wanglab/gogpt-training-data huggingface dataset:
Protein: Bengalin (P0CC11)
Organism: Deccanometrus bengalensis (Indian black scorpion) (Heterometrus bengalensis)
Function: Toxin that shows cardiotoxicity on isolated guinea pig heart and auricle and neurotoxicity on isolated rat phrenic nerve diaphragm. Shows antiosteoporosis activity in experimental rats. Also induces apoptosis against human leukemic cells (U937 and K562). Has no effect on normal human lymphocytes. Apoptosis has been evidenced from damaged nuclei, cell cycle arrest at sub G1 phase, increase of early apoptotic cells, augmentation of DNA fragmentation and also a reduction of telomerase activity. Also elicits loss of mitochondrial membrane potential (MMP) which induces cytochrome c release in cytosol, decreases heat shock protein (HSP) 70 and 90 expression, activates caspase-9, caspase-3, induces poly (ADP-ribose) polymerase (PARP) cleavage, and up-regulates caspase-3.
Subcellular location: Secreted {ECO:0000269|PubMed:19800909, ECO:0000269|PubMed:19913524}.
Interaction partners:
Sequence:
GPLTILHINDVHAAFEQFNT
Protein: NADP-dependent malic enzyme (NADP-ME) (EC 1.1.1.40) (Malic enzyme 1) (P13697)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the oxidative decarboxylation of (S)-malate in the presence of NADP(+) and divalent metal ions, and decarboxylation of oxaloacetate.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:2416344}.
Interaction partners:
- Pyruvate carboxylase, mitochondrial
- Fumarate hydratase, mitochondrial
- Malate dehydrogenase, mitochondrial
- Malate dehydrogenase, cytoplasmic
- Pyruvate kinase PKM
- Pyruvate kinase PKLR
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- L-lactate dehydrogenase A chain
- Citrate synthase, mitochondrial
- L-lactate dehydrogenase C chain
Sequence:
MDPRAPRRRHTHQRGYLLTRDPHLNKDLAFTLEERQQLKIHGLLPPCIVNQEIQVLRVIKNFERLNSDFDRYLLLMDLQDRNEKLFYSVLMSNVEKFMPIVYTPTVGLACQQYSLAFRKPRGLFISIHDKGHIASVLNAWPEDVVKAIVVTDGERILGLGDLGCNGMGIPVGKLALYTACGGVNPQQCLPITLDVGTENEELLKDPLYIGLRHRRVRGPEYDAFLDEFMEAASSKYGMNCLIQFEDFANLNAFRLLNKYRNKYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQTVLFQGAGEAALGIAHLIVMAMEKEGLSKEKARQKIWLVDSKGLIVKGRASLTEEKEVFAHEHEEMKNLEAIVQKIKPTALIGVAAIGGAFTEQILKDMAAFNERPIIFALSNPTSKAECSAEECYKVTKGRAIFASGSPFDPVTLPDGRTLFPGQGNNSYVFPGVALGVVACGLRHINDSVFLTTAEVISQQVSDKHLEEGRLYPPLNTIRDVSLKIAVKIVQDAYKEKMATVYPEPQNKEEFVSSQMYSTNYDQILPDCYSWPEEVQKIQTKVNQ
Protein: Protein Abitram (Actin-binding transcription modulator) (Protein Simiate) (Q9NX38)
Organism: Homo sapiens (Human)
Function: Actin-binding protein that regulates actin polymerization, filopodia dynamics and increases the branching of proximal dendrites of developing neurons.
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q80ZQ9}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q80ZQ9}. Nucleus {ECO:0000250|UniProtKB:Q80ZQ9}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q80ZQ9}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q80ZQ9}. Note=Localizes to somata and dendrites in cortical neurons (By similarity). Colocalizes with G- and F-actin in lamellipodia (By similarity). Colocalizes in the nucleus with PTK2 (By similarity). {ECO:0000250|UniProtKB:Q80ZQ9}.
