wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleoporin NUP53 (Nuclear pore protein NUP53) (Q03790)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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 (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP53 may play an important role in cell cycle regulation by inhibiting PSE1 transport functions during mitosis and sequestration of MAD1-MAD2 in a cell cycle-dependent manner. It also seems to play an important role in de novo NPC assembly by associating with nuclear membranes and driving their proliferation.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Interaction partners:
- Importin subunit beta-3
- Nucleoporin ASM4
- Nucleoporin NUP170
- Nucleoporin NIC96
- Nucleoporin NUP188
- Nucleoporin NUP157
- Nucleoporin NUP57
- Nucleoporin NUP159
- Nucleoporin NUP192
- Nucleoporin NUP49/NSP49
Sequence:
MADLQKQENSSRFTNVSVIAPESQGQHEQQKQQEQLEQQKQPTGLLKGLNGFPSAPQPLFMEDPPSTVSGELNDNPAWFNNPRKRAIPNSIIKRSNGQSLSPVRSDSADVPAFSNSNGFNNVTFGSKKDPRILKNVSPNDNNSANNNAHSSDLGTVVFDSNEAPPKTSLADWQKEDGIFSSKTDNIEDPNLSSNITFDGKPTATPSPFRPLEKTSRILNFFDKNTKTTPNTASSEASAGSKEGASTNWDDHAIIIFGYPETIANSIILHFANFGEILEDFRVIKDFKKLNSKNMSKSPSLTAQKYPIYTGDGWVKLTYKSELSKSRALQENGIIMNGTLIGCVSYSPAALKQLASLKKSEEIINNKTSSQTSLSSKDLSNYRKTEGIFEKAKAKAVTSKVRNAEFKVSKNSTSFKNPRRLEIKDGRSLFLRNRGKIHSGVLSSIESDLKKREQASKSKKSWLNRLNNWLFGWNDL
Protein: Putative colanic acid biosynthesis glycosyl transferase WcaC (P71237)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Putative colanic acid biosynthesis glycosyl transferase WcaE
- Putative colanic acid biosynthesis glycosyl transferase WcaI
- Putative colanic acid biosynthesis glycosyl transferase WcaA
- Putative colanic acid biosynthesis acetyltransferase WcaB
- Putative colanic acid biosynthesis acetyltransferase WcaF
- GDP-mannose mannosyl hydrolase
- GDP-mannose 4,6-dehydratase
- Colanic acid biosynthesis protein WcaK
- UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase
- Putative polysaccharide export protein Wza
Sequence:
MNILQFNVRLAEGGAAGVALDLHQRALQQGLASHFVYGYGKGGKESVSHQNYPQVIKHTPRMTAMANIALFRLFNRDLFGNFNELYRTITRTAGPVVLHFHVLHSYWLNLKSVVRFCEKVKNHKPDVTLVWTLHDHWSVTGRCAFTDGCEGWKTGCQKCPTLNNYPPVKIDRAHQLVAGKRQLFREMLALGCQFISPSQHVADAFNSLYGPGRCRIINNGIDMATEAILADLPPVRETQGKPKIAVVAHDLRYDGKTNQQLVREMMALGDKIELHTFGKFSPFTAGNVVNHGFETDKRKLMSALNQMDALVFSSRVDNYPLILCEALSIGVPVIATHSDAAREVLQKSGGKTVSEEEVLQLVQLSKPEIAQAIFGTTLAEFSQRSRAAYSGQQMLEEYVNFYQNL
Protein: 3'-5' exonuclease domain-containing protein (Q9XUL8)
Organism: Caenorhabditis elegans
Interaction partners:
- ELKS/RAB6-interacting/CAST family member 2
- C-type lectin domain-containing protein
- Thymosin beta
- Histone H1
- LiPocalin-Related protein
Sequence:
MVSYGKEDFLADIEHKDMQSKFVRTNGTRSLLSLKAEATYWTGLDLHKGETMSDWTNTHLRGDQLRYAIMDTIVMHLIIKQRLRNIHKNDPRLFQYVFENGHPLPYNR
Protein: Sodium/hydrogen exchanger (A0A2R8Y780)
Organism: Homo sapiens (Human)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004424}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004520}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004195}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004195}.
