wanglab/gogpt-training-data huggingface dataset:
Protein: Enamidase (EC 3.5.2.18) (Q0QLE9)
Organism: Eubacterium barkeri (Clostridium barkeri)
Function: Decyclization of 6-oxo-1,4,5,6-tetrahydronicotinate to form 2-(enamine)glutarate, followed by hydrolysis to form (S)-2-formylglutarate.
Interaction partners:
- 6-hydroxynicotinate reductase
- Amino acid synthesis
- Uncharacterized protein
- L-serine dehydratase
- 2-methyleneglutarate mutase
- 2-
- Putative repair enzyme for 2-methyleneglutarate mutase
- Nicotinate dehydrogenase medium molybdopterin subunit
Sequence:
MSKTIIKNIGKIVSGDIKSPVLQADTIVVEDGLIAAIGGEELMKDAGDATIIDAAGSTVTPGLLDTHVHVSGGDYAPRQKTMDFISSALHGGVTTMISAGSPHFPGRPKDAAGTKALAITLSKSYYNARPAGVKVHGGAVILEKGLTEEDFIEMKKEGVWIVGEVGLGTIKNPEDAAPMVEWAHKHGFKVQMHTGGTSIPGSSTVTADDVIKTKPDVVSHINGGPTAISVQEVDRIMDETDFAMEIVQCGNPKIADYVARRAAEKGQLGRVIFGNDAPSGTGLIPLGILRNMCQIASMSDIDPEVAVCMATGNSTAVYGLNTGVIAPGKEADLIIMDTPLGSVAEDAMGAIAAGDIPGISVVLIDGEAVVTKSRNTPPAKRAAKIL
Protein: Sporulation-specific cell division protein SsgB (Sporulation of Streptomyces griseus-like protein B) (SsgA-like protein B) (SALP B) (Q2JDA6)
Organism: Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3)
Function: Involved in sporulation-specific cell division. Required for early stages of sporulation. Important in the process of growth cessation prior to sporulation-specific cell division. Recruits cell division protein FtsZ to the future septum sites and tethers the contractile ring structure (Z ring) to the cytoplasmic membrane during sporulation. Stimulates polymerization and filament length of FtsZ in vitro (By similarity).
Subcellular location: Cell septum {ECO:0000250|UniProtKB:Q9L268}. Note=Localizes to the divisome in sporogenic aerial hyphae in a ladder-like manner. Temporospatial localization is controlled by SsgA and it colocalizes with SsgA in presporulation foci. Localizes to the septum sites prior to FtsZ and after that colocalizes with FtsZ at the divisome throughout cell division. {ECO:0000250|UniProtKB:Q9L268}.
Interaction partners:
- Transcriptional regulator, XRE family
- Transcriptional regulator, XRE family
- Transcriptional regulator, XRE family
- Uncharacterized protein
- Transcriptional regulator, XRE family
- RNA-binding protein
Sequence:
MTIRHDSITAELALRLVVPGGAPVPVAATVRYEPADPYAISIGFRTGADEVVEWTFARQLLSDGVRRPAGDGDVQVWPAAQSGGRIVCLSLSSPSGHALFEMPRSEVLAFLRRTYSAVPLGGESDIIDLDAELALLIWGGPER
Protein: Circadian clock oscillator protein KaiC (EC 2.7.11.1) (EC 3.6.4.-) (Q79PF4)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: The KaiABC oscillator complex constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation; KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. The Kai complex controls chromosome condensation, leading to a transcription accessible chromosome during the first half of the circadian cycle and a compact, less transcription-accessible chromosome during the latter half. Clock output pathways impact the RpaA transcriptional regulator. Circadian oscillations can be generated in vitro by incubating KaiA, KaiB and KaiC with 1 mM ATP. The cycle is self-sustainable for at least 3 cycles and resistant to temperature changes. Mutations in KaiC alone prolong or reduce the circadian rhythm. A very robust clock is reconstituted with KaiA, KaiB, KaiC, SasA, CikA and RpaA; output is measured by transcription from an appropriate reporter.