Interaction partners:
- DOMON domain-containing protein FRRS1L
- Peroxisome assembly protein 26
- Peroxisomal ATPase PEX6
- Synaptojanin-2-binding protein
- tRNA pseudouridine synthase Pus10
Sequence:
MATEPEAAEPVVPSLVDRYFTRWYKPDVKGKFCEDHCILQHSNRICVITLAESHPVLQSGKTIKSISYQISTNCSRLQNKVSGKFKRGAQFLTELAPLCKIYCSDGEEYTVSSCVRGRLMEVNENILHKPSILQEKPSTEGYIAVVLPKFEESKSITEGLLTQKQYEEVMVKRINATTATS
Protein: V(D)J recombination-activating protein 1 (EC 2.3.2.27) (EC 3.1.-.-) (G3V6K9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00820, ECO:0000256|RuleBase:RU366024}.
Interaction partners:
- V
- T-cell surface glycoprotein CD4
- High mobility group protein B1
- High mobility group protein B1
- High mobility group box 1 like 5
- HMG box domain-containing protein
- High mobility group protein B1-like
- Uncharacterized protein.
- Receptor-type tyrosine-protein phosphatase C
- Forkhead box P3
Sequence:
MAVPLPSTLRLSSAPDEIQHPHIKFSEWKFKLFRVRSFEKAPEEAQKEKDSSEGKPCLEQSPVVLDKPGGQNSVLTQRALKLHPKFSKKFHVDGKSSDKAIHQARLRHFCRICGNHFKSDGHNRRYPVHGPVDAKTQSLFRKKEKRVTSWPDLIARVFRIDVKSDVDSIHPTEFCHNCWSIMHRKFGSAHSQVYCPRNVTVEWHPHTPSCDICFTAHRGLKRKRHQPNVQLSKKLKTVLNHARRDRRKRTQARVSSKEVMKKISNCSKIHLSTKLLAVDFPAHFVKSISCQICEHILADPVETTCKHLFCRICILRCLKVMGSYCPSCRYPCFPTDLQSPVKSFLSILNSLMVKCPAQECNEEVSLEKYNHHVSSHKESKETLVHINKGGRPRQHLLSLTRRAQKHRLRELKIQVKEFADKEEGGDVKSVCLTLFLLALRARNEHRQADELEAIMQGRGSGLQPAVCLAIRVNTFLSCSQYHKMYRTVKAITGRQIFQPLHALRNAEKVLLPGYHPFEWQPPLKNVSSRTDVGIIDGLSGLASSVDEYPVDTIAKRFRYDSALVSALMDMEEDILDGMRSQDLDDYVSGPFTVVVKESCDGMGDVSEKHGSGPAVPEKAVRFSFTVMRVTVEHGSQNVKIFEEPKPNSELCCKPLCLMLADESDHETLTAILSPLIAEREAMKSSELLLEMGGIPRTFKFIFRGTGYDEKLVREVEGLEASGSVYICTLCDATRLEASQNLVFHSITRSHAENLQRYEVWRSNPYHESVEELRDRVKGVSAKPFIETVPSIDALHCDIGNAAEFYKIFQLEIGEVYKNPNASKEERKRWQATLDKHLRKRMNLKPIMRMNGNFARKLMTQETVDAVCELIPSEERHEALRELMDLYLKMKPVWRSSCPAKECPESLCQYSFNSQRFAELLSTKFKYRYEGKITNYFHKTLAHVPEIIERDGSIGAWASEGNESGNKLFRRFRKMNARQSKCYEMEDVLKHHWLYTSKYLQKFMNAHNALKNSGFTMNSKETLGDSLDIEDSLESQDSMEF
