wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxisomal membrane protein import receptor PEX19 (Peroxin-19) (Q07418)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for proper post-translational import and stabilization of peroxisomal membrane proteins (PMPs). Acts as a cytosolic import receptor for PMPs and delivers them to the docking factor PEX3 at the peroxisomal membrane for subsequent insertion into the membrane. Acts as a chaperone in stabilizing or maintaining PMPs in the lipid bilayer. Directs PEX17, a peripheral component of the peroxisomal matrix protein translocation machinery, to peroxisomes. Stabilizes VPS1, a protein required for peroxisomal fission, at the peroxisomal membrane. Also acts in conjunction with PEX3 in the formation of peroxisomes from preperoxisomal compartments at the endoplasmic reticulum during de novo peroxisome synthesis, probably via the import of additional PMPs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16009135, ECO:0000269|PubMed:9418908}. Peroxisome membrane {ECO:0000269|PubMed:16009135}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16009135}. Note=Predominantly cytoplasmic (PubMed:9418908). Concentrates in a PEX3-dependent manner to defined foci on the endoplasmic reticulum membrane, which then bud off to form newly sythesized peroxisomes (PubMed:16009135). {ECO:0000269|PubMed:16009135, ECO:0000269|PubMed:9418908}.
Interaction partners:
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein PMP27
- Peroxisomal biogenesis factor 3
- Peroxisomal biogenesis factor 2
- Peroxisomal targeting signal receptor
- Peroxisomal biogenesis factor 8
- Peroxisomal membrane protein PEX17
Sequence:
MNENEYDNFDDLDDLLDEDPTKLDEAEPDDVQAKGSVYNDSENKEKNAESKDSDGVQVANESEEDPELKEMMVDLQNEFANLMKNNGNENNVKTEDFNKLISALEEAAKVPHQQMEQGCSSLKSNSTDKGTVNGSNPGFKNIVSNTLDRLKENGNKVDTSLAEETKESQRSGQNNNIDDILSQLLDQMVASGGKESAENQFDLKDGEMDDAITKILDQMTSKEVLYEPMKEMRSEFGVWFQENGENEEHKEKIGTYKRQFNIVDEIVNIYELKDYDELKHKDRVTELLDELEQLGDSPIRSANSPLKHGNEEEELMKMLEIDGNDPNLGNLDKELTDGCKQQ
Protein: Protein/nucleic acid deglycase 3 (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Chaperone protein YajL) (Maillard deglycase) (Q46948)
Organism: Escherichia coli (strain K12)
Function: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, collagen, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. However, is less efficient than Hsp31 and YhbO, suggesting that YajL might be preferentially dedicated to protein repair. Displays a covalent chaperone activity with sulfenylated thiol proteins by forming mixed disulfides with members of the thiol proteome, and preferentially with sulfenylated cellular proteins, upon oxidative stress; these mixed disulfides can be subsequently reduced by low-molecular-weight thiols to regenerate YajL and reduced proteins. Involved in biogenesis of ribosomal proteins, probably as a ribosomal protein-folding chaperone. Confers resistance to oxidative stress. Plays an important role in protection against electrophile/carbonyl stress. The chaperone activity reported for YajL is probably recruited to execute its deglycase activity, to interact with non-native glycated proteins and gain access to partially buried glycated sites. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity.
Interaction partners:
- 2-dehydropantoate 2-reductase
- Protein/nucleic acid deglycase 2
- Protein/nucleic acid deglycase 1
- Small ribosomal subunit protein uS10
- Chaperone protein DnaJ
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein bL27
Sequence:
MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGNLAITCSRGVKLLADAPLVEVADGEYDVIVLPGGIKGAECFRDSTLLVETVKQFHRSGRIVAAICAAPATVLVPHDIFPIGNMTGFPTLKDKIPAEQWLDKRVVWDARVKLLTSQGPGTAIDFGLKIIDLLVGREKAHEVASQLVMAAGIYNYYE
Protein: Myelin-associated oligodendrocyte basic protein (Q13875)
Organism: Homo sapiens (Human)
Function: May play a role in compacting or stabilizing the myelin sheath, possibly by binding the negatively charged acidic phospholipids of the cytoplasmic membrane.
Subcellular location: Cytoplasm, perinuclear region. Note=Present in the major dense line of CNS myelin. {ECO:0000250}.
