wanglab/gogpt-training-data huggingface dataset:
Protein: Tolloid-like protein 2 (EC 3.4.24.-) (Q9Y6L7)
Organism: Homo sapiens (Human)
Function: Protease which specifically processes pro-lysyl oxidase. Required for the embryonic development. Predominant protease, which in the development, influences dorsal-ventral patterning and skeletogenesis.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Chordin
- Procollagen C-endopeptidase enhancer 1
- Bone morphogenetic protein 1
Sequence:
MPRATALGALVSLLLLLPLPRGAGGLGERPDATADYSELDGEEGTEQQLEHYHDPCKAAVFWGDIALDEDDLKLFHIDKARDWTKQTVGATGHSTGGLEEQASESSPDTTAMDTGTKEAGKDGRENTTLLHSPGTLHAAAKTFSPRVRRATTSRTERIWPGGVIPYVIGGNFTGSQRAIFKQAMRHWEKHTCVTFIERTDEESFIVFSYRTCGCCSYVGRRGGGPQAISIGKNCDKFGIVAHELGHVVGFWHEHTRPDRDQHVTIIRENIQPGQEYNFLKMEAGEVSSLGETYDFDSIMHYARNTFSRGVFLDTILPRQDDNGVRPTIGQRVRLSQGDIAQARKLYKCPACGETLQDTTGNFSAPGFPNGYPSYSHCVWRISVTPGEKIVLNFTSMDLFKSRLCWYDYVEVRDGYWRKAPLLGRFCGDKIPEPLVSTDSRLWVEFRSSSNILGKGFFAAYEATCGGDMNKDAGQIQSPNYPDDYRPSKECVWRITVSEGFHVGLTFQAFEIERHDSCAYDYLEVRDGPTEESALIGHFCGYEKPEDVKSSSNRLWMKFVSDGSINKAGFAANFFKEVDECSWPDHGGCEHRCVNTLGSYKCACDPGYELAADKKMCEVACGGFITKLNGTITSPGWPKEYPTNKNCVWQVVAPAQYRISLQFEVFELEGNDVCKYDFVEVRSGLSPDAKLHGRFCGSETPEVITSQSNNMRVEFKSDNTVSKRGFRAHFFSDKDECAKDNGGCQHECVNTFGSYLCRCRNGYWLHENGHDCKEAGCAHKISSVEGTLASPNWPDKYPSRRECTWNISSTAGHRVKLTFNEFEIEQHQECAYDHLEMYDGPDSLAPILGRFCGSKKPDPTVASGSSMFLRFYSDASVQRKGFQAVHSTECGGRLKAEVQTKELYSHAQFGDNNYPSEARCDWVIVAEDGYGVELTFRTFEVEEEADCGYDYMEAYDGYDSSAPRLGRFCGSGPLEEIYSAGDSLMIRFRTDDTINKKGFHARYTSTKFQDALHMKK
Protein: Probable dihydroorotate dehydrogenase A (fumarate) (DHOD A) (DHODase A) (DHOdehase A) (EC 1.3.98.1) (Q9X9S0)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MVSTKTQIAGFEFDNCLMNAAGVACMTIEELEEVKNSAAGTFVTKTATLDFRQGNPEPRYQDVPLGSINSMGLPNNGLDYYLDYLLDLQEKESNRTFFLSLVGMSPEETHTILKKVQESDFRGLTELNLSCPNVPGKPQIAYDFETTDRILAEVFAYFTKPLGIKLPPYFDIVHFDQAAAIFNKYPLKFVNCVNSIGNGLYIEDESVVIRPKNGFGGIGGEYIKPTALANVHAFYQRLNPQIQIIGTGGVLTGRDAFEHILCGASMVQVGTTLHKEGVSAFDRITNELKAIMVEKGYESLEDFRGKLRYID
Protein: SNF-related serine/threonine-protein kinase (EC 2.7.11.1) (SNF1-related kinase) (Q9NRH2)
Organism: Homo sapiens (Human)
Function: May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Dual specificity protein phosphatase 5
- Calcium-binding protein 39
- Dual specificity protein phosphatase 2
- Secreted frizzled-related protein 4
- A disintegrin and metalloproteinase with thrombospondin motifs 12
Sequence:
MAGFKRGYDGKIAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPSHVSKECKDLITRMLQRDPKRRASLEEIENHPWLQGVDPSPATKYNIPLVSYKNLSEEEHNSIIQRMVLGDIADRDAIVEALETNRYNHITATYFLLAERILREKQEKEIQTRSASPSNIKAQFRQSWPTKIDVPQDLEDDLTATPLSHATVPQSPARAADSVLNGHRSKGLCDSAKKDDLPELAGPALSTVPPASLKPTASGRKCLFRVEEDEEEDEEDKKPMSLSTQVVLRRKPSVTNRLTSRKSAPVLNQIFEEGESDDEFDMDENLPPKLSRLKMNIASPGTVHKRYHRRKSQGRGSSCSSSETSDDDSESRRRLDKDSGFTYSWHRRDSSEGPPGSEGDGGGQSKPSNASGGVDKASPSENNAGGGSPSSGSGGNPTNTSGTTRRCAGPSNSMQLASRSAGELVESLKLMSLCLGSQLHGSTKYIIDPQNGLSFSSVKVQEKSTWKMCISSTGNAGQVPAVGGIKFFSDHMADTTTELERIKSKNLKNNVLQLPLCEKTISVNIQRNPKEGLLCASSPASCCHVI
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (P03772)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Interaction partners:
Sequence:
MRYYEKIDGSKYRNIWVVGDLHGCYTNLMNKLDTIGFDNKKDLLISVGDLVDRGAENVECLELITFPWFRAVRGNHEQMMIDGLSERGNVNHWLLNGGGWFFNLDYDKEILAKALAHKADELPLIIELVSKDKKYVICHADYPFDEYEFGKPVDHQQVIWNRERISNSQNGIVKEIKGADTFIFGHTPAVKPLKFANQMYIDTGAVFCGNLTLIQVQGEGA
Protein: Transcription factor Sox-19b (Protein sox-31) (Q9DDD7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcriptional activator.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- POU domain, class 5, transcription factor 1
- Nanog
Sequence:
MYSMMEHELKTAGPPHTLQHSPGMSPPGSGVGNAHHVSKTACPPGVDPMDKVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLTDVEKRPFIDEAKRLRAVHMKEYPDYKYKPRRKTKALMKKDNPVGKYPLAAGNLLASAVAQGQGGSPRMDGYGWGHAGGYMGMQGDALGYPQQLHRYDLSALQYPAAQPYMNSASSYSQMSYSSSPQQPSPVMSMVKPEPLSHSPTGVPNHHRGAFQGDLRDMISMYIPGGDTSESSNQRAYPGVQQHYLGGTVPLTHI
Protein: Vomeronasal type-1 receptor 48 (Vomeronasal type-1 receptor A3) (Vomeronasal type-1 receptor A6) (Q9EQ52)
Organism: Mus musculus (Mouse)
Function: Putative pheromone receptor implicated in the regulation of social and reproductive behavior.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MNENSRLHTHSNIRNTFFSEIGIGISGNSFLLLFHIIKFFRGHRPRLTDLPIGLLSLIHLLMLLVAAVIATDIFISWRGWNDIICKFLVYLYRSLRGLSLCTTSMLSVLQAIILSPRSYCLAKFKRKSSHNISCAIIFLSVLYMSISSHLLISITATPNLTMNDFLYVSQSCSLLPLSYLMQSIYSTLLVLREVFLIGLMVLSTSYMVALLYMHRKQAQNLQGTSLSLKASAEQRATQTILMLMTFFVLMSIFDSIVSCSRTMFLDDPTSYSIHIFVMHIYATVSPFVFISTEKHIVNILRG
Protein: Exodeoxyribonuclease 7 small subunit (EC 3.1.11.6) (Exodeoxyribonuclease VII small subunit) (ExoVII small subunit) (Exonuclease VII small subunit) (P0A8G9)
Organism: Escherichia coli (strain K12)
Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. It can degrade 3' or 5' ss regions extending from the termini of duplex DNA molecules and displaced ss regions. It can also excise thymine dimers in vitro (Probable). Required for production of the mature 5'-end of retron Ec78 or Ec83 msDNA. When in excess of the large subunit, counteracts the large subunit's toxicity.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00337, ECO:0000305|PubMed:6284744}.