Interaction partners:
Sequence:
MWGLGARGPDRGLLLALALGGLARAGGVEVEPGGAHGESGGFQVVTFEWAHVQDPYVIALWILVASLAKIGFHLSHKVTSVVPESALLIVLGLVLGGIVWAADHIASFTLTPTVFFFYLLPPIVLDAGYFMPNRLFFGNLGTILLYAVVGTVWNAATTGLSLYGVFLSGLMGDLQIGLLDFLLFGSLMAAVDPVAVLAVFEEVHVNEVLFIIVFGESLLNDAVTVVLYNVFESFVALGGDNVTGVDCVKGIVSFFVVSLGGTLVGVVFAFLLSLVTRFTKHVRIIEPGFVFIISYLSYLTSEMLSLSAILAITFCGICCQKYVKANISEQSATTVRYTMKMLASSAETIIFMFLGISAVNPFIWTWNTAFVLLTLVFISVYRAIGVVLQTWLLNRYRMVQLEPIDQVVLSYGGLRGAVAFALVVLLDGDKVKEKNLFVSTTIIVVFFTVIFQGLTIKPLVQWLKVKRSEHREPRLNEKLHGRAFDHILSAIEDISGQIGHNYLRDKWSHFDRKFLSRVLMRRSAQKSRDRILNVFHELNLKDAISYVAEGERRGSLAFIRSPSTDNVVNVDFTPRSSTVEASVSYLLRENVSAVCLDMQSLEQRRRSIRDAEDMVTHHTLQQYLYKPRQEYKHLYSRHELTPTEDEKQDREIFHRTMRKRLESFKSTKLGLNQNKKAAKLYKRERAQKRRNSSIPNGKLPMESPAQNFTIKEKDLELSDTEEPPNYDEEMSGGIEFLASVTKDTASDSPAGDTGSDTPLTGRSSPRHGPPTAAAAVPEKPQIPARLQRPRAPSPASPTPAPAQNSESAAPAPAEPPEGEPGAGPAPGAGPERRGLPSAHARSAAARRVHSRRSFQRPRARRRPALLKLASLPPSCHAPPHALEQEETPL
Protein: Integrin-binding sialoprotein (Bone sialoprotein 2) (Bone sialoprotein II) (BSP II) (Cell-binding sialoprotein) (Q28862)
Organism: Bos taurus (Bovine)
Function: Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P21815}.
Interaction partners:
- Integrin alpha-V
- Integrin beta
- Integrin beta-5
- Osteocalcin
- Osteopontin
- Dentin matrix acidic phosphoprotein 1
- Runt-related transcription factor
- Alkaline phosphatase, tissue-nonspecific isozyme
- Transcription factor Sp7
- Matrix extracellular phosphoglycoprotein
Sequence:
MKTVLILLSILGMACALSMKNLNRRAKLEDSEENGVFKYRPQYYVYKHGYFYPALKRFAVQSSSDSSEENGNGDSSEEEEEEEETSNEEGNNGGNEDSDENEDEESEAENTTLSTTTLGYGEITPGTGDIGLAAIWLPRKAGATGKKATKEDESDEEEEEEEEEENEAEVDDNEQGINGTSSNSTEVDNGHGSSGGDNGEEDGEEESVTEANTEGITVAGETTTSPNGGFKPTTPHQEVYGTTPPPFGKITTPGEYEQTGTNEYDNGYEIYESENGDPRGDNYRAYEDEYSYYKGRGYDSYDGQDYYSHQ
Protein: Treble clef zinc finger domain-containing protein (Q4GZ46)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Guide RNA binding protein
- HTH OST-type domain-containing protein