Protein: Vascular endothelial growth factor receptor 3 (EC 2.7.10.1) (E9PD35)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU000311}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQRGAALCLRLWLCLGLLDGLVSGYSMTPPTLNITEESHVIDTGDSLSISCRGQHPLEWAWPGAQEAPATGDKDSEDTGVVRDCEGTDARPYCKVLLLHEVHANDTGSYVCYYKYIKARIEGTTAASSYVFVRDFEQPFINKPDTLLVNRKDAMWVPCLVSIPGLNVTLRSQSSVLWPDGQEVVWDDRRGMLVSTPLLHDALYLQCETTWGDQDFLSNPFLVHITGNELYDIQLLPRKSLELLVGEKLVLNCTVWAEFNSGVTFDWDYPGKQAERGKWVPERRSQQTHTELSSILTIHNVSQHDLGSYVCKANNGIQRFRESTEVIVHENPFISVEWLKGPILEATAGDELVKLPVKLAAYPPPEFQWYKDGKALSGRHSPHALVLKEVTEASTGTYTLALWNSAAGLRRNISLELVVNVPPQIHEKEASSPSIYSRHSRQALTCTAYGVPLPLSIQWHWRPWTPCKMFAQRSLRRRQQQDLMPQCRDWRAVTTQDAVNPIESLDTWTEFVEGKNKTVSKLVIQNANVSAMYKCVVSNKVGQDERLIYFYVTTIPDGFTIESKPSEELLEGQPVLLSCQADSYKYEHLRWYRLNLSTLHDAHGNPLLLDCKNVHLFATPLAASLEEVAPGARHATLSLSIPRVAPEHEGHYVCEVQDRRSHDKHCHKKYLSVQALEAPRLTQNLTDLLVNVSDSLEMQCLVAGAHAPSIVWYKDERLLEEKSGVDLADSNQKLSIQRVREEDAGRYLCSVCNAKGCVNSSASVAVEGSEDKGSMEIVILVGTGVIAVFFWVLLLLIFCNMRRPAHADIKTGYLSIIMDPGEVPLEEQCEYLSYDASQWEFPRERLHLGRVLGYGAFGKVVEASAFGIHKGSSCDTVAVKMLKEGATASEHRALMSELKILIHIGNHLNVVNLLGACTKPQGPLMVIVEFCKYGNLSNFLRAKRDAFSPCAEKSPEQRGRFRAMVELARLDRRRPGSSDRVLFARFSKTEGGARRASPDQEAEDLWLSPLTMEDLVCYSFQVARGMEFLASRKCIHRDLAARNILLSESDVVKICDFGLARDIYKDPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLRDGTRMRAPELATPAIRRIMLNCWSGDPKARPAFSELVEILGDLLQGRGLQEEEEVCMAPRSSQSSEEGSFSQVSTMALHIAQADAEDSPPSLQRHSLAARYYNWVSFPGCLARGAETRGSSRMKTFEEFPMTPTTYKGSVDNQTDSGMVLASEEFEQIESRHRQESGFRGTRRTRGA
Protein: Cysteine dioxygenase CDG1 (CDO) (EC 1.13.11.20) (Q5A3Z5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Cysteine dioxygenase involved in sulfite formation from cysteine. Plays an important role in filamentous growth and virulence.
Interaction partners:
- Glutamate decarboxylase
- Cystathionine beta-lyase
- cystathionine gamma-lyase
- Cysteine synthase
- Cysteine synthase 1
- Sulfite efflux pump SSU1
- Homocysteine/cysteine synthase
- Transaminase A
- Glutamate decarboxylase
- Aspartate aminotransferase
Sequence:
MLLNQYTFSAERCTTPTSISHPPLACPTSPPPTNSLNRYQHKPVTLAPTVDHGCEINGTTIDCIPKDSKFYQLIMDLKQLLAGKGLSNEDIDVEKVKQLMADYDSNEIDWQHLALHDPSRNYSRNGIINLNGNANLLILVWSPGKSSAIHDHADAHCCVKMLAGELIEHLYDFPDHEGEELQCRQETSMKRNDVGYINDSIGLHKMSNPLQNRVSVSLHLYTPPYASMYGCSMYEASSGRKHHVDMSKYYSWQGQLVNEKESSTC
Protein: Non-selective voltage-gated ion channel VDAC3 (E5RJN6)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}.