Interaction partners:
- Exodeoxyribonuclease 7 large subunit
- Farnesyl diphosphate synthase
- 1-deoxy-D-xylulose-5-phosphate synthase
Sequence:
MPKKNEAPASFEKALSELEQIVTRLESGDLPLEEALNEFERGVQLARQGQAKLQQAEQRVQILLSDNEDASLTPFTPDNE
Protein: F-actin-capping protein subunit beta (Aginactin subunit beta) (CAP32) (P13021)
Organism: Dictyostelium discoideum (Social amoeba)
Function: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:A9XFX6}.
Interaction partners:
- F-actin-capping protein subunit alpha
- Dynactin subunit 2
- Dynactin subunit 4
- Actin-interacting protein 1
- Twinfilin
- Dynactin subunit 6
- Dynactin 150 kDa subunit
- Dynactin subunit 5
- Cytoplasmic dynein 1 light intermediate chain 1
- Myotrophin homolog
Sequence:
MTEKQLSCCLDLMRRLPPSQIEDNLAGLLDLVPDLTEDLLSSIDQPLKVAYDAVSKKDYLLCDYNRDADSYRSPWSNKYDPPLSGACYPSSKLRDIEVQANEIFEIYLNLYFEGGVSSVYCWDLDDNFAAVVLMKKTQDQSKKGQPMRGTWDSIHVVEVKLGKKDKAVYKLTSTVMLSIETDNDNTGKVNLAGSLTRQDEKEYTFNEVDTHCVNIGKMVEDMESKLRQTLETIYFGKTKEVVNTLRNATGNSELEKRKNLSNQIGSAIGNRG
Protein: TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (Q58EQ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Membrane {ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU361271}.
Interaction partners:
Sequence:
MERYQLSVLCWWTFLISTVVDWRGVDGNNPFYRPYRIPQLCKFCDVLESNCNGKDTCESNCSITSICESPDEICVAIWRQSDDNNTIETLCHNPTVPLYGIMVENNNNTKCEMKKRISNSGPFHICSCNEVECNDMLLFKLPTNNQVVLVILVSLLPLLVLAVLVIASFYWYRLYRRRKLDEWETKKPSKHKGPKGALDCSDACAIMMDDDRSDSSSTHANNINHNMDPLPIELDLQVGKGRFAEVYKAKLRQSPSEQFETVAVKIFPYEEYASWKNEKDIFQDIDLKHENILHFLTAEERKVEKQYWLITAFHPRGNLQEYLMRHLLSWEDLRLLGSSLASGVAHLHSDHTPCGRPKVPIVHRDLKSSNILVKNDLTCCLCDFGLGLRLDNSLSVDELANSGQVGTARYMAPEVLESRINLENIESFKQTDVYSMALVLWEITSRCNAIGEVKDYEPPFGSKVREHPCVESMKDNVLRDRGRPEIPSSWMKHQGVAAVCATINECWDHDPEARLTAQCVAERFNEMDDDLDKLSTCSSSEEKIPEDCAVSVSDDK
Protein: Protein MID1-COMPLEMENTING ACTIVITY 2 (Q3EBY6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calcium-permeable stretch-activated channel component. Probably involved in mechanosensing and in mechano-stimulated calcium uptake mechanism.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20097794}; Single-pass membrane protein {ECO:0000269|PubMed:20097794}.