- Mitochondrial RNA binding protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MLRYTSCAANMLYARGALRVLAGEESLMSHKLLVITAPLLSARCVRMASTGAPGAAESLDNSNVGSGSNMQCREASIRRLAVVRPDLVGEWVPELNDSDVSSVLCTSTIDAWWRCNACGTNYRATVKDRATIEKGCPECASTRTLRQNHVSSDSCTGTAAVSERTNETAKGSLKETHPAIADRWDYERNGLLLPTDVDAASELNVWWKPAPGRPSRERSFRRPVFAFVETPYSEEEQLEAQTALELDVLQQVRQASKITTARENHALPAAARMLDDIVFRNNSSSSSEHTSATTNIAASSEPMITEGAQGNRCNLDGEDLYKAVELWERKHKTKAGLETRPMFYSTENCDGAAIARGQVLTAYHRFVSDRKPKVCTAHDGNENDQLPIPSAIEDPDWLQHFTLRVDDVAIGHSASSARLVLPDNVAFVSAVDHEKHTTVASNGASRKSRMATLPPPPEEYGSEVRTTFAVQKRSYPRRPPQPPAREDDVTEAVPKATEAAGERAIGSFPRHTGSGAARNNGLPEASFAVVSLSGAQSLAREYNSGTTDNIDALFDAKGEELQRQTLLGPTAISSMTEEQVRALQYNRGSPRPRRTGRFRLRPPVETDSGSTEVVRKGDVLTSTFGSGVLSAADAPTQDEDKDLKIIQAPGAPRKVSRPKRKKAEEAAPGDDYGNNAVRAAAGDASKDKVAAPA
Protein: STI1 domain-containing protein (G5EE04)
Organism: Caenorhabditis elegans
Interaction partners:
- Heat shock protein 110
- RING-type domain-containing protein
- RING-type domain-containing protein
- Heat shock protein 90
- E3 ubiquitin-protein ligase CHIP
- ENTH domain-containing protein
- B30.2/SPRY domain-containing protein
Sequence:
MDHVALLKQFVGMCQANPAVLHAPEFGFFKDYLVSLGATLPPKPADKPEGKCPMSEEPKKETPAAEATPEPEIPKPEEIPFPKIDNEGVIEPEEAVALPMGDSAKEATEDEIEKASEERGKAQEAFSNGDFDTALTHFTAAIEANPGSAMLHAKRANVLLKLKRPVAAIADCDKAISINPDSAQGYKFRGRANRLLGKWVEAKTDLATACKLDYDEAANEWLKEVEPNAHKIQEYNRAVERQKADIELAERRERVRRAQEANKKAAEEEAKRQAEQGDDFDFEGGFPGGMPGGFPGAGGMPGGFPGAPGGGAPGGMGAGIEQLFSDPEIAAAIQDPEVLPALMDIMQNPANMMKYINNPKVAKLISKLQSKGAGMPGMFGGAPPSAGGGCEDADCGGPCPGARGGASVPQQPPRRAPEPDLD
Protein: EF-hand domain-containing protein (Troponin C) (G5EF37)
Organism: Caenorhabditis elegans
Interaction partners:
- Troponin T
- Troponin T
- TropoNin T
- Troponin T, skeletal muscle
- Troponin I 2
- Troponin I 1
- Troponin I 3
- Tropomyosin isoforms a/b/d/f
- Paramyosin
- Actin
Sequence:
MAEDIEEILAEIDGSQIEEYQKFFDAFDRGKQGYIMATQIGQIMHGMEQDFDEKTLRKLIRKFDADGSGKLEFDEFCALVYTVANTVDKETLEKELREAFRLFDKEGNGYISRPTLKALLKEIADDLTDQQLEEAVDEIDEDGSGKIEFEEFWELMAGESD
Protein: Photosystem II D2 protein (PSII D2 protein) (EC 1.10.3.9) (Photosystem Q(A) protein) (P09192)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700, ECO:0000269|PubMed:9512353}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01383, ECO:0000269|PubMed:34937700}.