Interaction partners:
- Circadian clock oscillator protein KaiB
- Circadian clock oscillator protein KaiA
- Adaptive-response sensory kinase SasA
- Circadian input-output histidine kinase CikA
- Protein RecA
- Low amplitude and bright protein LabA
- Light dependent period A
- Thiamine-phosphate synthase
- Amidophosphoribosyltransferase
- Circadian phase modifier
Sequence:
MTSAEMTSPNNNSEHQAIAKMRTMIEGFDDISHGGLPIGRSTLVSGTSGTGKTLFSIQFLYNGIIEFDEPGVFVTFEETPQDIIKNARSFGWDLAKLVDEGKLFILDASPDPEGQEVVGGFDLSALIERINYAIQKYRARRVSIDSVTSVFQQYDASSVVRRELFRLVARLKQIGATTVMTTERIEEYGPIARYGVEEFVSDNVVILRNVLEGERRRRTLEILKLRGTSHMKGEYPFTITDHGINIFPLGAMRLTQRSSNVRVSSGVVRLDEMCGGGFFKDSIILATGATGTGKTLLVSRFVENACANKERAILFAYEESRAQLLRNAYSWGMDFEEMERQNLLKIVCAYPESAGLEDHLQIIKSEINDFKPARIAIDSLSALARGVSNNAFRQFVIGVTGYAKQEEITGLFTNTSDQFMGAHSITDSHISTITDTIILLQYVEIRGEMSRAINVFKMRGSWHDKAIREFMISDKGPDIKDSFRNFERIISGSPTRITVDEKSELSRIVRGVQEKGPES
Protein: Cytoskeleton associated protein 5 (H0YCF6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XRKGPAEDMSSKLKIMYRTYRIQARSMSGHPEAAQMVRREFQLDLDEIENDNGTVRCEMPELVQHKLDDIFEPVLIPEPKIRAVSPHFDDMHSNTASTINFIISQVASGDINTSIQALTQLRLIYNTHMADEKLEKDEIIKLYSCIIGNMISLFQIESLAREASTG
Protein: TRM32-like protein (DUF3741) (Q9LZ87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transducin/WD40 repeat-like superfamily protein
- Heavy metal transport/detoxification superfamily protein
- Chromatin remodeling 34
- Heavy metal-associated isoprenylated plant protein 17
- Sugar transport protein 8
- F-box/LRR-repeat protein 12
- 14-3-3-like protein GF14 omicron
- At4g28530
Sequence:
MGKNLRHKVTCSPIQNHPGFMWGLFDILKHNHWRYIKKRLPHKRPVCRRTAPGTKNEVNNTIPSSPDGIPVPKIKLEDKTDVESVQRPKKPSSAVKSKESSNSGEKTKKKHNPEEKSKKLNSEERSRKTHSEIKRSVKALIKALVIEDKSKKKGRHHRSCTYPVQSNSKEKDSLSEVGSSDKNSSNGDERNRVFNKKVGISPAVGSLNPLYLMSEESSNSDSEEFRVDNNIQVDDNTDGSKSDFDEKEFKKKEKSDDEEAWFDPKMRHTKGFSENDDDTSPRRSKACLDALNLIHMNRNFLLKVLQDPGSPLARHFQSQQSFSSKTMTKAGSFPTHGINREDHNKAFDPVGDVDKIPMSPPSIAAEHRADGIQKMNETVLKLGDEDSSGSGYARKRGKNQVVIKRFKDLRQKIKHVINENKNEKHRITMDAVLDKVPRKYGFSKDLRDDIFEHLKGNSAAKNNNKAEGTKLKQITRASSLCGSLDRYLQLYECSFQREAKNSSNSEKSKMELEESALPSKRAPKFLGRILSLPQMKFHALKIDDLTVQSIEEEQDGLDNISEISEDHSQSSEHETLDQTMDASEDSPVDAETEQDREISTLDVEHETRSLKESSEESPNNVSTVDIDENASVFDISRDLDTETVSTSKQLDEEVLNIDAQDKVKFNYVRDILEISGFNAPESLSMWQLDYQPLDPLVYEEVTTTTTGCMFQDPECSRNEEEGGNCNHLLLFDLINEVLIEIYERSYHYYPKPLSSLCKIHPMPVGYSVLKEVWVRISCYLRYKPYDEQQSFDKVMSRDLSRDDGWMDLQFESECVGIEVEDLIFEELLEELLISC
Protein: SPARC (Osteonectin) (Secreted protein acidic and rich in cysteine) (Q6IQH0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MRVWIFFLFCLAGKTLAAPTEEEPAVEEELEVGINPVQVETGEFDEAIEVVEDVIAENPCLNHHCKKGKVCEVDDSNQPMCVCQDPLTCPAPIGDFEHVCGTNNKTYESSCHFFATKCSLEGTKKGHKLHIDYIGPCKYIAPCLENELNEFPLRMRDWLKNVLVTLYERDEDNNLLTEKQKLRVKKIYENEKRLQAGDHSLDLLALDFEKNYNMYIFPVHWQFGQLDQHPIDGFLSHTELAPLRAPLIPMEHCTTSFFEQCDADQDKYIALEEWANCFGIKEQDVDKDLVI