Interaction partners:
Sequence:
MCNTPTYCDLGKAAKDVFNKGYGFGMVKIDLKTKSCSGVEFSTSGHAYTDTGKASGNLETKYKVCNYGLTFTQKWNTDNTLGTEISWENKLAEGLKLTLDTIFVPNTGKKSGKLKASYKRDCFSVGSNVDIDFSGPTIYGWAVLAFEGWLAGYQMSFD
Protein: Histone H1 (Putative histone H1 protein) (P94109)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU003894}.
Interaction partners:
- Histone H4
- Replication protein A 32 kDa subunit A
- Replication protein A 32 kDa subunit B
- RNA-binding
- F-box/LRR-repeat protein At1g52650
- Putative F-box protein At1g59675
- At5g38760 family protein)
- Telomere repeat-binding factor 2
- ARM repeat superfamily protein
- ARM repeat superfamily protein
Sequence:
MAEDKILKKTPAAKKPRKPKTTTHPPYFQMIKEALMVLKEKNGSSPYAIAKKIEEKHKSLLPESFRKTLSLQLKNSVAKGKLVKIRASYKLSDTTKMITRQQDKKNKKNMKQEDKEITKRTRSSSTRPKKTVSVNKQEKKRKVKKARQPKSIKSSVGKKKAMKASAA
Protein: Ceramide glucosyltransferase (EC 2.4.1.80) (GLCT-1) (Glucosylceramide synthase) (GCS) (Glycosylceramide synthase) (UDP-glucose ceramide glucosyltransferase) (UDP-glucose:N-acylsphingosine D-glucosyltransferase) (Q16739)
Organism: Homo sapiens (Human)
Function: Participates in the initial step of the glucosylceramide-based glycosphingolipid/GSL synthetic pathway at the cytosolic surface of the Golgi. Catalyzes the transfer of glucose from UDP-glucose to ceramide to produce glucosylceramide/GlcCer (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine). GlcCer is the core component of glycosphingolipids/GSLs, amphipathic molecules consisting of a ceramide lipid moiety embedded in the outer leaflet of the membrane, linked to one of hundreds of different externally oriented oligosaccharide structures. Glycosphingolipids are essential components of membrane microdomains that mediate membrane trafficking and signal transduction, implicated in many fundamental cellular processes, including growth, differentiation, migration, morphogenesis, cell-to-cell and cell-to-matrix interactions (By similarity). They are required for instance in the proper development and functioning of the nervous system (By similarity). As an example of their role in signal transduction, they regulate the leptin receptor/LEPR in the leptin-mediated signaling pathway (By similarity). They also play an important role in the establishment of the skin barrier regulating keratinocyte differentiation and the proper assembly of the cornified envelope (By similarity). The biosynthesis of GSLs is also required for the proper intestinal endocytic uptake of nutritional lipids (By similarity). Catalyzes the synthesis of xylosylceramide/XylCer (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) using UDP-Xyl as xylose donor.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12873973}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R0E0}.
Interaction partners:
- Lysosomal acid glucosylceramidase
- Beta-1,4-galactosyltransferase 6
- Ceramide kinase
- Non-lysosomal glucosylceramidase
- Sphingomyelin phosphodiesterase 2
- Ceramide synthase 6
- Sphingolipid delta
- Acid ceramidase
- Ceramide synthase 2
- Sphingomyelin phosphodiesterase
Sequence:
MALLDLALEGMAVFGFVLFLVLWLMHFMAIIYTRLHLNKKATDKQPYSKLPGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMPGYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEKVGLVHGLPYVADRQGFAATLEQVYFGTSHPRYYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRGWRFAMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVASLIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMTIYIFLSALWDPTISWRTGRYRLRCGGTAEEILDV
Protein: BHLH protein-like (Q69TX2)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEFDMAMDMMSQEQLMHIISQLDSALASSPSPSTSPSASPPRQSPAAHVPVPPGLLNTTMVSTSRAQAAPSAPLHPVAATAAVQSSSRGIMYTTTRQGVIDAAEEEEAAAPRPRRRNARVSSEPQSVAARLRRERVSQRMRALQRLVPGGARLDTASMLEEAIRYVKFLKGHVQSLERAAAALHMHGGHAAAAGFAGDAGDAVYSCPSYYA
Protein: Max dimerization protein 4 (Max dimerizer 4) (Max-associated protein 4) (Max-interacting transcriptional repressor MAD4) (Q60948)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor. Binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. Antagonizes MYC transcriptional activity by competing for MAX and suppresses MYC dependent cell transformation.