Interaction partners:
- Photosystem II reaction center protein K
- Photosystem II extrinsic protein O
- Photosystem II CP47 reaction center protein
- Photosystem II reaction center protein H
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein L
- Photosystem II reaction center protein I
- Photosystem II extrinsic protein V
- Cytochrome b559 subunit beta
- Photosystem II protein D1 2
Sequence:
MTIAVGRAPVERGWFDVLDDWLKRDRFVFIGWSGLLLFPCAFMALGGWLTGTTFVTSWYTHGLASSYLEGANFLTVAVSSPADAFGHSLLFLWGPEAQGNLTRWFQIGGLWPFVALHGAFGLIGFMLRQFEISRLVGIRPYNAIAFSGPIAVFVSVFLMYPLGQSSWFFAPSFGVAGIFRFILFLQGFHNWTLNPFHMMGVAGILGGALLCAIHGATVENTLFEDGEDSNTFRAFEPTQAEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSSVGIVGLALNLRAYDFVSQELRAAEDPEFETFYTKNILLNEGMRAWMAPQDQPHENFIFPEEVLPRGNAL
Protein: SNARE associated Golgi protein family (T12C22.23 protein) (Q9LPD5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKKWLAIAATVAIIAIIVRQGTTQYGWNKEAALEKLKEWSDRLGIWAIPTYVAVHTITLALCLPHAVFFEAGASMLFGFLPALLCVFSAKVLAASFSFWIGRFVFKSSTRATGWAHSNKYFNILSRGVERDGWKFVLLARFSPIPSYVINYALAATEVRFVADFLFPTVIGCLPMILQNASVGSLAGMAVASVAGKQKSQVWGYVFPVLGILSSVLISLRIKKYSAGITEASSDTSANNSSLASSETANPAYGTDGSKKSE
Protein: Pentatricopeptide repeat-containing protein At2g20540 (Q9SIL5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Phosphoglycerate mutase family protein
Sequence:
MAFHGIREVENYFIPFLQRVKSRNEWKKINASIIIHGLSQSSFMVTKMVDFCDKIEDMDYATRLFNQVSNPNVFLYNSIIRAYTHNSLYCDVIRIYKQLLRKSFELPDRFTFPFMFKSCASLGSCYLGKQVHGHLCKFGPRFHVVTENALIDMYMKFDDLVDAHKVFDEMYERDVISWNSLLSGYARLGQMKKAKGLFHLMLDKTIVSWTAMISGYTGIGCYVEAMDFFREMQLAGIEPDEISLISVLPSCAQLGSLELGKWIHLYAERRGFLKQTGVCNALIEMYSKCGVISQAIQLFGQMEGKDVISWSTMISGYAYHGNAHGAIETFNEMQRAKVKPNGITFLGLLSACSHVGMWQEGLRYFDMMRQDYQIEPKIEHYGCLIDVLARAGKLERAVEITKTMPMKPDSKIWGSLLSSCRTPGNLDVALVAMDHLVELEPEDMGNYVLLANIYADLGKWEDVSRLRKMIRNENMKKTPGGSLIEVNNIVQEFVSGDNSKPFWTEISIVLQLFTSHQDQDVITNNNALAFIGIV
Protein: Possible formate hydrogenase HycE (FHL) (Q10884)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv0083
- Uncharacterized protein Rv0085
- Probable oxidoreductase
- Possible hydrogenase HycQ
- Possible formate hydrogenlyase HycD
- NADH-quinone oxidoreductase subunit I
- Urease accessory protein UreG
- Chaperonin GroEL 1
- Chaperonin GroEL 2
- Uncharacterized HTH-type transcriptional regulator Rv0081
Sequence:
MMSASWLRHRVSERGLIATAEQLWADSFRLALVAAHDDGDSLRVVYLFLAGYPDRRVELEYVVPADNPEIRSLAYLSFPAGRFEREMADLYGIRPVGHPKPRRLVRHAHWPDWHPMRTDAGPAPEFTDTGAFPFLAVEGPGVYEIPVGPVHAGLIEPGHFRFSVAGETIVRLKARLWFVHRGIEKLFHGRPATAAVDLAERISGDTSAAHALAHSLAIEDALGIELPHEVHRLRALIVELERLYNHAADLGALANDVGYSLANAHAQRIRENLLRRNAAVTGHRLLRGAIRAGGVALRALPDTDELAALAVDLAEVATLTLANSVVYDRFAGTAVLHPDDASALGCLGYVARASGLRSDARVEHPTIVLPITEIGAPDGDVLARYTVRRDEFAASAALAQHIVESHTGPIEYAATLHPVGAPSSGIGIVEGWRGTIVHRVEIDVDGRITRAKVVDPSWFNWPALPVAMADTIVPDFPLANKSFNQSYAGNDL
Protein: Serine transporter (Q8XAF5)
Organism: Escherichia coli O157:H7
Function: Transports both D- and L-serine; allows growth of strain CFT073 cells normally unable to transport D-serine on that substrate. Transport relies on the H(+) gradient and is not competed by L-threonine. May play a role in L-cysteine detoxification (By similarity).