Interaction partners:
- Myelin-oligodendrocyte glycoprotein
- Myelin proteolipid protein
- Opalin
- Methyl-CpG-binding protein 2
- Ermin
- Myelin-associated glycoprotein
- Myelin basic protein
- 2',3'-cyclic-nucleotide 3'-phosphodiesterase
Sequence:
MSQKPAKEGPRLSKNQKYSEHFSIHCCPPFTFLNSKKEIVDRKYSICKSGCFYQKKEEDWICCACQKTRTSRRAKSPQRPKQQPAAPPAVVRAPAKPRSPPRSERQPRSPPRSERQPRSPPRSERQPRSPPRSERQPRPRPEVRPPPAKQRPPQKSKQQPRSSPLRGPGASRGGSPVKASRFW
Protein: Heparan-sulfate 6-O-sulfotransferase 1 (HS6ST-1) (mHS6ST-1) (EC 2.8.2.-) (Q9QYK5)
Organism: Mus musculus (Mouse)
Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. Critical for normal neuronal development where it may play a role in neuron branching. May also play a role in limb development. May prefer iduronic acid.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
- D-glucuronyl C5-epimerase
- Heparan sulfate glucosamine 3-O-sulfotransferase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- Exostosin-1
- NMDA receptor synaptonuclear signaling and neuronal migration factor
Sequence:
MRRRRAGGRTMVERASKFVLVVAGSACFMLILYQYAGPGLSLGAPGGRVPPDDLDLFPTPDPHYEKKYYFPVRELERSLRFDMKGDDVIVFLHIQKTGGTTFGRHLVQNVRLEVPCDCRPGQKKCTCYRPNRRETWLFSRFSTGWSCGLHADWTELTNCVPGVLDRRDPAGLRSPRKFYYITLLRDPVSRYLSEWRHVQRGATWKTSLHMCDGRTPTPEELPPCYEGTDWSGCTLQEFMDCPYNLANNRQVRMLADLSLVGCYNLSFIPESKRAQLLLESAKKNLRGMAFFGLTEFQRKTQYLFERTFNLKFIRPFMQYNSTRAGGVEVDEDTIRHIEELNDLDMQLYDYAKDLFQQRYQYKRQLERREQRLRNREERLLHRSKEALPREDPEEPGRVPTEDYMSHIIEKW
Protein: Large ribosomal subunit protein eL24 (60S ribosomal protein L24) (Q9VJY6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 60S ribosomal protein L27
- Small ribosomal subunit protein uS14
- 40S ribosomal protein S27
- Small ribosomal subunit protein uS11A
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein RACK1
Sequence:
MKIGLCAFSGYKIYPGHGKTMVKIDGKSFTFLDKKCERSYLMKRNPRKVTWTVLYRRKHRKGIEEEASKKRTRRTQKFQRAIVGASLAEILAKRNMKPEVRKAQRDQAIKVAKEQKRAVKAAKKAAAPAPAKKSAPKQKAAKVTQKAAPRVGGKR
Protein: Methylated-thiol--coenzyme M methyltransferase (EC 2.1.1.251) (Methylthiol:coenzyme M methyltransferase 40 kDa subunit) (Q48924)
Organism: Methanosarcina barkeri
Function: Methyltransferase involved in methanogenesis from methylated-thiols. Catalyzes two successive steps: mediates the transfer of a methyl group from the substrate to the cobalt cofactor of a methylated-thiol-specific corrinoid protein (MtsB), and the subsequent transfer of the methyl group from the corrinoid protein to coenzyme M.
Interaction partners:
Sequence:
MVSEMTPTRRVMAAVLGGRVDYVPPANPLAQTTTELMQICNASWPKAHFDSKMMADLAAAPYEICGIEAARPQFDISLEAEVLGCKLDWNKPDRPPVTGPAYTDPADITWPDNLEEAGRIPVVLGAIEELRKRYDGMLPVIPVLTSPFTVAGHIAGVENLVRWTKTDPEKAHAFIEAATDFVIAYGKLQTAYGAHILFPADPSASGDLISGETYKEFVLPAHKRMAKEISCPLILHICGDTSKLLPYIKQSGIDCFSFDAVPVWYCRQVMGNEMSILGSLDVIDLMPNGTPEQVYNRTRECILQGADIVGTACDVSFGTSLENLRAYVRACKETPIPKYDDVEDIIRQIGVGIGRNMKENVLGGMQK
Protein: Nucleoporin Nup43 (Nup107-160 subcomplex subunit Nup43) (p42) (Q8NFH3)
Organism: Homo sapiens (Human)
Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation.
