wanglab/gogpt-training-data huggingface dataset:
Protein: Slit homolog 1 protein (Slit-1) (Multiple epidermal growth factor-like domains protein 4) (Multiple EGF-like domains protein 4) (O88279)
Organism: Rattus norvegicus (Rat)
Function: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Roundabout guidance receptor 2
- Roundabout homolog 1
- Roundabout homolog 4
- Roundabout homolog 4
- Roundabout homolog 3
- Netrin-1
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L2
- Plexin-A1
Sequence:
MALTPQRGSSSGLSRPELWLLLWAAAWRLGATACPALCTCTGTTVDCHGTGLQAIPKNIPRNTERLELNGNNITRIHKNDFAGLKQLRVLQLMENQIGAVERGAFDDMKELERLRLNRNQLQVLPELLFQNNQALSRLDLSENSLQAVPRKAFRGATDLKNLQLDKNQISCIEEGAFRALRGLEVLTLNNNNITTIPVSSFNHMPKLRTFRLHSNHLFCDCHLAWLSQWLRQRPTIGLFTQCSGPASLRGLNVAEVQKSEFSCSGQGEAAQVPACTLSSGSCPAMCSCSNGIVDCRGKGLTAIPANLPETMTEIRLELNGIKSIPPGAFSPYRKLRRIDLSNNQIAEIAPDAFQGLRSLNSLVLYGNKITDLPRGVFGGLYTLQLLLLNANKINCIRPDAFQDLQNLSLLSLYDNKIQSLAKGTFTSLRAIQTLHLAQNPFICDCNLKWLADFLRTNPIETTGARCASPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYHLNSECTSDVACPHKCRCEASVVECSGLKLSKIPERIPQSTTELRLNNNEISILEATGLFKKLSHLKKINLSNNKVSEIEDGTFEGATSVSELHLTANQLESVRSGMFRGLDGLRTLMLRNNRISCIHNDSFTGLRNVRLLSLYDNHITTISPGAFDTLQALSTLNLLANPFNCNCQLAWLGDWLRKRKIVTGNPRCQNPDFLRQIPLQDVAFPDFRCEEGQEEVGCLPRPQCPQECACLDTVVRCSNKHLQALPKGIPKNVTELYLDGNQFTLVPGQLSTFKYLQLVDLSNNKISSLSNSSFTNMSQLTTLILSYNALQCIPPLAFQGLRSLRLLSLHGNDVSTLQEGIFADVTSLSHLAIGANPLYCDCHLRWLSSWVKTGYKEPGIARCAGPPEMEGKLLLTTPAKKFECQGPPSLAVQAKCDPCLSSPCQNQGTCHNDPLEVYRCTCPSGYKGRNCEVSLDSCSSNPCGNGGTCHAQEGEDAGFTCSCPSGFEGLTCGMNTDDCVKHDCVNGGVCVDGIGNYTCQCPLQYTGRACEQLVDFCSPDLNPCQHEAQCVGTPEGPRCECVPGYTGDNCSKNQDDCKDHQCQNGAQCVDEINSYACLCAEGYSGQLCEIPPAPRNSCEGTECQNGANCVDQGSRPVCQCLPGFGGPECEKLLSVNFVDRDTYLQFTDLQNWPRANITLQVSTAEDNGILLYNGDNDHIAVELYQGHVRVSYDPGSYPSSAIYSAETINDGQFHTVELVTFDQMVNLSIDGGSPMTMDNFGKHYTLNSEAPLYVGGMPVDVNSAAFRLWQILNGTSFHGCIRNLYINNELQDFTKTQMKPGVVPGCEPCRKLYCLHGICQPNATPGPVCHCEAGWGGLHCDQPVDGPCHGHKCVHGKCVPLDALAYSCQCQDGYSGALCNQVGAVAEPCGGLQCLHGHCQASATRGAHCVCSPGFSGELCEQESECRGDPVRDFHRVQRGYAICQTTRPLSWVECRGACPGQGCCQGLRLKRRKLTFECSDGTSFAEEVEKPTKCGCAPCA
Protein: Actin cytoskeleton-regulatory complex protein SLA1 (Q5ALV2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Required for assembly of the cortical actin cytoskeleton and for hyphal growth.