Interaction partners:
- Mechanosensitive ion channel protein 10
- Mechanosensitive ion channel protein 9
- Hyperosmolality-gated Ca2+ permeable channel 1.1
- Mechanosensitive ion channel protein 4
- Two pore calcium channel protein 1
- Mechanosensitive ion channel protein 8
- Mechanosensitive ion channel protein 2, chloroplastic
- Hyperosmolality-gated Ca2+ permeable channel 1.2
- F-box protein At1g55000
- Calpain-type cysteine protease DEK1
Sequence:
MANSWDQLGEIASVAQLTGIDALKLIGMIVNAANTARMHKKNCRQFAHHLKLIRNLLEQIKNSEMNQRSEILEPLQGLDDALRRSYILVKSCQEKSYLYLLAMGWNIVNQFEKAQNEIDLFLKIVPLINMADNARIRERLEAIERDQREYTLDEEDRKVQDVILKQESTREAATSVLKKTLSRSYPNMGFCEALKTEEEKLQLELQRSRARYDADQCEVIQRLIDVTQTAATVEPNLEKVLTKKEELTSSKKRDDLYDTDSSSIRADSRSTSYVSSGHELLSGRSLQHRGNWHADLLDCCSEPCLCLKTLFFPCGTLAKISTVATSRQISSTEVCKNLIVYSLILSCCCYTCCIRKKLRKTLNITGGCIDDFLSHLMCCCCALVQELREVEIHRASYGTEKSNKEMSPPTPQFMEE
Protein: Probable L,D-transpeptidase ErfK/SrfK (EC 2.-.-.-) (P39176)
Organism: Escherichia coli (strain K12)
Function: Responsible, at least in part, for anchoring of the major outer membrane lipoprotein (Lpp, also known as the Braun lipoprotein) to the peptidoglycan via a meso-diaminopimelyl-L-Lys- bond on the terminal residue of Lpp.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Probable L,D-transpeptidase YcbB
- Putative L,D-transpeptidase YafK
- Major outer membrane lipoprotein Lpp
Sequence:
MRRVNILCSFALLFASHTSLAVTYPLPPEGSRLVGQSFTVTVPDHNTQPLETFAAQYGQGLSNMLEANPGADVFLPKSGSQLTIPQQLILPDTVRKGIVVNVAEMRLYYYPPDSNTVEVFPIGIGQAGRETPRNWVTTVERKQEAPTWTPTPNTRREYAKRGESLPAFVPAGPDNPMGLYAIYIGRLYAIHGTNANFGIGLRVSQGCIRLRNDDIKYLFDNVPVGTRVQIIDQPVKYTTEPDGSNWLEVHEPLSRNRAEYESDRKVPLPVTPSLRAFINGQEVDVNRANAALQRRSGMPVQISSGSRQMF
Protein: Vascular SH2 domain-containing protein (A2AM67)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MQRAGAGARRASDCGPAPYRPRCIAKLAQYVGSFPVDDLDTQESVGLVQQQLWALQDCSRRRAVILKFSLQGLKIYSGEGEVLLMAHALKRILYATWYPAACQFAFIARNPRSPSSKLFCHLFVGSQPGEVHILYLLLCRSFQLAYLLQHPEERAQSEPCLAPVGDLSLKPLCSPGVPPALVREPFSRDQLSQNVHALVSFRRLPAEGLLGSNGKELPESEGRGGTRHIRLGNPYCSPTLVRKKAIRSKVIRSGAYRGCTYETQLQLSAREAFPAAWEAWPRGPGGPSCLVENEGSLTENIWAFAGLSRSCALSLLRRDVHGAFLLWPEPGTSDQWSLSVRTQCGVVPHQVFRNHLGRFCLEHLPAEFPSLEALVESHAGVERSLFCPLSMGRLNPTYEEQDCGTEGRFPRTLRPLSHAKSEAELQGLG