Subcellular location: Chromosome, centromere, kinetochore. Nucleus, nuclear pore complex.
Interaction partners:
- Nuclear pore complex protein Nup160
- Nuclear pore complex protein Nup107
- Nucleoporin Nup37
- Nuclear pore complex protein Nup85
- Protein SEC13 homolog
- Nuclear pore complex protein Nup98-Nup96
- Nuclear pore complex protein Nup133
- Nucleoporin SEH1
- Protein ELYS
- Nuclear pore complex protein Nup205
Sequence:
MEEIYAKFVSQKISKTRWRPLPPGSLQTAETFATGSWDNEENYISLWSIGDFGNLDSDGGFEGDHQLLCDIRHHGDVMDLQFFDQERIVAASSTGCVTVFLHHPNNQTLSVNQQWTTAHYHTGPGSPSYSSAPCTGVVCNNPEIVTVGEDGRINLFRADHKEAVRTIDNADSSTLHAVTFLRTPEILTVNSIGQLKIWDFRQQGNEPSQILSLTGDRVPLHCVDRHPNQQHVVATGGQDGMLSIWDVRQGTMPVSLLKAHEAEMWEVHFHPSNPEHLFTCSEDGSLWHWDASTDVPEKSSLFHQGGRSSTFLSHSISNQANVHQSVISSWLSTDPAKDRIEITSLLPSRSLSVNTLDVLGPCLVCGTDAEAIYVTRHLFS
Protein: V-type proton ATPase subunit G (A0A0G2K2R1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MASQSQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREQEFQSKQQAVSCGESRDGLTPVQIVGASCKMYVGDSTRS
Protein: Formin-like protein 3 (Formin homology 2 domain-containing protein 3) (Q6NXC0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for developmental angiogenesis, but not for vasculogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8IVF7}. Cell membrane {ECO:0000250|UniProtKB:Q8IVF7}; Lipid-anchor {ECO:0000255}.
Interaction partners:
- Rho guanine nucleotide exchange factor 9
- Cell division control protein 42 homolog
- Rho-related GTP-binding protein RhoA-D
- Cell division cycle 42-like 2
- Ras homolog family member J
Sequence:
MGNIESVDGQSEMKHHIMPLKVPMPDPTELEERFAIVLNSMNLPPDKARLLRQYDNEKKWDLICDQERFQVKNPPHTYIQKLRGYLDPKVTRKKFRRRVQESTKVLRELEISLRTNHIGWVREFLNDENRGLDILVEYLSFAQCAVMLDFEGLENGEDFSLDKAKSWSRSIEDLHQNGCNTLVRSARQSVLRYGSTSNSKTIKNSRLVSQKDDVHVCIMCLRAIMNYQYGFNLVMSHAHAVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHEIILSAFDNFKEVCKEKHRFEKLMEYFRSEDGNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLDDFLEKSKHTESDKLSVQIQAYLDNVFDVGGLLEDAETKNVALEKVEELEEHLSHVTEKLLDVENETMTKVADLEKQLLHKDKELAVIKETYESASTQVHTLRRMIQEKDAAFQRHNNIEKQLLELEQQGTIRLRKQPDGDIAIETLGAGAVAGTPLTDLRSLTVGMSTIGGLGGTSAVPVEAVAPPPPPPPPPPPPPPAPPLPSEVESIPIPPPPPPPLPGPSPSVILSVGLSAIRIKKPIKTKFRLPVFNWTALKPNQINGTVFNEIDDDRVLEELDLEKFEELFKTKAQGPVVDLSCSKSKVSQKVINKVQLLDANRSKNLAITLRKANKTTEEICKAIQTFDLKALPVDFVECLMRFLPTEAESKLLRQYERERRPLDQLAEEDRFMLLFSKIERLTQRMSIITFVGNFNDNVNMLTPQLNAIIAASASVKSSPKLKKILEIILALGNYMNSSKRGSVYGFKLQSLDLLLDTKSTDRKMTLLHYIALVVKEKYPELANFYNELHFVDKAAAVSLENVLLDVKELGKGMDLVRRECSLHDHAVLKGFAQTSDTQLDKLAKDAKTAEEAFNNVVLYFGESPKTTPPSVFFPVFVRFIRAYKEAVEENEQRKKQEEAMREKLLAQEAKQHDPKVQAQKKRHQQQELIAELRRRQAKDHRPVYEGKDGTIEDIITVLKSVPFTARTAKRGSRFFCDANLFDESIC
Protein: Nucleoporin nup44 (Nuclear pore protein nup44) (O42963)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Nucleoporin nsp1
- Nucleoporin nup45
- Nucleoporin nup186
- Probable nucleoporin C890.06
- Nucleoporin nup189
- Nucleoporin nup184