Subcellular location: Nucleus {ECO:0000250}. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch {ECO:0000250}. Cell tip. Note=Localizes in patches that are found concentrated at the hyphal tip.
Interaction partners:
- Ecm25p
- Actin-binding protein
- Sla2p
- Actin cytoskeleton-regulatory complex protein END3
- Actin cytoskeleton-regulatory complex protein PAN1
- Polyubiquitin
- Profilin
- Fimbrin
- SH3 domain-containing protein
- Regulator of cytoskeleton and endocytosis RVS167
Sequence:
MSSIYIGVYKALYDYAAQAEEELNIKQNDLLYLLEKSDIDDWWKVKKRVVATGEEIVDEPSGLVPSTYIEEAPVIKTATALYDYDKQTEEELSFNENDKFNVFDLNDPDWILVGDLAKEKFGFVPSNYIQLDSTAEPAQHQQQQPQQVFQPPPQQQQAIPQQQTQIPINNFPPPPTHKDRTPDFPAPPAHRDRSPEHPPPTPEKDYPRMFEQEPRSLGSRYDRQPEGREEEEDEAPPPMPSRPTGSNIVAPEPVVGRSNTYEQEENVEHSEHSYDGEFFTWYIDEVDGRKKRAIKLSIGQGLVIIKPNTTNPKKLRMRSSSSLDNQWRIKDLITFNNEKKHVFLEFKNPAASLELHAGSKDVAEAIMAILGDLKGAEAAHGLREVAKASKASANERNRKIGRLLYDFEVQGDDELDCKEGDEVYIIDQKKSKDWWMVENIATRRQGVVPSTYIEIISTSNLDKLTDGPLRRKSTKSKGRVVETKDKRSSHHRTREERDRIREKDRAQRDKAPTSQTEQDKSMPNFHRVRTWIDSSGTFKVEAEFLGCVEGKIHLHKTNGVKIAVAADKLSVEDLEYVERVTGTSLEQYKEQVMKQQAKRAKSKSKSGATATPSSTNETKYASSATAAINDIAPPKPTRPQTTTQVSNNGAPLYDWFDFFLECGVDIGNCQRYTLNFEREQMDENILEDISPSLLRTLGLREGDIIRVMKYLDAKFDRKKTPEAPQQNGGLFIDKNGNLKNNSSSTEISKVSADALPSPVKTQVTSFTPVNESTQNNNKIEDDAWAMKPAARSSEDLLKPSPQPQTPQYTGALSDLVNIKPVGTSNENKAKTEQIPVEPSAPALQPMKTSNTAATSSIPPQGPGVTPQRTGTLVPVQKTGGLVPVQRTGAGLVPVQTGGYLPAQPTGFVPITAQPTGFIPIQATGILQPQLTFGIVPLQTGTSTFNANNKTAPPRPDTAPPPITTFGQQPTFQPAFVPLQTGVITMPQTTFGGQSQQLPTQITGGAPPQTSFNQPALVPTQRTGGQITGGFVPQSNFGKQITGGFMDTNTLSFGQQITGNAQQQPPPSTSFGQQITGGLPATSFGQQITGGFPQTSFGQQMTGGAPQTSFGQHITGGNMPNTSFGQPFSQQATSNPFPQMANQFTQQQQYQQQQPVMNQFQQQPQQQQQPFYNQFQSQPNLNQMTNMFQNTSISSPATFNQQIPTTTFGQQPQFEGFGSQPLQSQPTGMGFGNAPLQSQPTGKRANLQAATPDNPFGF
Protein: Peptidyl-prolyl cis-trans isomerase FKBP1B (PPIase FKBP1B) (EC 5.2.1.8) (12.6 kDa FK506-binding protein) (12.6 kDa FKBP) (FKBP-12.6) (Calstabin-2) (FK506-binding protein 1B) (FKBP-1B) (Immunophilin FKBP12.6) (Rotamase) (P97534)
Organism: Rattus norvegicus (Rat)
Function: Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Cytoplasm {ECO:0000250}. Sarcoplasmic reticulum.
Interaction partners:
- Ryanodine receptor 2
- Ryanodine receptor 1
- Triadin
- Inositol 1,4,5-trisphosphate/ryanodine receptor domain-containing protein
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Uncharacterized protein.