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P42628, ECO:0000255, ECO:0000305|PubMed:26727373}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- UPF0597 protein YhaM
- UPF0597 protein YhaM
- HTH-type transcriptional regulator YhaJ
- HTH-type transcriptional regulator YhaJ
- Serine/threonine transporter SstT
- D-serine/D-alanine/glycine transporter
Sequence:
MEIASNKGVIADASTPAGRAGMSESEWREAIKFDSTDTGWVIMSIGMAIGAGIVFLPVQVGLMGLWVFLLSSVIGYPAMYLFQRLFINTLAESPECKDYPSVISGYLGKNWGILLGALYFVMLVIWMFVYSTAITNDSASYLHTFGVTEGLLSDSPFYGLVLICILVAISSRGEKLLFKISTGMVLTKLLVVAALGVSMVGMWHLYNVGSLPPLGLLVKNAIITLPFTLTSILFIQTLSPMVISYRSREKSIEVARHKALRAMNIAFGILFIIVFFYAVSFTLAMGHDEAVKAYEQNISALAIAAQFISGDGAAWVKVVSVILNIFAVMTAFFGVYLGFREATQGIVMNILRRKMPAEKINENLVQRGIMIFAILLAWSAIVLNAPVLSFTSICSPIFGLVGCLIPAWLVYKVPALHKYKGMSLYLIIVTGLLLCVSPFLAFS
Protein: Arasin 1 (Ara-1) (Proline-rich antimicrobial peptide) (PR-AMP) (Pro-rich AMP) (A6XMY0)
Organism: Hyas araneus (Atlantic lyre crab) (Great spider crab)
Function: Antimicrobial peptide that has a large activity spectrum with activity against Gram-positive, Gram-negative bacteria, as well as against fungi. Shows activity at micromolar concentrations. Displays minimal inhibitory concentration (MIC) values lower than minimal bactericidal concentrations (MBC). Synthetic peptides with similar activities than the full length peptide (composed of the first 23 or 25 amino acids (Arasin 1(26-48) or Arasin 1(26-50))) may have a dual mode of action depending on the peptide concentrations. At MIC concentrations, the peptide penetrates into the cytoplasm of target cells (tested on the Gram-negative E.Coli). The two inner membrane proteins YgdD and SbmA may be required for this uptake. At concentrations higher than MIC, arasin may act by disrupting membranes. Full-length and N-terminal peptides do not show hemolytic activity.
Interaction partners:
Sequence:
MERRTLLVVLLVCSCVVAAAAEASPSRWPSPGRPRPFPGRPKPIFRPRPCNCYAPPCPCDRWRH
Protein: Manganese lipoxygenase (Mn-LO) (MnLOX) (EC 1.13.11.-) (EC 1.13.11.45) (Linoleate 11S-lipoxygenase) (Linoleate 13R-lipoxygenase) (Manganese 13R-lipoxygenase) (13R-MnLOX) (Q8X151)
Organism: Gaeumannomyces avenae (Oat take-all root rot fungus) (Gaeumannomyces graminis var. avenae)
Function: Lipoxygenase that metabolizes linoleic and alpha-linolenic acids to 11S- and 13R-hydroperoxy fatty acids. At the end of lipoxygenation, the intermediate product 11S-HPODE from linoleic acid is then transformed into 13R-HPODE as the final product. It also acts on alpha-linolenic acid producing 11S-HPOTrE and 13R-HPOTrE with subsequent transformation of 11S-HPOTrE to 13R-HPOTrE as final product.
Subcellular location: Secreted {ECO:0000269|PubMed:12047377, ECO:0000269|PubMed:9582345}.