- Nucleoporin nup107
- Meiotically up-regulated gene 87 protein
- Nucleoporin nup85
- Nucleoporin nup146
Sequence:
MAFSFGQQGSSIKAPSIGSTGVFGQSNTTKPTAPFGSGSIFGSTNTNVGAGGPTGSSSAPPFGNSIFGKTQQQPTTSFSNTTTNAPQSTVFGQNAASRTGNSNTQPLFSWSTVNNPTKPVDETNATIPSSLLLSSGISPNATVSNAQYGPAQPPSVEEQVQKILNAWNLNHPDCAFQRFFYNKVPVEQAALYVKPPNYNQQKWDEAVANRPSNSVVPVLAVGFPDVQKRINMQIQQVNTYRIRMREIVETLGRLSNKHDLDFSIKLAEAKNRHVRLSERILRLAIKVHVLRHRGYALKPNEEELRKKLDDLTKSLNNPEIFGRLNEIWARITLIFEGEKISEDQRSNLAKGVVDWRKNSDQLEVITDVLRDHQVGLSYVVKLMQEDLATLNKQLTEHVPQSQK
Protein: Protein c-Fos (Cellular oncogene fos) (FBJ osteosarcoma oncogene) (Transcription factor AP-1 subunit c-Fos) (P01101)
Organism: Mus musculus (Mouse)
Function: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling (By similarity). Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30 (By similarity). {ECO:0000250}.
Interaction partners:
- Protein FosB
- Transcription factor JunD
- Transcription factor JunB
- Transcription factor Jun
- Estrogen receptor
- Fos-related antigen 1
- Fos-related antigen 2
- Transcription factor Maf
- Mitogen-activated protein kinase 3
- Cyclic AMP-responsive element-binding protein 1
Sequence:
MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNTQDFCADLSVSSANFIPTVTAISTSPDLQWLVQPTLVSSVAPSQTRAPHPYGLPTQSAGAYARAGMVKTVSGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEASTPESEEAFTLPLLNDPEPKPSLEPVKSISNVELKAEPFDDFLFPASSRPSGSETSRSVPDVDLSGSFYAADWEPLHSNSLGMGPMVTELEPLCTPVVTCTPGCTTYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL
Protein: Protein kinase (Q24458)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRVRKSTTSFFVASKIKSVSLYKRDDRCAYLYVHHNSDDFQIYFPSTERRQKFYDMILEMTADQVVFVNLSNDDANIEYEYDYDEQNRKMVLGKGTYGTVYAARDKQTQVRIAIKEVPEKNSQDVQPLHEEIKLHSQLRHRNIVRYLGSCSENGFFKIFMEQVPGGSLSDLLETKWGPLKDNESTMAFYSKQILEGLKYLHEQDIVHRDIKGDNVLVNTYSGVVKISDFGTSKRLARINPMTETFTGTLQYMAPEVIDQGVRGYGPAADIWSFGCTNVEMATGKPPFIELGSAHAAMFKVGFYKKHPNIPEELSANAKNFILRCFAISVMDRPSASQLLEDPFLQDKPRKVRPALPINTEFGRSISVPADRFVHKTTPPLSYNTTCNTPTTPELDITHSSSVDIDELPSNQFMLERRNSHGFLLSPEIEPSTPSLRTSISETSETDGFYRLKKDSQRRTTLSKVLALDESKICDIWLKKVDADQNSIAIRKSDLEVLIRGLRDYIMNENEKHLEATINELKQKLNNDAVALDHLHLALYSFQDAVVCVLRYHCIKPHWMFALDNLVKRAVQAAVTIFSPELGANLADKDLSGNDDESLRTSLMQKGSTESQEKQSLEKVLPTSNTREGVGLTLRNRAGMLCPVRWSARAS
Protein: Bile salt hydrolase (I3QNT8)
Organism: Bifidobacterium longum subsp. suis
Interaction partners:
Sequence:
SDDEGNTYFGRNLDWSFSYGETILVTPRGYRYDTVFGAGGKAKPNAVIGVGVVMADRPMYFDCANEHGLAIAGLNFPGYASFVHEPVEGTENVATFEFPLWVARNFDSVDEVEKALRNVTLVSQIVPGQQESLLHWFIGDGKRSIVVEQMADGMHVHHDDV