- Serine/threonine-protein kinase mTOR
- A-kinase anchor protein 6
Sequence:
MGVEIETISPGDGRTFPKKGQICVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE
Protein: Arginase (EhArg) (EC 3.5.3.1) (C4LSS0)
Organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)
Function: Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis. By depleting host L-arginine, a substrate for nitric oxide synthase (NOS), prevents the production of nitric oxide (NO) by host activated macrophages, and thus allows the parasite to evade host immune response.
Interaction partners:
- ornithine decarboxylase
- Histidine ammonia-lyase
- Ornithine cyclodeaminase, putative
- Uncharacterized protein
- Aldehyde dehydrogenase
- Aspartate ammonia-lyase, putative
- NAD-specific glutamate dehydrogenase, putative
- fumarate hydratase
- Inositol-1-monophosphatase
- Small heat shock protein
Sequence:
MQFEKVTYIAVPQKYGQKKVGVEEGPKFLEKLGFMNVLEQVAKSVNKKTITEPKTPQELGVTNARNLNEVESVNIELRDTIAKEYDVNNLLINIGGDHSIGLGTIAGVVKAMKPNARVGVVWFDAHPDMNTPENSPSGNIHGMPLACAVGLGPQRLTSIMPHYITPKDIMYVGIRSIDVGEQFEIQDKHIDHFTAEDVKRVGMKEVIEAINKKFVDYDVIHLSFDIDGIDPEFILGTGTPVPKGISLEDSLYFMSEMGKMKKLHSVDIVEYNPKIEEEITGKNVLKCISSLFGIKC
Protein: Patatin-like phospholipase domain-containing 6 (Patatin-like phospholipase domain-containing protein 6 isoform X3) (F1R844)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004643}; Single-pass type III membrane protein {ECO:0000256|ARBA:ARBA00004643}.
Interaction partners:
- Glycerophosphocholine phosphodiesterase 1
- Lecithin-cholesterol acyltransferase.
- Phospholipase A2, group XV.
- Membrane-bound O-acyltransferase domain-containing 2b
- Lysophospholipid acyltransferase 2
- Retinoic acid receptor responder 3-like
- Retinoic acid receptor responder 3
- Si:dkey-177p2.18.
- Si:ch211-214p16.3.
- Lysophospholipid acyltransferase 1
Sequence:
MGQSTSDTESAEPPETDRFGNIKSLVEDQLQTSMVVGIVIGAGVVIVLIAVLIFFVLRRMQLRKLEAQEVPKYRFRKRDKVLFYGRKIMRKVSQSTSSLVGATSSTRPRLKKKQKMLNIAKKILRFKKEVPTLQMKEPPPSVLEADLTEFDVANSHLPSEVLYMLKNVRVLGHFEKPLFLELCKHMVFLQFQQGEYVFRPGQPDSSIYVVQDGKLELCLTGQDGKDGVVKEVYPGDSVHSLLSILDVITGHQRPYKTVSARAAEVSTVLRLPVDAFLSIFEKYPESLVRVVQIIMVRLQRVTVLALHNYLGLTNELFSHEMQPRSSPLSPHPTRSSPVRHSKRFGSLTVPDKHREAAVQNATGGDHGKEGGTIPTLSRTISMPVDIAGMQKSLRSDFDMAYERGRISVSAEDGVPAFTKEQRERKVTVDEVPSGVYLYPEEESGMDIFSSFQGRPNATVFEEAQKEILRLMKIEDPSLLNGRVTFHHAKAGSVLARQGDQDVSLHFVLSGCLHVYQKMIDKQEAVCLFVTQPGEMVGQLAVLTGEPLIFTIKAERDCTFLKISKSEFYEIMREQPSVVLSAAHTVAIRMSAFVRQMDFAIDWMAVEAGRALYRQDDQSDCTYIVLNGRLRSVIRKANGKKELVGEYGRGDLIGVVEALTRQPRATTVHAVRDTELVKLPEGTLNNIKRRYPQVVTRLIHLLGQKILGNLQQPRGPFSSSALGLPSMASSPDVTNPASNLSTVAVLPVCDEVPINAFNLELSHALSAIGPTLLLTSDIIRERLGASALDSIHEYRLSGWLAQQEDINRIVLYQTDSGMTPWTQRCIRQADCILIVGLGDQEPALGELEQMLENTAVRALKQLILLHREDGPGPSRTVEWLNMRSWCSGHLHLKCPRRVFSRRSPTKLREVYEKVFEKTADRHSDFSRLARVLTGNSIALVLGGGGARGCSHVGVIKAMEDTGIPIDIVGGTSIGSFIGALYAEERSAVRVKQRAREWSKAMNSVFKTVLDLTYPITSMFSGSAFNTSISKVFEDKQIEDLWLPYFNVTTDITASAMRVHKDGSLWRYVRASMTLSGYLPPLCDPKDGNLLMDGGYINNLPADIARTLGTKTVIAIDVGSQDETDLCNYGDCLSGWWLLWKRINPWAEKVKVPDMAEIQSRLAYVSCVRQLELVKKSAYCEYIRPPIDRFKTMDFGKFDEIYDVGYQHGKLVFTEWARGDIIDNMLKDHRSADYNDSKKTDSCPCPSADFTDLAEIVSRIEPVQSYVGADEESDYATEYEEDGMDTVREEEGEEEEEEGEDPEDQSPGEWGPNGVFPPDEDKTVRQRKNVSRDPNADFSGVSDC