Interaction partners:
Sequence:
MRSRILAIVFAARHVAALPLAAEDAAATLSLTSSASSTTVLPSPTQYTLPNNDPNQGARNASIARKRELFLYGPSTLGQTTFYPTGELGNNISARDVLLWRQDAANQTATAYREANETFADITSRGGFKTLDDFALLYNGHWKESVPEGISKGMLSNCTSDLLFSMERLSSNPYVLKRLHPTKDKLPFSVESKVVKKLTATTLEALHKGGRLFLVDHSYQKKYTPQPGRYAAACQGLFYLDARSNQFLPLAIKTNVGVDLTYTPLDDKDDWLLAKIMFNNNDLFYSQMYHVLFHTIPEIVHEAAFRTLSDRHPVMGVLNRLMYQAYAIRPVGGAVLFNPGGFWDQNFGLPASAAIDFPGSVYAQGGGGFQAGYLEKDLRSRGLIGEDSGPRLPHFPFYEDAHRLIGAIRRFMQAFVDSTYGADDGDDGALLRDYELQNWIAEANGPAQVRDFPAAPLRRRAQLVDVLTHVAWITGGAHHVMNQGSPVKFSGVLPLHPAALYAPIPTAKGATGNGTRAGLLAWLPNERQAVEQVSLLARFNRAQVGDRKQTVRDAFAAPDLLAGNGPGYAAANARFVEDTGRISREIAGRGFDGKGLSQGMPFVWTALNPAVNPFFLSV
Protein: LD37169p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform D) (Q9VWG1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAEANKRNIPIKLGDFSVIDTEFSNIRERFDSEMRKMEEEMAKFRHELMNREANFFESTSSTTNSALPSRIPKQQNYVSDISSPLIQDEGDNKVLKLRFDVSQYAPEEIVVKTVDQKLLVHAKHEEKSDTKSVYREYNREFLLPKGVNPESIRSSLSKDGVLTVDAPLPALTAGETLIPIAHK
Protein: LD41424p (Loechrig isoform IV) (Q8I0K6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSNNGPTASSNYQLLNSANLRDLIDGQRHSHHVSRRDDSQSHSHSESPSHIGHISQSNQSIPSLPSLPSGKNKTKDGKKLKATLTAAMSSSLLRRKAHSNHSQQQKLQLQQQQQEQHQQQLQQQQLRSNNSKAIANAARHSLGHSPSAAAAAAAVQQTLVYERRRVSSAHSSPSPTSRHHSPVHQCMLMRRRSDYSVEQIEQWKRQQQLLPRSGRKISLPVADPFLEKVNLSDLEEDDSQIFVKFFRFHKCYDLIPTSAKLVVFDTQLLVKKAFYALVYNGVRAAPLWDSEKQQFVGMLTITDFIKILQMYYKSPNASMEQLEEHKLDTWRSVLHNQVMPLVSIGPDASLYDAIKILIHSRIHRLPVIDPATGNVLYILTHKRILRFLFLYINELPKPAYMQKSLRELKIGTYNNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEHRNEWFEGVQKCNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLVLRPSGEGVGGSESSLRASDPVLLRKVAEVEIPATAAAATTTTPPRSPSAGSGNRSLIEDIPEEETAPARSDDADSDNNKSASEDKANNNQHDQTTTAATANGDSNNSPVEVSFADEAQEEEAADQVERSNCDDDDQPALAEIERKNASMDDDEDDGMSSAVSAASALGQSLTPAAQEMALVSE
Protein: Probable succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (FP) (Q9UTJ7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q00711}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q00711}; Matrix side {ECO:0000250|UniProtKB:Q00711}.