Subcellular location: Nucleus.
Interaction partners:
- Protein max
- MLX-interacting protein
Sequence:
MELNSLLLLLEAAEYLERRDREAEHGYASMLPFDGDFARKKTKTAGLVRKGPNNRSSHNELEKHRRAKLRLYLEQLKQLGPLGPDSTRHTTLSLLKRAKMHIKKLEEQDRRALSIKEQLQREHRFLKRRLEQLSVQSVERVRTDSTGSAVSTDDSEQEVDIEGMEFGPGELDSAGSSSDADDHYSLQSSGCSDSSYGHPCRRPGCPGLS
Protein: DnaJ homolog subfamily C member 5 (Cysteine string protein) (CSP) (P60905)
Organism: Rattus norvegicus (Rat)
Function: Acts as a general chaperone in regulated exocytosis (By similarity). Acts as a co-chaperone for the SNARE protein SNAP-25 (By similarity). Involved in the calcium-mediated control of a late stage of exocytosis (By similarity). May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q29455}. Membrane {ECO:0000250|UniProtKB:Q29455}; Lipid-anchor {ECO:0000250|UniProtKB:Q29455}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane {ECO:0000250|UniProtKB:Q29455}. Melanosome {ECO:0000250|UniProtKB:Q9H3Z4}. Cell membrane {ECO:0000250|UniProtKB:Q9H3Z4}. Note=The association with membranes is regulated by palmitoylation. {ECO:0000250|UniProtKB:Q29455}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Synaptotagmin-1
- Heat shock cognate 71 kDa protein
- Vesicle-associated membrane protein 2
- Ras-related protein Rab-3A
- Vesicular inhibitory amino acid transporter
- Tuftelin-interacting protein 11
- WD repeat-containing protein 7
- Cell division cycle 5-like protein
- Heat shock 70 kDa protein 1A
Sequence:
MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEINNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVVCGLLTCCYCCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATETTQLTADSHPSYHTDGFN
Protein: Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) (P35748)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Muscle contraction.
Subcellular location: Melanosome {ECO:0000250}. Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Actin gamma 2, smooth muscle
- Actin, aortic smooth muscle
- Myosin light chain 9
- Uncharacterized protein
- EF-hand domain-containing protein
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- EF-hand domain-containing protein
- Myosin regulatory light chain 11
- Myosin light chain 10
- Actin beta
Sequence:
MAQKGQLSDDEKFLFVDKNFINSPVAQADWVAKRLVWVPSEKQGFEAASIKEEKGDEVVVELVENGKKVTVGKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKQLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAREERTFHIFYYLIAGAKEKMRNDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMSIMGFSEEEQLSVLKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIMAFQAMCRGYLARKAFAKRQQQLTAMKVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKEDELQKIKERQQKAESELQELQQKHTQLSEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKMDGEASDLHEQIADLQAQIAELKMQLAKKEEELQAALARLEDETSQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDTTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQVVEELTEQLEQFKRAKANLDKTKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLSEAEGKAIKLAKEVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQEQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVESLEEGKKRFQKEIESLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKVQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLLKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELKSKLQEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAAAKALKQRDKKLKEMLLQVEDERKMAEQYKEQAEKGNAKVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNETSFVPTRRSGGRRVIENADGSEEEVDARDADFNGTKSSE
Protein: DAN domain family member 5 (Cerberus-like protein 2) (Cerl-2) (Q76LW6)
Organism: Mus musculus (Mouse)
Function: Seems to play a role in the correct specification of the left-right axis. May antagonize NODAL and BMP4 signaling. Cystine knot-containing proteins play important roles during development, organogenesis, and tissue growth and differentiation.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MFRSQFTTLLGLFSGAWLPTGSGRPGAPATPVQSGTAINQSWTLDPLVPISALGSWEAFLGLQNKQQGTGELQGGGQRVAAGVPLPLAPQEVLQETCKALSFVQVISRPGCTSARVLNHLCFGRCSSFYIPSSDPTPVVFCNSCVPARKRWTSVTLWCGAGQLASPRRVRISTVLVQKCQCRPKL
Protein: Endoplasmic reticulum oxidoreductin-1 (EC 1.8.4.-) (Q9C7S7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI to transfer oxidizing equivalent. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:13678526}; Peripheral membrane protein {ECO:0000269|PubMed:13678526}; Lumenal side {ECO:0000269|PubMed:13678526}.