Protein: Forkhead box protein B1 (FoxB1) (Transcription factor FKH-5) (O93529)
Organism: Xenopus laevis (African clawed frog)
Function: Probable transcription factor. May be involved in the early anteroposterior patterning of the neuroectoderm.
Subcellular location: Nucleus {ECO:0000255, ECO:0000305}.
Interaction partners:
Sequence:
MPRPGRNTYSDQKPPYSYISLTAMAIQGSQEKMLPLSEIYKFIMDRFPYYRENTQRWQNSLRHNLSFNDCFIKIPRRPDQPGKGSFWALHPRCGDMFENGSFLRRRKRFKVMKSDHLAPSKASDAAQYLQQQAKLRLSALAASGTHLPPMSTYNLGVSPTSSFKHPFAIENIIAREYKMPGGLAFSTMQPMPAAYPLHNQLTTVGGSIGTGWPHMYSSSMLDSTTPISMANSDYSVSAYGVPIKPICHGAQTLLPAIPVPIKPTAALPALPTHIPAILSNSSPSMSPTSPQTATSQSSPATPSDTLTNPSTALLSVAVH
Protein: Peptidyl-tRNA hydrolase 2, mitochondrial (PTH 2) (EC 3.1.1.29) (Bcl-2 inhibitor of transcription 1) (Q9Y3E5)
Organism: Homo sapiens (Human)
Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:27184847}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- TLE family member 5
- Glutamyl-tRNA
- Voltage-gated monoatomic cation channel TMEM109
Sequence:
MPSKSLVMEYLAHPSTLGLAVGVACGMCLGWSLRVCFGMLPKSKTSKTHTDTESEASILGDSGEYKMILVVRNDLKMGKGKVAAQCSHAAVSAYKQIQRRNPEMLKQWEYCGQPKVVVKAPDEETLIALLAHAKMLGLTVSLIQDAGRTQIAPGSQTVLGIGPGPADLIDKVTGHLKLY
Protein: SBP (S-ribonuclease binding protein) family protein (Q8L7G9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- E3 ubiquitin-protein ligase RMA
- Probable E3 ubiquitin-protein ligase WAVH2
- Transmembrane protein
- Probable E3 ubiquitin-protein ligase RHY1A
- At1g14180/F7A19_27
- At3g29270
- Emb|CAB89385.1
- Putative defensin-like protein 227
- AT4G01090 protein
- At3g06890
Sequence:
MPLLSDNERIGLFSDSSMAIQAQHPSRFFFNNSNGQEASDCSLQPQDTPFTNFTKAGVDSRKRSREVYSSALMNPPPPKPSQVIDITELLQKTPNVVSTGLRLFHDQSQNQQQFFSSLPGDVTGKIKRQRDELDRFIQTQGEELRRTLADNRERRYVELLCAAEEIVGRKLRKKEAELEKATRRHAELEARVAHIVEEARNWQLRAATREAEVSSLHAHLQQAIANRLDTAAKQSTFGEDGGDAEEAEDAESVYVDPERIELIGPSCRICRRKSATVMALPCQHLILCNGCDVGAVRVCPICLAVKTSGVEVLF
Protein: Sorting nexin 1 (AtSNX1) (Vacuolar protein sorting-associated protein 5 homolog) (Q9FG38)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in vesicular protein sorting. Acts at the crossroads between the secretory and endocytic pathways. Is involved in the endosome to vacuole protein transport via its interaction with the BLOS1/2 proteins and, as component of the membrane-associated retromer complex, is also involved in endosome-to-Golgi retrograde transport. Required for the auxin-carrier protein PIN2 sorting to the lytic vacuolar pathway and the trafficking of several plasma membrane proteins. Also involved in the efficient sorting of seed storage protein globulin 12S.