Protein: Alcohol dehydrogenase 4 (EC 1.1.1.1) (Alcohol dehydrogenase IV) (ADHIV) (P10127)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Alcohol dehydrogenase 3, mitochondrial
- Alcohol dehydrogenase 1
- Alcohol dehydrogenase 2
- S-
- Alcohol dehydrogenase 5
- Pyruvate decarboxylase isozyme 2
- Pyruvate decarboxylase isozyme 1
- Pyruvate decarboxylase isozyme 3
- Thiamine metabolism regulatory protein THI3
- Magnesium-activated aldehyde dehydrogenase, cytosolic
Sequence:
MSSVTGFYIPPISFFGEGALEETADYIKNKDYKKALIVTDPGIAAIGLSGRVQKMLEERDLNVAIYDKTQPNPNIANVTAGLKVLKEQNSEIVVSIGGGSAHDNAKAIALLATNGGEIGDYEGVNQSKKAALPLFAINTTAGTASEMTRFTIISNEEKKIKMAIIDNNVTPAVAVNDPSTMFGLPPALTAATGLDALTHCIEAYVSTASNPITDACALKGIDLINESLVAAYKDGKDKKARTDMCYAEYLAGMAFNNASLGYVHALAHQLGGFYHLPHGVCNAVLLPHVQEANMQCPKAKKRLGEIALHFGASQEDPEETIKALHVLNRTMNIPRNLKELGVKTEDFEILAEHAMHDACHLTNPVQFTKEQVVAIIKKAYEY
Protein: Viral macrophage inflammatory protein 2 (Viral macrophage inflammatory protein II) (vMIP-II) (vMIP-1B) (Q98157)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Blocks infection by several different human immunodeficiency virus type 1 (HIV-1) strains. This occurs because vMIP-II binds to a wide range of chemokine receptors. May form part of the response to host defenses contributing to virus-induced neoplasia and may have relevance to KSHV and HIV-I interactions.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MDTKGILLVAVLTALLCLQSGDTLGASWHRPDKCCLGYQKRPLPQVLLSSWYPTSQLCSKPGVIFLTKRGRQVCADKSKDWVKKLMQQLPVTAR
Protein: Serine/threonine protein phosphatase 2A regulatory subunit (Q9VB23)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- Serine/threonine-protein phosphatase PP2A
- Protein phosphatase PP2A 55 kDa regulatory subunit
- MIP22305p
- Uncharacterized protein, isoform B
- Shugoshin
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase
- Well-rounded, isoform B
- Cyclin G
Sequence:
MSSGTFVDRIDPFAKRSLKKKGKKSQGSSRYRNSQDVELQQLPPLKADCSSLEQEELFIRKLRQCCVSFDFMDPVTDLKGKEIKRAALNDLSTYITHGRGVLTEPVYPEIIRMISCNLFRTLPPSENPDFDPEEDDPTLEASWPHLQLVYEVFLRFLESQDFQATIGKRVIDQKFVLQLLELFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNIFLRFIYETEHFNGVGELLEILGSIINGFALPLKAEHKQFLVKVLLPLHKVKCLSLYHAQLAYCIVQFLEKDPFLTEPVVRGLLKFWPKTCSQKEVMFLGEIEEILDVIDPPQFVKIQEPLFRQIAKCVSSPHFQVAERALYLWNNEYAMSLIEENNAVIMPIMFPALYRISKEHWNQTIVALVYNVLKTFMEMNSKLFDELTSSYKAERQKEKKRERDREELWKKLHELESNRSSGRTAGGSATTSNSAASAASTSLQPPSSAGLNSHQQQSNSGSSGSLSSGGAGGDNNPATTNAKIKQDKADN
Protein: Scinderin (Adseverin) (Gelsolin-like protein) (Q60604)
Organism: Mus musculus (Mouse)
Function: Ca(2+)-dependent actin filament-severing protein that has a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane. Severing activity is inhibited by phosphatidylinositol 4,5-bis-phosphate (PIP2) (By similarity). In vitro, also has barbed end capping and nucleating activities in the presence of Ca(2+). Required for megakaryocyte differentiation, maturation, polyploidization and apoptosis with the release of platelet-like particles (By similarity). Plays a role in osteoclastogenesis (OCG) and actin cytoskeletal organization in osteoclasts. Regulates chondrocyte proliferation and differentiation (By similarity). Inhibits cell proliferation and tumorigenesis. Signaling is mediated by MAPK, p38 and JNK pathways (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, podosome {ECO:0000269|PubMed:25681458}.