Interaction partners:
- Protein disulfide isomerase-like 1-3
- Protein disulfide isomerase-like 1-1
- Protein disulfide isomerase-like 1-4
- Protein disulfide isomerase-like 1-2
- Protein disulfide-isomerase 2-3
- Protein disulfide-isomerase like 2-1
- Protein disulfide-isomerase 5-2
- Sulfhydryl oxidase 1
- Sulfhydryl oxidase 2
- Endoplasmic reticulum oxidoreductin-2
Sequence:
MGKGAIKEEESEKKRKTWRWPLATLVVVFLAVAVSSRTNSNVGFFFSDRNSCSCSLQKTGKYKGMIEDCCCDYETVDNLNTEVLNPLLQDLVTTPFFRYYKVKLWCDCPFWPDDGMCRLRDCSVCECPENEFPEPFKKPFVPGLPSDDLKCQEGKPQGAVDRTIDNRAFRGWVETKNPWTHDDDTDSGEMSYVNLQLNPERYTGYTGPSARRIWDSIYSENCPKYSSGETCPEKKVLYKLISGLHSSISMHIAADYLLDESRNQWGQNIELMYDRILRHPDRVRNMYFTYLFVLRAVTKATAYLEQAEYDTGNHAEDLKTQSLIKQLLYSPKLQTACPVPFDEAKLWQGQSGPELKQQIQKQFRNISALMDCVGCEKCRLWGKLQVQGLGTALKILFSVGNQDIGDQTLQLQRNEVIALVNLLNRLSESVKMVHDMSPDVERLMEDQIAKVSAKPARLRRIWDLAVSFW
Protein: Hydrogenase maturation factor HybF (Hydrogenase nickel incorporation protein HybF) (Hydrogenase-2 operon protein HybF) (P0A703)
Organism: Escherichia coli (strain K12)
Function: Involved in the maturation of [NiFe] hydrogenases. Required for nickel insertion into the metal center of the hydrogenase. HybF is involved in maturation of hydrogenases 1 and 2. It may partially substitute for the function of HypA and vice versa.