Subcellular location: Cytoplasm. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Prevacuolar compartment membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- CLIP-associated protein
- Vacuolar protein sorting-associated protein 26A
- Vacuolar protein sorting-associated protein 35C
- Vacuolar protein sorting-associated protein 35A
- Sorting nexin 2A
- Vacuolar protein sorting-associated protein 35B
- Sorting nexin 2B
- Vacuolar protein sorting-associated protein 26B
- Sorting nexin
Sequence:
MESTEQPRNISGSMQSPRSPSSHPYLSVSVTDPVKLGNGVQAYISYRVITKTNLPEYQGPEKIVIRRYSDFVWLRDRLFEKYKGIFIPPLPEKSAVEKFRFSAEFIEMRRAALDIFVNRIALHPELQQSEDLRTFLQADEETMDRFRFQETSIFKKPADLMQMFRDVQSKVSDAVLGKEKPVEETTADYEKLKHYIFELENHLTEAQKHAYRLVKRHRELGQSLLDFGKAVKLLGACEGEPTGKAFSDLGTKSELLSIKLQKEAQQVLMNFEEPLKDYVRYVQSIKATIAERGTAFKQHCELSETTKLKEINLDKLMLTRSDKVGEAEIEYREIKAESEEATRRFERIVKRMEDEIVRFQEQKTEEMGVAFHQFAKGQARLANSVADAWRSLLPKLEASYSV
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (Q38DA6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU365079}; Single-pass membrane protein {ECO:0000256|RuleBase:RU365079}.
Interaction partners:
Sequence:
MGYRLLRDNVFKASCAKDSDELRARREPTMLYKEDQLVAPASGTERRYTLVLDLDETVIYAREGPLYARAYLKELLSFIRKNFEVIVWTAGEREYAECILEEINIRNTVRHLIHRHKTWFSFDDYTKDLTKLGRNLDYVIIIENSPDCVRTNPQNGIIVDDFRVSQTPPMEEAEAAWEGDGNNRERKAGSRSDSKTRRQVTDRTLLLLREVLKAMVESGETVPDFLAKCPLLTQRRVIGSDGSQIQTYHLGTRRKRGIPQLCASSPKRRRVTKESAPGATCTS
Protein: Serine/threonine-protein kinase PCRK2 (EC 2.7.11.1) (Protein PTI-COMPROMISED RECEPTOR-LIKE CYTOPLASMIC KINASE 2) (Q9LZF8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions redundantly with PCRK1 in basal resistance against bacterial pathogens and in regulation of plant immunity. Functions together with PCRK1 downstream of the pathogen-associated molecular pattern (PAMP) receptor FLS2. Contributes to the induction of SARD1 and CBP60G, which are transcriptional activator of ICS1, an enzyme involved in salicylate (SA) biosynthesis upon pathogen attack.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27208222}; Peripheral membrane protein {ECO:0000305|PubMed:27208222}.