Protein: Ensconsin, isoform D (Q8IRB9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASLGGQHGNISTNPEVENTAKRPESREGSAERKASKDREEKLKYARDRQNEERHRKIEELRAQAEAAQRYREQKEEERRRRIEEIRTRDTEKRHQVEERKKAIFEAEKERREYILKKNQERESRIEVKKRDRNSIGFAFGSSTPRLLDVPADYGLVSPSAFWGQRRSTSISNVAGASLTRRSSERELADSGAKKRASSSTDRQDDHRRKSSSMYEVFNWGYSNDEPPKRFSLSIAGSEINIDGPANPHPPPTSKQTANAHRPTNLTTTTATSTTTAGHNNFNNNNSYRKEDSVDSSPMVFRSVYRRKTDLMPTIPSPRDGHYGSRGSLSSTPARTPGSRSGNATPGGHFNNSRPGSAMSTSTNMSTSGLVPRRPATAPRKPRPASIAGTGMSLEEINKLKRDQKPPVKTTAASPSAQTTPKRTANLMSTSLIVTSSSSRLSSAEKKTPSKREPPVPKAASASKALPSRTASSERISRLTKEPKTKDTSAMTRSMIVTSSSTSTITKPAPAPVAPTSAPVPEQNGVAKEVEKTTADEPVPEAEVPTEAPVVVPSVSKAEKEALNTEKTEEGARQEEEQILAVESVPEALVTSINVEEKSDEGNEKEVPKPQEQAAPKKPSRSKENSEVRELTPPEGADLMTASMMAKKITTEEEAKAALAERRRLAREEAERQAELERQRLEAERLAEIKAQEEEAERQRLFEEESTRLAEEQRRGEEERLRKAIEEAQQREEEEKRRREEEEKQRVEREEAEKKAKEEAEKQRVEVAERLKREEKEREERRKRVEAIMLRTRKGGAATTPSKDANDKAAPAATAPENNSSSNSSVTGSSNNSAEGSPSAADSTPAPTATETVQEAPNSQAMYEQSVLDKENSLINSFSTMIIDENAKNLQQVSNGKLLVDFESTNTVPAVANGNGHIENVNNKNDINLLQDVVAPVATQLIDLSIESQDLHLNNNNSLLTSTAATTTLVTADSHENKDISLL
Protein: 5'-3' exoribonuclease 2 (EC 3.1.13.-) (Q5AMG5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Possesses 5'->3' exoribonuclease activity. Required for the processing of nuclear mRNA and rRNA precursors. May promote termination of transcription by RNA polymerase II (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Decapping nuclease RAI1
- CID domain-containing protein
- 5'-3' exoribonuclease 1
- Decapping enzyme complex catalytic subunit
- Endoribonuclease YSH1
- Decapping nuclease
- DNA/RNA helicase
- Pentafunctional AROM polypeptide
- Exosome nuclease subunit
- Ribosome biogenesis protein ERB1
Sequence:
MGVPALFRWLSRKYPKIISPVVEEEDHEIGGAKYENPNPNGEIDNLYLDMNGIVHPCSHPEHKKPPETEDEMFLDIFKYTDRVLMMARPRKVLMIAVDGVAPRAKMNQQRARRFRAAKDAELKAKQLEIEVQERELRGEIINDAIKGKKQWDSNAITPGTPFMDRLAEALRYWVAYKLSSDPGWANLQVIISDATVPGEGEHKLMSFIRSQRSDPQYDPNTKHCIYGLDADLIFLGLATHEPHFRVLREDVFASQDKKFTIKDQIADANSNGDTVAKEDKKPFLWLHVNVLREYLQVELFTPRMSFPFELERAIDDWVFLCFFAGNDFLPHLPSLDVRDNGIDTLVQCWKRSLPILKDYVTCDGKLNLKSVEVLMSNLAYKESEIFKNKHAAEQRREENNKRRKLAQEQERALKRVYSSQVSKGKDKAPLTADVNMPLMDTSGQNVEGYANLTNSDIVQNRAILTKANLANSDAAAELKKLIDSKKTQVTVVQDQIATDSSANSETTTSESELEEIQSDNSLKRKLEPEEDKQTQSDDIKLWEPGYNKRYYEAKFHCQSDEEIEQTKRDVVRHYVEGIAWVALYYYQGCPSWNWYFPYHYAPFAADFTNLEELFPEGVKFKLGEPFRPFEQLMSVLPAASGHTLPQVFRDLMSNPDSEIIDFYPEEFEIDMNGKKMSWQGIPLLPFIDEKRLLDAVQKKYELLTPDEKSRNTNKEAELFISPANKNFSKFSEKLYKENENEVTFKYAKSGLSGKIFKLGTFNPEGVFNFPLNEGYMPNVNNSDYFQAIYHFPKTKTGKSMILNGHIAPLPALTTADKNDLLYQLDKFNNRRNGGRFNSTLDNSDYINKGPAGKELYKTYSMRRGGYRSYLQYLTNGHHPDHQSQNSQYLSYGQQKPYGGQGSYNQQGYYNQQGRYNQQGNNYNQQGRYSQQSQYNQYRSNTQRFNNNQNYNQSSNNSRSGYLPPRPQR
Protein: Integrin alpha-6 isoform X1 (Integrin, alpha 6a) (A8WHQ8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
- Integrin beta.