Interaction partners:
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase cytochrome B subunit
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- NADH-ubiquinone oxidoreductase 51 kDa subunit homolog SPBC18E5.10, mitochondrial
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Aconitate hydratase, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MLRFRKVAPSLKNGGNLKLFSTSSTLKKIASSQPLRAKQVSTSESVKYPVIDHTYDAIVVGAGGAGLRATFGLAEAGFNTACITKLFPTRSHTVAAQGGINAALGNMTKDDWRWHFYDTVKGSDWLGDQDAIHYMTKEAPKAVLELEHFGVPFSRTKEGKIYQRAFGGQSLEYGKGGQAYRCAAVADRTGHSILHTLYGQSLKHNTNFFIEYFAMDLIMEGGECRGVIAMNLEDGSIHRFRAHKTILATGGYGRAYFSCTSAHTCTGDGNAMVSRAGLPLQDLEFVQFHPTGIYGAGCLITEGCRGEGGYLLNSKGERFMERYAPTAKDLASRDVVSRAMTVEIREGRGVGPEKDHCYLQLSHLPAEILKERLPGISETAAIFAGVDVTKEPIPVLPTVHYNMGGIPTRFTGEVLTIDENGKDKIVPGLYAAGEAACVSVHGGNRLGANSLLDIVVFGRACALHIKDTLEPNTPHKPLAADAGLDSLKFLDQIRTSQGPKHTSEIRLDMQKTMQRDVSVFRMEETLQEGVKNIARVDGTYKDIGIRDRGLIWNTDLVEALELRNLLTCAVQTANAALNRKESRGAHAREDYPERDDKNWIKHTLTWQHKTGDPVTLKYRAVTRTTMDENEVKPVPPFKRVY
Protein: Alpha-defensin 6/12 (Defensin-related cryptdin-6/12) (Cryptdin-2) (P50704)
Organism: Mus musculus (Mouse)
Function: Has broad-spectrum antimicrobial properties. Has antibacterial activity against the Gram-positive bacterium L.monocytogenes EGD and the Gram-negative bacteria E.coli ML-35p and avirulent S.typhimurium 7953, but not against the mouse-virulent S.typhimurium 14028S. Probably contributes to the antimicrobial barrier function of the small bowel mucosa.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MKTLILLSALVLLAFQVQADPIQNTDEETKTEEQPGEEDQAVSVSFGDPEGTSLQEESLRDLVCYCRARGCKGRERMNGTCRKGHLLYMLCCR
Protein: Mitochondrial import inner membrane translocase subunit tim13 (Q10481)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins, while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit tim8
- Mitochondrial import inner membrane translocase subunit tim10
- Mitochondrial import inner membrane translocase subunit tim9
- Mitochondrial import inner membrane translocase subunit tim23
- Mitochondrial import inner membrane translocase subunit tim22
- Probable mitochondrial import receptor subunit tom40
- Mitochondrial import inner membrane translocase subunit tim16
- Mitochondrial import inner membrane translocase subunit tim17
- Mitochondrial import inner membrane translocase subunit tim54
- Mitochondrial intermembrane space import and assembly protein 40
Sequence:
MGIFGGNSGNAPSSEDKKSIFMKQIRQELAVAQAGELISKINENCFDKCIPEPGSTFDPNEKSCVSKCMERYMDAWNIVSRTYISRMQREQKNLN
Protein: Protein transport protein Sec61 subunit gamma (P60059)
Organism: Homo sapiens (Human)
Function: Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (By similarity). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (By similarity). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex. The SEC61 channel cooperates with the translocating protein TRAM1 to import nascent proteins into the ER (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:36261522}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit alpha isoform 1
- Translocation protein SEC63 homolog
- Translocation protein SEC62
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Protein transport protein Sec61 subunit alpha isoform 2
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL29
Sequence:
MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIPINNIIVGG
Protein: SR-CI (Q5ELS1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEFFWTLAVIVIYCIGHIHGRCERSIDLDNGSINYRQRNIVRFRCNRGYTLQGTVMQTCDRDGRLRGEKPFCASRGCAKPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVKLMTGSECGTNGFTTTTEPTAPTGSNEQPLVYDMMSCSGRCGTSISASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELITTTEDDISSLPPTVTSTSTSTTRKSTTTTSTTSTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPKSTTSTTSTTSTTSTTPTTTTTINVFTTKKTTTMIPTSSTEKTTGINTTMKTRKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLGIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLRKQRKRNGMDDQPLCDSDNDDVEYFEGMGVDIRHRTDL