Interaction partners:
- Transmembrane protein
- Histone-lysine N-methyltransferase SETD1B-like protein
- Probable sugar phosphate/phosphate translocator At2g25520
Sequence:
MKCFLFPLGDKKDEQRSPKPVSPTSNFSDVNKSGSDFSPRDVSGTSTVSSTGRNSNTSMSARENNLREFTIGDLKSATRNFSRSGMIGEGGFGCVFWGTIKNLEDPSKKIEVAVKQLGKRGLQGHKEWVTEVNFLGVVEHSNLVKLLGHCAEDDERGIQRLLVYEYMPNQSVEFHLSPRSPTVLTWDLRLRIAQDAARGLTYLHEEMDFQIIFRDFKSSNILLDENWTAKLSDFGLARLGPSPGSSHVSTDVVGTMGYAAPEYIQTGRLTSKSDVWGYGVFIYELITGRRPLDRNKPKGEQKLLEWVRPYLSDTRRFRLIVDPRLEGKYMIKSVQKLAVVANLCLTRNAKARPKMSEVLEMVTKIVEASSPGNGGKKPQLVPLKSQETSRVEEGKNKKVLDGAEGGWLEKLWNPKNVRAC
Protein: RNA-editing ligase 1, mitochondrial (RNA ligase 1) (EC 6.5.1.3) (P86926)
Organism: Trypanosoma brucei brucei
Function: Essential for RNA editing. RNA editing in kinetoplastid mitochondria inserts and deletes uridylates at multiple sites in pre-mRNAs as directed by guide RNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11134327, ECO:0000269|PubMed:19465686}.
Interaction partners:
Sequence:
MQLQRLGAPLLKRLVGGCIRQSTAPIMPCVVVSGSGVFLTPVRTYMPLPNDQSDFSPYIEIDLPSESRIQSLHKSGLAAQEWVACEKVHGTNFGIYLINQGDHEVVRFAKRSGIMDPNENFFGYHILIDEFTAQIRILNDLLKQKYGLSRVGRLVLNGELFGAKYKHPLVPKSEKWCTLPNGKKFPIAGVQIQREPFPQYSPELHFFAFDIKYSVSGAEEDFVLLGYDEFVEFSSKVPNLLYARALVRGTLDECLAFDVENFMTPLPALLGLGNYPLEGNLAEGVVIRHVRRGDPAVEKHNVSTIIKLRCSSFMELKHPGKQKELKETFIDTVRSGALRRVRGNVTVISDSMLPQVEAAANDLLLNNVSDGRLSNVLSKIGREPLLSGEVSQVDVVLMLAKDALKDFLKEVDSLVLNTTLAFRKLLITNVYFESKRLVEQKWKELMQEEAAAQSEAIPPLSPAAPTKGE
Protein: Probable cytochrome b5 1 (O94391)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Lanosterol 14-alpha demethylase erg11
- NADH-cytochrome b5 reductase 1
- C-22 sterol desaturase ERG5
- Uncharacterized FAD-binding protein C17H9.12c
- NADPH--cytochrome P450 reductase
- Putative lipase atg15
Sequence:
MSVKYFEPEEIVEHNNSKDMYMVINGKVYDVSNFADDHPGGLDIMLDYAGQDATKAYQDIGHSIAADELLEEMYIGDLKPGTEERLKELKKPRSFDNDTPPLPLLIALIVLPAIAVIVFVKLNK
Protein: Endolysin LysK (D-alanyl-glycyl endopeptidase) (EC 3.4.22.-) (N-acetylmuramoyl-L-alanine amidase) (EC 3.5.1.28) (Q6Y7T6)
Organism: Staphylococcus phage K
Interaction partners:
Sequence:
MAKTQAEINKRLDAYAKGTVDSPYRVKKATSYDPSFGVMEAGAIDADGYYHAQCQDLITDYVLWLTDNKVRTWGNAKDQIKQSYGTGFKIHENKPSTVPKKGWIAVFTSGSYEQWGHIGIVYDGGNTSTFTILEQNWNGYANKKPTKRVDNYYGLTHFIEIPVKAGTTVKKETAKKSASKTPAPKKKATLKVSKNHINYTMDKRGKKPEGMVIHNDAGRSSGQQYENSLANAGYARYANGIAHYYGSEGYVWEAIDAKNQIAWHTGDGTGANSGNFRFAGIEVCQSMSASDAQFLKNEQAVFQFTAEKFKEWGLTPNRKTVRLHMEFVPTACPHRSMVLHTGFNPVTQGRPSQAIMNKLKDYFIKQIKNYMDKGTSSSTVVKDGKTSSASTPATRPVTGSWKKNQYGTWYKPENATFVNGNQPIVTRIGSPFLNAPVGGNLPAGATIVYDEVCIQAGHIWIGYNAYNGNRVYCPVRTCQGVPPNQIPGVAWGVFK