Interaction partners:
- Hydrogenase maturation factor HybG
- Hydrogenase-2 operon protein HybE
- Hydrogenase-2 large chain
- Hydrogenase 2 maturation protease
- Hydrogenase maturation factor HypB
- Hydrogenase maturation factor HypC
- Probable Ni/Fe-hydrogenase 2 b-type cytochrome subunit
- Hydrogenase maturation factor HypD
- Hydrogenase-2 small chain
- Carbamoyl dehydratase HypE
Sequence:
MHELSLCQSAVEIIQRQAEQHDVKRVTAVWLEIGALSCVEESAVRFSFEIVCHGTVAQGCDLHIVYKPAQAWCWDCSQVVEIHQHDAQCPLCHGERLRVDTGDSLIVKSIEVE
Protein: Slowpoke 2, isoform H (A0A0B4K738)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSRLIQPRYRFRDLLLGDFSFNDDGERVRVEYYVNENTFKERLQLYFIKNQRSSLRIRIADLFLKLLSCVLYIIRVILDKNPTFITCYGCEVGNKTEFIISAKLTEEEFQENPIINWDAILWVNRPTVLWVLQLLLAMVSLTQSLVLTYLGYKGNIWQQILSFHFILELVTTIPFALTIVHPPLRNLFIPIFLNCWLAKRSLENMFNDLHRAMQKSQSALSQQLTILSATLLCLVFTSVCGIQHFQRAGHRHLNLFQSTYYVVVTFSTVGYGDFVPDIWPSQLYMVIMICVALIVLPTQFEQLAFTWMERQKLGGSYSSHRAQSEKHVVVCSTTLHADTIMDFLNEFYAHPLLQDFYVVLLSPMELDTTMRMILQVPIWAQRVIYIQGSCLKDGDLARARMNEAEACFILAARNYADKTAADEHTILRSWAVKDFAPNVPQYVQIFRPEHKLHVKFAEHVVCEDEFKYALLANNCTCPGASTLVTLLLHTSRGQEGQQSPEEWHRLYGKCSGNEIYHIVLGDSRFFGEYEGKSFTYASFHSHRKYGVALVGVRPAELPEFYEETILLNPGPRHIMKKDDTCYYMSITKEENSAFVVNQNQTSDPTAAAKEGSGTGGGGGASSSASHHHTAATASENPTAVIISDSRQNLKDTTVTQTAATITTTTLPPPPQTMGSPSMAGGSGGCGGGGLGLGSAHSMGTSLSITPATLTTTGNHLDVPFANNPNLLSPDVLNQRRGSRRPSILPVPDMFTSSSFSIAGNDDGEEGDESDDEIDDEMPWRSPSEKIAIVKGFPPVSPFIGVSPTLCYLLKEKKPLCCLQLAQVCEHCSYRNAKEYQWQNKTIILAADYASNGIYNFIIPLRAHFRSKTSLNPIILLLERRPDVAFLDALSYFPLVYWMLGSIDCLDDLLRAGITLAESVVVVNKELSNSAEEDSLSDCNTIVAVQNMFKFFPSIKSITELSQSSNMRFMQFRAHDKYALHLSKMEKREKERGSHISYMFRLPFAAGAVFSASMLDTLLYQAFVKDYVITFVRLLLGIDQAPGSGFLTSMRITKDDMWIRTYGRLYQKLCSTTCEIPIGIYRTQDTSNADTSHVSNSPVERWGPFSAFSRHCVRLRPSYSINLADEARDNHAQQIERAEIANLVRSRMESLNLPTIDYDDVSEKRNHLSYVIINPSCDLKLEEGDLIYLVRPSPFSAQKTFERHNSRRKSNISFCSNINLGATCGPQMPQMNMNMANTAVGAGSRRGSGIAGLNPMQMQSVQTLAGPTVVGNQRGRSNSLRIDNDILLRRSSSLRQGLPSVGVSHGRRKSSLEEIGISHFTTLMQATNHSNPIKISLNGSIGMENQISLQVTPPEEPTPMLGVPCMLGGGGGGGINPSGAGSSTGGMLGGGSSLAINTADLGPGPSTSSGASGSLQAQDSLGQQSSQVSSPQHLQGTIV
Protein: Porin thermoregulatory protein EnvY (P10805)
Organism: Escherichia coli (strain K12)
Function: Influences the temperature-dependent expression of several E.coli envelope proteins, most notably the porins OmpF and OmpC and the lambda receptor, LamB.
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator YbcM
Sequence:
MQLSSSEPCVVILTEKEVEVSVNNHATFTLPKNYLAAFACNNNVIELSTLNHVLITHINRNIINDYLLFLNKNLTCVKPWSRLATPVIACHSRTPEVFRLAANHSKQQPSRPCEAELTRALLFTVLSNFLEQSRFIALLMYILRSSVRDSVCRIIQSDIQHYWNLRIVASSLCLSPSLLKKKLKNENTSYSQIVTECRMRYAVQMLLMDNKNITQVAQLCGYSSTSYFISVFKAFYGLTPLNYLAKQRQKVMW