- Integrin beta
- Integrin beta
- Integrin beta
- Integrin beta
- Integrin, alpha 6b
- Integrin, alpha 6,-like
- Laminin, gamma 2.
- Laminin, beta 1a.
- Laminin subunit gamma-1
Sequence:
MELFEKALSLNLCVFSWLVWTSASAFNLDTQNVLRKSGQPGSLFGFSIALHRQLQPHDKTILLIGAPKARALSNQGANVTGGLYSCDITTHPNDCSRVDFDNDVDVRVENKENQWMGVTVQSQGPGGKIVTCAHRYQRLLFPNTPQEARDITGRCYMLSQDLSIDNQSDEDGGNWKFCDGRTRGHERFGACQQGLAATFTKDYHYVIFGAPGAYNWKGIVRIEQKNNTLLEMGLFDDGPYEVGDENRLDPNLVPVPANSYLGFSLDSGHSITEKGKLIIVSGAPRANHSGAVVFLRKEGELSSMLTPEHILEGPGLASSFGYDVAVVDLNGDGWQDVVVGAPQFFQRDEEVGGAVYVYINKAGRWRDVTPVRLNGTKDSMFGLSVENIGDVNLDSFEDIAVGAPYADSGFGSVYIYHGSADGISTKPAQILEGKQHNTKMFGYSLAGNMDLDHNSYPDLAVGSLSDTVFIYRSKNVISIKKDIKVTPKEIDLTKKTCGNSICLTVEACFSYRANPTTYNPKITISCTFEAEWYRRKLGLPSRVVFLDKTEIDQDYQSTGTLELRGQNKKACYKTKLRLQDGIRDKLRAIPIEVSVAIQSAKRGKRQSSLPQLVPILDSTVPNKTLTEVNFLKEGCGTDNICQSNLNLQYRFCYRESKQDIFPPLPLENGVPVISLSDQKDIALEVTVRNRNGDDAHEAKLVSHFDDSLSYSGFRSLRTNDKHVICAANQNGSLADCELGNPFKRDSEVTFYIILSTGKISLETKEVEIDLQLETTSSQEGLSKVKAKAKVVIELLLSVQGVAKPSQVYFGGEVKGMSAMKKEEEVGSLIEYEFRVINLGKPLKSFGTASLNIQWPKESSVGKWLLYLMKINTRDLQLVTCSPEREINPLKLREDSSIRKKRELEERRPSEGNKISLFTDKRKHKILSCSGDARCVEIKCPLQGLDSTAVIVLKSRLWNSTFLEDFASYNYLDIIVKASISLDVSAKNIVLKNPETQVRLTVFPETTATPFGGVPWWIILVAVLAGILMLALLVLLLWKCGFFKRSKYEDSVPKYHAVRIRKETRLLKDGKVMLDPFEKKQWMTTWDENESYS
Protein: Reticulon-like protein 1 (Q04947)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Reticulon-like protein 2
- Saccharopepsin
- Protein SEY1
- Protein YOP1
- Pore membrane protein of 33 kDa
- Peroxisomal membrane protein PEX30
- Endoplasmic reticulum junction formation protein lunapark
- Nucleoporin NDC1
- Pore and endoplasmic reticulum protein of 33 kDa
- Vesicle-associated membrane protein-associated protein SCS2
Sequence:
MSASAQHSQAQQQQQQKSCNCDLLLWRNPVQTGKYFGGSLLALLILKKVNLITFFLKVAYTILFTTGSIEFVSKLFLGQGLITKYGPKECPNIAGFIKPHIDEALKQLPVFQAHIRKTVFAQVPKHTFKTAVALFLLHKFFSWFSIWTIVFVADIFTFTLPVIYHSYKHEIDATVAQGVEISKQKTQEFSQMACEKTKPYLDKVESKLGPISNLVKSKTAPVSSTAGPQTASTSKLAADVPLEPESKAYTSSAQVMPEVPQHEPSTTQEFNVDELSNELKKSTKNLQNELEKNNA
Protein: Ascorbate-specific PTS system EIIC component (Ascorbate-specific permease IIC component UlaA) (P39301)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Ascorbate-specific PTS system EIIA component
- Ascorbate-specific PTS system EIIB component
- Probable L-ascorbate-6-phosphate lactonase UlaG