Protein: ER degradation-enhancing alpha-mannosidase-like protein 1 (EC 3.2.1.24) (P38888)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Alpha-1,2-specific exomannosidase involved in endoplasmic reticulum-associated degradation (ERAD). Delivers misfolded glycoproteins to proteasomes. Forms a complex with PDI1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:11254655, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein OS-9 homolog
- Protein disulfide-isomerase
- Calnexin homolog
- Putative endoplasmic reticulum mannosidase MNL2
- Protein RER1
- ERAD-associated E3 ubiquitin-protein ligase HRD1
- ERAD-associated E3 ubiquitin-protein ligase component HRD3
- Degradation in the endoplasmic reticulum protein 1
- Alpha-mannosidase
- Endoplasmic reticulum chaperone BiP
Sequence:
MVCCLWVLLALLLHLDHVACEDDAYSFTSKELKAYKQEVKELFYFGFDNYLEHGYPYDEVKPISCVPKKRNFEDPTDQGTNDILGNFTITLIDSLTTIAILEDRPQFLKAVRLVERTFPDGNFDIDSTIQVFEITIRVIGSLLSSHLYATDPTKAVYLGDDYDGSLLRLAQNMADRLLPAYLTSTGLPMPRRNIKRKWDVSEFPEFLETENNVAAMASPMFEFTILSYLTGDPKYEKVTRYAFDKTWSLRTGLDLLPMSFHPEKLTPYTPMTGIGASIDSLFEYALKGAILFDDSELMEVWNVAYEALKTNCKNDWFFANVMADTGHLFVPWIDSLSAFFSGLQVLAGDLDDAIANHLMFLKMWNTFGGIPERWNFSPPEFPPLSPLERSGAVALDNILPLEWYPLRPEFFESTYFLYRATKDPFYLNIGVHLLKDLKQRFKSNCGFAGFQNVITGELQDRMETFVLSETLKYLYLLFDEENELHNSASDVIFSTEAHPMWLPQEVRSNYKRNAKFNNSVYSSHLEICQKKDREQAGENTLSQRIVGFAKSIFHKGPPDEEATDPIIDYTIDTELPGTCSIKPHHVIGDEFWYSPMLSNFDRLFEIDSRFAATLIKPSHMHNYNAIELEPGFYNRWSNPQFSTCLIPPTTEIFELLFDLPGYHQLNPLMLENKTITFETFGGRSRLKIEKLQIYQIDYYGDLITASTFQDVSRKDIFSNACDAVASLYSPTYLYRVVAINGRILPRHGSVQIKKHSPVLTSNGTREEDEFKMDGIGINDHSQLMLECTPIINLFIV
Protein: Cytochrome P450 3A43 (EC 1.14.14.1) (Q9HB55)
Organism: Homo sapiens (Human)
Function: Exhibits low testosterone 6-beta-hydroxylase activity.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
Sequence:
MDLIPNFAMETWVLVATSLVLLYIYGTHSHKLFKKLGIPGPTPLPFLGTILFYLRGLWNFDRECNEKYGEMWGLYEGQQPMLVIMDPDMIKTVLVKECYSVFTNQMPLGPMGFLKSALSFAEDEEWKRIRTLLSPAFTSVKFKEMVPIISQCGDMLVRSLRQEAENSKSINLKDFFGAYTMDVITGTLFGVNLDSLNNPQDPFLKNMKKLLKLDFLDPFLLLISLFPFLTPVFEALNIGLFPKDVTHFLKNSIERMKESRLKDKQKHRVDFFQQMIDSQNSKETKSHKALSDLELVAQSIIIIFAAYDTTSTTLPFIMYELATHPDVQQKLQEEIDAVLPNKAPVTYDALVQMEYLDMVVNETLRLFPVVSRVTRVCKKDIEINGVFIPKGLAVMVPIYALHHDPKYWTEPEKFCPERFSKKNKDSIDLYRYIPFGAGPRNCIGMRFALTNIKLAVIRALQNFSFKPCKETQIPLKLDNLPILQPEKPIVLKVHLRDGITSGP
Protein: Nuclear pore complex protein Nup98-Nup96 (A0A0R4IAQ8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004620}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004620}; Nucleoplasmic side {ECO:0000256|ARBA:ARBA00004620}. Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567}.