Protein: Denticleless E3 ubiquitin protein ligase homolog (F5GZ90)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLFNSVLRQPQLGVLRNAPNMEHVLAVANEEGFVRLYNTESQSFRKKCFKEWMAHWNAVFDLAWVPGELKLVTAAGDQTAKFWDVKAGELIGTCKGHQCSLKSVAFSKFEKAVFCTGGRDGNIMVWDTRCNKKDGFYRQVNQISGAHNTSDKQTPSKPKKKQNSKGLAPSVDFQQSVTVVLFQDENTLVSAGAVDGIIKVWDLRKNYTAYRQEPIASKSFLYPGSSTRKLGYSSLILDSTGSTLFANCTDDNIYMFNMTGLKTSPVAIFNGHQNSTFYVKSSLSPDDQFLVSGSSDEAAYIWKVSTPWQPPTVLLGHSQEVTSVCWCPSDFTKIATCSDDNTLKIWRLNRGLEEKPGGDKLSTVGWASQKKKESRPGLVTVTSSQSTPAKAPRAKCNPSNSSPSSAACAPSCAGDLPLPSNTPTFSIKTSPAKARSPINRRGSVSSVSPKPPSSFKMSIRNWVTRTPSSSPPITPPASETKIMSPRKALIPVSQKSSQAEACSESRNRVKRRLDSSCLESVKQKCVKSCNCVTELDGQVENLHLDLCCLAGNQEDLSKDSLGPTKSSKIEGAGTSISEPPSPISPYASESCGTLPLPLRPCGEGSEMVGKENSSPENKNWLLAMAAKRKAENPSPRSPSSQTPNSRRQSGKKLPSPVTITPSSMRKICTYFHRKSQEDFCGPEHSTEL
Protein: Protein transport protein Sec31A (SEC31-like protein 1) (SEC31-related protein A) (Vesicle-associated protein 1) (Q9Z2Q1)
Organism: Rattus norvegicus (Rat)
Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10574704}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:10574704}; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10574704}; Peripheral membrane protein. Note=Associates with membranes in a GTP-dependent manner (PubMed:10574704). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER) (By similarity). {ECO:0000250|UniProtKB:Q3UPL0, ECO:0000269|PubMed:10574704}.
Interaction partners:
- Protein transport protein SEC23
- Protein SEC13 homolog
- Small COPII coat GTPase SAR1B
- Protein transport protein SEC23
- SEC24 homolog A, COPII coat complex component
- SEC24 homolog B, COPII coat complex component
- SEC24 homolog D, COPII coat complex component
- SEC24 homolog C, COPII coat complex component
- Peflin
- Protein transport protein Sec31B
Sequence:
MKLKEIDRTAMQAWSPAQNHPIYLATGTSAQQLDATFSTNASLEIFELDLSDPSLDMKSCATFSSSHRYHKLIWGPHKMDSKGDVSGVLIAGGENGNIILYDPSKIIAGDKEVVIAQKDKHTGPVRALDVNIFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCSGLAWHPDVATQMVLASEDDRLPVVQMWDLRFASSPLRVLENHARGILAIAWSMADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSAASFDGRIRVYSIMGGSIDGLRQKQVDKLSSSFGNLDPFGTGQPLPPLQIPQQTSQHSIVLPLKKPPKWIRRPVGASFSFGGKLVTFENVTGQPQQGAEQPRRQPVFISQVVTEKDFLSRSEQLQHVVQSQGFISYCQKKIDASQTDFEKNVWSFLKVNFEEDSRGKYLELLGYRREDLGEKIALALNRVDGSDVALKDSDRVAQSDGEESPAEEGQLLGERIKEEKQECDFLPSAGGGTFNISVSGDIDGLITRALLTGNFESAVDLCLHDNRMADAIILAIAGGQELLAQTQKKYFAKSQSKITRLITAVVMKNWKEIVESCDLKNWREALAAVLTYAKPDEFSALCDLLGARLESEGDSLLRTQACLCYICAGNVERLVACWTKAQDGSNPLSLQDLIEKVVILRKAVQLTQALDTNTVGALLAEKMSQYANLLAAQGSIAAALAFLPDNTNQPDIVQLRDRLCRAQGRSVPGQESSRSSYEGQPLPKGGPGPLAGHPQVSRVQSQQYYPQVRIAPTVTTWSDRTPTALPSHPPAACPSDTQGGNPPPPGFIMHGNVVPNSPAPLPTSPGHMHSQPPPYPQPQPYQPAQQYSLGTGGSAVYRPQQPVAPPASKRYPNAPYVSPVASYSGQPHMYTAQPASSPTSSSAPLPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTPPAASELPASQRTGPQNGWNDPPALNRVPKKKKLPENFMPPVPITSPIMNPGGDPQPQGLQQQPSASGPRSSHASFPQPHLAGGQPFHGIQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQHVQALPTEKITKKPIPDEHLILKTTFEDLIQRCLSSATDPQTKRKLDDASKRLECLYDKLRDQTLSPTIISGLHSIARSIETRNYSEGLTVHTHIVSTSNFSETSAFMPVLKVVLSQASKLGV
Protein: Exocrine gland secreted peptide 4 (Exocrine gland-secreting peptide 4) (A8R0T8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Exocrine gland secreted peptide 31
- Predicted gene 1330.