Interaction partners:
- Src substrate cortactin
- Hematopoietic lineage cell-specific protein
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- Talin-1
- Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma
- Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
- Gelsolin
Sequence:
MAQELQHPEFARAGQQAGLQVWRVEKLELVPVPQGAYGDFYVGDAYLVLHTTKSSRGFSYRLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQSRELQGYESTDFVGYFKGGLKYKAGGVASGLNHVLTNDLTAKRLLHVKGRRVVRATEVPLSWESFNKGDCFIIDLGTEIYQWCGSSCNKYERLKASQVAIGIRDNERKGRSQLIVVEEGSEPSELMKVLGRKPELPDGDNDDDVVADISNRKMAKLYMVSDASGSMKVTLVAEENPFSMGMLLSEECFILDHGAAKQIFVWKGKNANPQERKTAMKTAEEFLQKMKYSTNTQIQVLPEGGETPIFKQFFKDWKDKDQSDGFGKVYITEKVAQIKQIPFDASKLHSSPQMAAQHNMVDDGSGGVEIWRVENSGRVQIDPSSYGEFYGGDCYIILYTYPRGQIIYTWQGANATRDELTMSAFLTVQLDRSLGGQAVQVRVSQGKEPAHLLSLFKDKPLIIYKNGTSKKEGQAPAPPTRLFQVRRNLASITRIVEVDVDANSLNSNDTFVLKLPRNNGFIWIGKGASQEEEKGAEYVADVLKCKASRIQEGKEPEEFWNSLGGRGDYQTSPLLETRAEDHPPRLYGCSNKTGRFIIEEVPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESVKSAKMYLETDPSGRDKRTPIVIIKQGHEPPTFTGWFLGWDSSRW
Protein: PHD finger-like domain-containing protein 5A (PHD finger-like domain protein 5A) (Splicing factor 3B-associated 14 kDa protein) (SF3b14b) (Q7RTV0)
Organism: Homo sapiens (Human)
Function: Involved with the PAF1 complex (PAF1C) in transcriptional elongation by RNA polymerase II, and in regulation of development and maintenance of embryonic stem cell (ESC) pluripotency. Required for maintenance of ESCs self-renewal and cellular reprogramming of stem cells. Maintains pluripotency by recruiting and stabilizing PAF1C on pluripotency genes loci, and by regulating the expression of the pluripotency genes. Regulates the deposition of elongation-associated histone modifications, including dimethylated histone H3 'Lys-79' (H3K79me2) and trimethylated histone H3 'Lys-36' (H3K36me3), on PAF1C targets, self-renewal and pluripotency genes. Regulates RNA polymerase II promoter-proximal pause release of the PAF1C targets and self-renewal genes, and the levels of elongating ('Ser-2' phosphorylated) RNA polymerase II in their gene bodies. Regulates muscle specification in adult stem cells by stabilizing PAF1C in chromatin to promote myogenic differentiation (By similarity). Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. Acts as a transcriptional regulator by binding to the GJA1/Cx43 promoter and enhancing its up-regulation by ESR1/ER-alpha (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300}. Nucleus speckle {ECO:0000250|UniProtKB:P83870}.
