPVRPLCKPRGICSRAYFLVLMVFVHLYLGNVLALLLFVHYSNGDESSDPGPQHRAQGPGPEPTLGPLTRLEGIKVGHERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYEEAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDGDGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRLTRLSPEIVELSEPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYMTVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRVKPQQGTAVFWYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLAREGGTDSQPEWALDRAYRDARVEL
Protein: Small hydrophobic protein (P22112)
Organism: Mumps virus genotype B (strain Miyahara vaccine) (MuV)
Function: Plays a role in the inhibition of the host NF-kappa-B pathway. This inhibition occurs at the receptor level, by preventing the signaling of TNFR1 as well as IL-1R and TLR3.
Subcellular location: Virion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Host cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPAIQPPLYPTFLLLILLSLIITLYVWIISTITYKTAVRHAALHQRSFSRWSLDHSL
Protein: Calsyntenin-1 [Cleaved into: Secreted calsyntenin-1] (G5ED46)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:25035490}; Single-pass type I membrane protein {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:18381821, ECO:0000269|PubMed:25035490}. Cell projection, axon {ECO:0000269|PubMed:25035490}.; SUBCELLULAR LOCATION: [Secreted calsyntenin-1]: Secreted {ECO:0000269|PubMed:18381821}. Synaptic cleft {ECO:0000269|PubMed:29529030}. Note=Released in the extracellular space following proteolytic cleavage. {ECO:0000269|PubMed:18381821}.
Interaction partners:
- Kinesin light chain
- Kinesin light chain
- Neurexin-related protein bam-2
- Cadherin domain-containing protein
Sequence:
MRTAYFIFVGALLGVSYAKHHHAARAPIINLQGAEELVAVVREDENIISTVPDFAILSETGPVCNYLLTSQNNEPVPFDIQVVDKYTGAAVLRVKDAATLDCKKPEYNLQVQAVKCDNDNVKSEGVSLKIRVKDTNNHAPEIENPWYTFHVEEGKVVEEVGVLKASDKDCGHPNGEICEYEITNGLKELPFAINNHGVLRTTQPLNFTQSKSYILTVVAIDCAMRKSKSSLVTVHVDEKCVQGITAMNERVNYAPGVGSKLLLPDVSLEFCEKETICEPKSVQSVIELRAGHVTQGCARDTVYDNQTIQSCGLSTATVKLLNEEALTSSAENQILADQGIEFDGARGVTVSDENHQGLIPDHFTLSFSMKHAAGTKDEQSNKQNILCESDDFNMNRHHFSVYIRHCKLEVVLRREAGATSDFRAAEWRWSMPEVCDNEWHSYSLLFNGIDDVNVIVDGKSFKADERNPEILDDWPLHKTKATKTKLVVGACWHGRQQKLAQFFRGQLSSLYLLSGAVESERAIKCAHTCPEQLQFTGVDELLESQSATFSPDQTSLTLKAETSKQIGQMLKRVAYVNTQEKPAPGHRVFLVETEVTCKQDDKKMKLPSSKGYVFVQQAAEPTLSISASSQLKSNQHMVKVGQAMVPDLTITISQNNADGELEDVTQSHKIDYCKMHLQPARDMDVEYFSSPASLIAALNIEFEHDKDGILLRGEESAQGYKEVLSKVHYFNTRPESYAKRVYTVQCAMLKGRVLSNQLFVTMTIDGVTTTTSTTTEAPAPAQPDPIQFNFNSGETALDSLELIERHFEPAFDQLGSSRLQNILEMDLPRPKALLSHHGYDVGQGAIAGGAVAVVVVVCVGFLLVLLVIGVLKMRDTPMPRRRRQKRQSDGGMHWDDSGMNITVNPLDDVEKNGGAIDEFSDEEEEEETDGESECSYRDEEDDVSEDEEDQTEVLPHLDANQRVVGGLEWDDEDAISTNARSYRV
Protein: Uncharacterized protein YPL277C (Q08989)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Putative uncharacterized protein YHR214C-E
- Uncharacterized protein YOR389W
Sequence:
MRFHRQGISAIIGVLLIVLLGFCWKLSGSYGIVSTALPHNQSAIKSTDLPSIRWDNYHEFVRDIDFDNSTAIFNSIRAALRQSPSDIHPVGVSYFPAVIPKGTLMYHAGSKVPTTFEWLAMDHEFSYSFGLRSPSYGRKSLERRHGRFGNGTNGDHPKGPPPPPPPPDEKGRGSQKMLTYRAARDLNKFLYLDGASAAKTDSGEMDTQLMLSNVIKEKLNLTDDGENERMAERLYAARICKWGKPFGLDGIIRVEVGFEVVLCDFSADNVELVSMLEMVQPNQYLGLPAPTVISKEEGWPLDENGSLVEDQLTDDQKAILEREDGWEKAFSNFNAVKSFNQLRAGAAHDNGEHRIHIDYRYLVSGINRTYIAPDPNNRRLLDEGMTWEKQLDMVDDLEKALEVGFDATQSMDWQLAFDELVLKFAPLLKSVSNILNSDGDINESIAINATALTLNFCLPICEPIPGLKNGCRLFDLVICCQRCRRNC
Protein: UPF0259 membrane protein YciC (P21365)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Inner membrane-spanning protein YciB
- Acyl-CoA thioester hydrolase YciA
- Zinc chaperone YjiA
- Zinc chaperone YeiR
Sequence:
MSITAQSVYRDTGNFFRNQFMTILLVSLLCAFITVVLGHVFSPSDAQLAQLNDGVPVSGSSGLFDLVQNMSPEQQQILLQASAASTFSGLIGNAILAGGVILIIQLVSAGQRVSALRAIGASAPILPKLFILIFLTTLLVQIGIMLVVVPGIIMAILLALAPVMLVQDKMGVFASMRSSMRLTWANMRLVAPAVLSWLLAKTLLLLFASSFAALTPEIGAVLANTLSNLISAILLIYLFRLYMLIRQ