Interaction partners:
Sequence:
MFNKSFGAPFGGGTGGFGTSSTFGQPNSGFGATPGGFGSSAFGTTNNTGGLFGNTQNKPGGLFGSSTFSQPVTSSTSSGFGFGATSGTSNSLFGSTNTGGGGLFSQQNNAFGANKPAAFGNFGTSTSSGGLFGTTNTASNPFGGTSGSLFGSSSFTAAPPGTTIKFNPPTGSDTMVKGGVTTSINTKHQCITAMKEYENKSLEELRLEDYQAGRKGPSNLPMAAGTGGLFGAAAPATPSTGTGLFGSSAPNTGFNFGQNKTTFGTSTGAFGTTTGSLFAQPQQQQQQQQQNSSLFKPFGSATTTQNNTFSFGNTSSMQGLFANTAASQAGGLFGNTNTSTATGFGTGIFGQTNTGFGNVGTQNLFGNKPAGFGTTTTSAPSFGSGPGLFANKPTLTLGTNTNTSTFGFSGTGAGGGLFGNKTAATGLGPVLGAGFGAGVGTGQTSLFGNNQKLGSTLGSVGTFGAGGFNTGASTLNFGAPQQPIALTDPSAGAAQQAVLQQQISALAYSPFGDSPLFRNPLSDPKKKEERLKPTNPAAQKALTTPTQYKLTPRPATRVRPKALSSSGSSKSQLFDGLDDDELSLNNGAFMPRKSIKKLVLKNLNNSSLYNNSLNREADDLASPSEYPQNGLSLSLDEGEPREANMERRGEDDLEVSKFYTNPITKPIPHAQLSPLLQDTISEFNMRGSGSHRNGLEASSEDLSLAEDSIQEERDEELEAQKPPHPAGIVLSRVGYYTIPSMEELGKMLNENGECIVENFTIGRKGYGSVFFPGEVNLTNMILDEIVHFRRKEIIVYPDDKDKPPVGEGLNRRAEVTLDGVWPNDKTTCCQIKSPDRLTEMNYEGRLEAASRKQGARFLEYRPETGSWVFEVAHFSKYGLQESDEEEEISPAKLDLKKLKTAVPPGLAQLPLTQQQGAPQAQSTAVLELLSRVSELDSDMADITQEHPVESILDDEDGERTSFEENKLRSETPAENEPVSASSQIASSMGINPHTLQIMKASLFADDDECDMFQEHVSSKLIQDVASTKLLLSGAGRPSIGALLQNKFTSGGGLFSQLPEVPFSGISQKLNKSLASEAAWPSLGPSFLLPPPPPEPTLRTVGARRLGGPVPLEASITLGKGRLLMDAALFRGRSFRVGWGPNWTLVHSGDQLSVTHPVKEPAAENLGFGFLPKPTKTKPITESPFKVRVEQVVGLEPKQSSESLSLYLRPLEIGLKHSTINTEEPCPFIQPAGGVDALHGYAEWIVEVNKDIGGSDAGLAHWKQVWTLCAALWGRLGDRDLDTEQYSDYQQQLERRRSFSHWLSDCAANCIEEEVGRALQRSHAEAVFSYLTGHCISKACKLSQKSGDHRLSLMLSQAVGSQFCRDLLALQLTDWNRMQTDSFIEEERLRIFALLAGKPVWQSTDCCINVCSELDWKRCVAVHLWYMLPPTASVADALTKYETAFQGSEEVKRYAGPPLPPYIDELELLGLDEDMDEIDSKKPLYDICFHLLKLYSDRHYSLQQLLDPSTVTADHLDYRLSWHLWSVLQALNYNHLATSCQGLLHASYAAQLESAGLWEMAIFVLLHITDSGRRESAVREMLSLHCSLEETEESMEKEQFLTEKLLIPIQWIHQAKAIRACREGDKHREALHLYKAGHWNHCHRLVIQHLASDCIINDNHKYLLDFLEGLAVPERSVQIQGWDTSGRVFLDYIHVIQTLQDIQQMESPGYELERLHTEVTSLCNRIVLLPCSKAKDKLAQSEMAKRVANILRVVLSLQQGGEGTPDSQYIPLCQLASHIGRLPMPEDYALEELRSLTNSYMQEYVISH