- L-ribulose-5-phosphate 3-epimerase UlaE
- 3-keto-L-gulonate-6-phosphate decarboxylase UlaD
- L-ribulose-5-phosphate 4-epimerase UlaF
- HTH-type transcriptional regulator UlaR
- Phosphocarrier protein HPr
- Putative L-ribulose-5-phosphate 3-epimerase SgbU
- 3-keto-L-gulonate-6-phosphate decarboxylase SgbH
Sequence:
MEILYNIFTVFFNQVMTNAPLLLGIVTCLGYILLRKSVSVIIKGTIKTIIGFMLLQAGSGILTSTFKPVVAKMSEVYGINGAISDTYASMMATIDRMGDAYSWVGYAVLLALALNICYVLLRRITGIRTIMLTGHIMFQQAGLIAVTLFIFGYSMWTTIICTAILVSLYWGITSNMMYKPTQEVTDGCGFSIGHQQQFASWIAYKVAPFLGKKEESVEDLKLPGWLNIFHDNIVSTAIVMTIFFGAILLSFGIDTVQAMAGKVHWTVYILQTGFSFAVAIFIITQGVRMFVAELSEAFNGISQRLIPGAVLAIDCAAIYSFAPNAVVWGFMWGTIGQLIAVGILVACGSSILIIPGFIPMFFSNATIGVFANHFGGWRAALKICLVMGMIEIFGCVWAVKLTGMSAWMGMADWSILAPPMMQGFFSIGIAFMAVIIVIALAYMFFAGRALRAEEDAEKQLAEQSA
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 3B (SMEK homolog 2) (Q5MIZ7)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18487071}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18487071}. Nucleus {ECO:0000269|PubMed:18487071}. Note=In interphase localized in the cytoplasm and (with higher levels) the nucleus. During metaphase located in pericentriolar regions.
Interaction partners:
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 3A
- CREB-regulated transcription coactivator 2
- Protein PPP4R3C
- Serine/threonine-protein phosphatase 4 regulatory subunit 1
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Ran-specific GTPase-activating protein
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
Sequence:
MSDTRRRVKVYTLNEDRQWDDRGTGHVSSTYVEELKGMSLLVRAESDGSLLLESKINPNTAYQKQQDTLIVWSEAENYDLALSFQEKAGCDEIWEKICQVQGKDPSVEVTQDLIDESEEERFEEMPETSHLIDLPTCELNKLEEIADLVTSVLSSPIRREKLALALENEGYIKKLLQLFQACENLENTEGLHHLYEIIRGILFLNKATLFEVMFSDECIMDVVGCLEYDPALAQPKRHREFLTKTAKFKEVIPITDSELRQKIHQTYRVQYIQDIILPTPSVFEENFLSTLTSFIFFNKVEIVSMLQEDEKFLSEVFAQLTDEATDDDKRRELVNFFKEFCAFSQTLQPQNRDAFFKTLAKLGILPALEIVMGMDDLQVRSAATDIFSYLVEFSPSMVREFVMQEAQQSDDDILLINVVIEQMICDTDPELGGAVQLMGLLRTLIDPENMLATTNKTEKSEFLNFFYNHCMHVLTAPLLTNTSEDKCEKDFFLKHYRYSWSFICTPSHSHSHSTPSSSISQDNIVGSNKNNTICPDNYQTAQLLALILELLTFCVEHHTYHIKNYIMNKDLLRRVLVLMNSKHTFLALCALRFMRRIIGLKDEFYNRYITKGNLFEPVINALLDNGTRYNLLNSAVIELFEFIRVEDIKSLTAHIVENFYKALESIEYVQTFKGLKTKYEQEKDRQNQKLNSVPSILRSNRFRRDAKALEEDEEMWFNEDEEEEGKAVVAPVEKPKPEDDFPDNYEKFMETKKAKESEDKENLPKRTSPGGFKFTFSHSASAANGTNSKSVVAQIPPATSNGSSSKTTNLPTSVTATKGSLVGLVDYPDDEEEDEEEESSPRKRPRLGS