- Predicted gene 12887
- ABPA19
- Exocrine gland secreted peptide 18
Sequence:
MLFLVTLLLPSMLTEGRVLTQTGKETTMSADHKTNHKADLEKNDSQGERNTQEAFEMILCAFNQEKMLLKDQANSGQHELKLSKFFTALSKCGAQNYQVDTVNYRIIPHIYPLHSPK
Protein: Phospholipid hydroperoxide glutathione peroxidase (PHGPx) (EC 1.11.1.12) (Glutathione peroxidase 4) (GPx-4) (GSHPx-4) (EC 1.11.1.9) (P36970)
Organism: Rattus norvegicus (Rat)
Function: Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins (By similarity). Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation. Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species (By similarity). The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis (By similarity). The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures (By similarity). May be required to protect cells from the toxicity of ingested lipid hydroperoxides (By similarity). Required for normal sperm development and male fertility (By similarity). Essential for maturation and survival of photoreceptor cells (By similarity). Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion (By similarity). Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism (By similarity). Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down-regulator of the cellular 15-lipoxygenase pathway (By similarity).
Subcellular location: [Isoform Nuclear]: Nucleus {ECO:0000269|PubMed:11344099}. Nucleus, nucleolus {ECO:0000269|PubMed:14575705}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:1556123}. Cytoplasm {ECO:0000269|PubMed:1556123}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:1556123}.
Interaction partners:
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Glutathione synthetase
- Glutathione hydrolase 7
- Glutathione hydrolase 5 proenzyme
- Glutathione hydrolase 6
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Endoplasmic reticulum chaperone BiP
- Glutathione S-transferase kappa 1
- Thioredoxin reductase 1, cytoplasmic
- Superoxide dismutase
Sequence:
MSWGRLSRLLKPALLCGALAVPGLAGTMCASRDDWRCARSMHEFAAKDIDGHMVCLDKYRGCVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEFAAGYNVRFDMYSKICVNGDDAHPLWKWMKVQPKGRGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDLPCYL
Protein: Probable alpha-L-arabinofuranosidase B (ABF B) (Arabinosidase B) (EC 3.2.1.55) (A2R511)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MFSRRNLVALGLAATVSAGPCDIYEAGDTPCVAAHSTTRALYSSFSGALYQLQRGSDDTTTTISPLTAGGVADASAQDTFCANTTCLITIIYDQSGNGNHLTQAPPGGFDGPDVDGYDNLASAIGAPVTLNGQKAYGVFMSPGTGYRNNEATGTATGDEPEGMYAVLDGTHYNDACCFDYGNAETSSTDTGAGHMEAIYLGNSTTWGYGAGDGPWIMVDMENNLFSGADEGYNSGDPSISYSFVTAAVKGGADKWAIRGGNAASGSLSTYYSGARPDYSGYNPMSKEGAIILGIGGDNSNGAQGTFYEGVMTSGYPSDDVENSVQENIVAAKYVSGSLVSGPSFTSGEVVSLRVTTPGYTTRYIAHTDTTVNTQVVDDDSSTTLKEEASWTVVTGLANSQCFSFESVDTPGSYIRHYNFELLLNANDGTKQFHEDATFCPQAPLNGEGTSLRSWSYPTRYFRHYDNVLYAASNGGVQTFDSKTSFNNDVSFEIETAFAS