Protein: Solute carrier family 25 member 33 (Bone marrow stromal cell mitochondrial carrier protein) (BMSC-MCP) (HuBMSC-MCP) (Protein PNC1) (Q9BSK2)
Organism: Homo sapiens (Human)
Function: Mitochondrial transporter that imports/exports pyrimidine nucleotides into and from mitochondria. Selectively transports uridine, thymidine, guanosine, cytosine and inosine (deoxy)nucleoside di- and triphosphates by an antiport mechanism. May import (deoxy)nucleoside triphosphates in exchange for intramitochondrial (deoxy)nucleoside diphosphates, thus providing precursors necessary for de novo synthesis of mitochondrial DNA and RNA while exporting products of their catabolism. Participates in mitochondrial genome maintenance, regulation of mitochondrial membrane potential and mitochondrial respiration. Upon INS or IGF1 stimulation regulates cell growth and proliferation by controlling mitochondrial DNA replication and transcription, the ratio of mitochondria-to nuclear-encoded components of the electron transport chain resulting in control of mitochondrial ROS production. Participates in dendritic cell endocytosis and may associate with mitochondrial oxidative phosphorylation.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:14715278}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial carrier homolog 1
- Mitochondrial carrier homolog 2
Sequence:
MATGGQQKENTLLHLFAGGCGGTVGAIFTCPLEVIKTRLQSSRLALRTVYYPQVHLGTISGAGMVRPTSVTPGLFQVLKSILEKEGPKSLFRGLGPNLVGVAPSRAVYFACYSKAKEQFNGIFVPNSNIVHIFSAGSAAFITNSLMNPIWMVKTRMQLEQKVRGSKQMNTLQCARYVYQTEGIRGFYRGLTASYAGISETIICFAIYESLKKYLKEAPLASSANGTEKNSTSFFGLMAAAALSKGCASCIAYPHEVIRTRLREEGTKYKSFVQTARLVFREEGYLAFYRGLFAQLIRQIPNTAIVLSTYELIVYLLEDRTQ
Protein: MBL-associated serine protease 1 (Mannan-binding lectin serine protease 1 isoform 2 precursor) (A0A2R8QH04)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MELTRVFVILAQCVWPLWTQVIPLSDMYGTIKSPNFPEPYPKETDLQWNITVPDGYQIRLYFMHFDIEPSYLCEYDYLKVYSDIEELAVFCGREKTDTERVPASDIILSPGNVLSVAFRSDFSNEERYFGFEAHFSAIDVDECRDRNDEDLVCDHFCHNYIGGFYCSCRFGFLLHSDNRTCKVECNKNVYTERSGEITSADFPKAYPKSSECKYSIELEEGFQVSLEFDDTFDIEDHPEVSCPYDFIKIQAGEKEFGPFCGEKSPGKIQTGSNIVNILFHSDNSGENLGWKLTYTSTGPECSPPTPLLNGQLEPLQPIYIFRDHITLTCDPGYLLRQGDEEFEHYQIECLRDGKWSSGVPLCKKKESQRRSRSLLSILTNQILS