Interaction partners:
- Splicing factor 3B subunit 1
- Splicing factor 3A subunit 3
- Splicing factor 3B subunit 6
- Splicing factor 3B subunit 4
- RNA-binding motif protein, X-linked 2
- Splicing factor 3B subunit 5
- Small nuclear ribonucleoprotein G
- Splicing factor 3A subunit 2
- U2 small nuclear ribonucleoprotein B''
- U4/U6.U5 tri-snRNP-associated protein 1
Sequence:
MAKHHPDLIFCRKQAGVAIGRLCEKCDGKCVICDSYVRPCTLVRICDECNYGSYQGRCVICGGPGVSDAYYCKECTIQEKDRDGCPKIVNLGSSKTDLFYERKKYGFKKR
Protein: Uncharacterized protein DKFZp586I1023 (Q7L8P3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
KNRQFFNEPEENFWMVMVVRNPIIEKQSKDGKPVIEYQEEELLDKVYSSVLRQCYSMYKLFNGTFLKAMEDGGVKLLKERLEKFFHRYLQTLHLQSCDLLDIFGGISFFPLDKMTYLKIQSFINRMEESLNIVKYTAFLYNDQLIWSGLEQDDMRILYKYLTTSLFPRHIEPELAGRDSPIRAEMPGNLQHYGRFLTGPLNLNDPDAKCRFPKIFVNTDDTYEELHLIVYKAMSAAVCFMIDASVHPTLDFCRRLDSIVGPQLTVLASDICEQFNINKRMSGSEKEPQFKFIYFNHMNLAEKSTVHMRKTPSVSLTSVHPDLMKILGDINSDFTRVDEDEEIIVKAMSDYWVVGKKSDRRELYVILNQKNANLIEVNEEVKKLCATQFNNIFFLD
Protein: Fms related receptor tyrosine kinase 3 ligand (A0A1W2Q602)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAGAIFWAAWRPLWPSRYCWAERWWLYAVRASTFLEISTETSKKRMVVPAALKVVRLKPTRKFAYLGRLAHEVGWKYQAVTATLEEKRKEKAKIHYRKKKQLLRLRKQAEKNVEKKICKFTEVLKTNGLLV
Protein: DNA-binding protein SATB (Special AT-rich sequence-binding protein) (A8WIP9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- T-box 1, brain
- Fez family zinc finger protein 2
- Eomesa protein
Sequence:
MERGGGESPRLRDSPERRGSSSPDIGCPPQKLGRLELNGSPTGHRSRHNGAPQRPLSGLMIPVFCVVEQMDGGMISDGESREEHAEFVLVRKDILFTQLVETALLALGYSHSSAAQAHGIIKVGRWNPLPIHYLTDAPEATVADMLLDVYHMVTLRIQLQSFAKLEDLPSEQWNHATVRNALKELLKEMNQSTLAKECPLSQSMISSIVNSSYYANVSTAKCQEFGRWYKKYKKIKGDYLWQGREGSEIKVERDNIADFCVLAQRPPPHLTALGQLGPLNSAGSLVKGNSGEPQNSAQSQPPPQGQPQPPSSLGQLHHSPPLRAQVPPPPPPAALQPLLAPGGLLSPQLSPQLVRQQLAMAHLINQQLAVSRLLHQHPQALNQQFLNHPPIPRPSKSGGPGEPGSNPSAAEVSSDIYQLVRDELKRASVSQAVFARVAFNRTQGLLSEILRKEEDPRSASQSLLVNLKAMQNFLNLPESERDRIYQEERERSMNPPVSLPPSTNPSPGAVRLSQCKTPNPDLPVKLEPLVNITSAIYDEIQQEMKRAKVSQALFAKVAANKSQGWLCELLRWKESPSPENRTLWENLCTIRRFLSLPQTDRDMVYEEESRHHHSERLHTVLHLPTDPQALHRQPMQPLKDHSPIREDPIPSSGAEENPQANTGSGNNGPVVSVTKKPRSRTKISLEALGILQSFIQDVGLYPDQEAIHTLSAQLDLPKHTIVKFFQNQRYHVKHHGRLKELGSEGGGVDVAEYRDEELLSSSEDAESSEDGHEEIYSGHESAPAGAANSVSTPALSSVQDENKDKCLPLGTVRPNSLPPCSSSSSPRDQADYQR
Protein: B-cell lymophoma 10 protein (E7EC82)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MEVSGPASSAVGRPLTEDEMADVKKEALERMRPYLCDKIIAERHFDYPRSKKILTREDTEEISSRSSSRKKTGKLLDYLAENPKGLDALVESIRRERTQNFLLQKITDIVLKVKNEKLEALKGLSCSTCMTSLYGGTNNLSRSYSDESNFFDKTKDKESTQMHNPEEDYSTAAFMSAVSLHSMNLPVAEMGNAESAVFSVTLPGPGDSGAPPLPPELQSEQQEPCTSSSDNCFLPLRSRSLHPQ
Protein: AT16851p (Q8MSN3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCRKKEALNEELMRTRQRLEQTTETNSRLNRNLEEMVKDVEEKQVVIDLHEKDTHRLNELLAALRSEKESLESVLFDTNTSLEATEERRSQLERDLQEALVREESLKNHVARLQKELEQCQRKAQETKTQLLNAARAAESDFNQKIANLQACAEEAAKRHGEEILQLRNALEKRMQQALQALQTAKDDEIEKLQERLATLQAHLESLVQQHEEALIRAESEKQQALLIAHRDKQAVAERLEAVSRDLKTEQESLDRSRREANARDEKQRAAIAQLKDEMVQMRTKEEEHKIKLEECIRKQELQLSSLREERESLCRVSEELKMEIRLKEDRMESTNNELQDALRKSKEGEGFIDSLRKELTDCRRQLADSNIERDKYSGSNKELRDHVKRVESAKREQARAIEEALQKISNLEDTKNSLENERTRLSTILKETENHFTKTTQDLNATKAQLQKAQVEFAQKDEGGKELQCKLVAEVELKERAQQELCQIKKQLSDLEANLCATRQELGRARCQNNQEEHRFHAREQELAQRLEEGRGREKRLEDQKHNLEVCLADATQQIQELKARLGGAEGRIRALDEQLSCVELHKRDTEQKLSSVVHTLRRIAGIQVDGSVNLSHRLLSPSRRFSPSRSCGDYDNRSTSQCPDGPIDVDPDLVRKGVRNLMHQVAQLEREKDDYKSQLGAAKKQLQDAADQQLRCDAKLGKLQAMLRNLQEEKSNLETDRKMKISAIQALEEKLKHRNDECQMLRERLAQTEMQLAATSEENGQNEERLEKSRQQCSKLDNEKRQLQEELAKVEGRASKLELQRVAMEGDLTRLQMALQEKDCSIRQMAERLENQNRALTQLEDRCTALKSTVDQLKERLQKSAVSETQLRGEIKTLQKELSEQGHCSQANEDKLKLVQKSLQTAENEKRILTERLDSAQTNLNELRRSQQAQLDGNQRLQEQVTDLEVQRSALESQLRIAKWNQESGGDKDLTNGNGGGNGEEELSRQLKSSQREKSELRSKLQTLQDKVKQLECDRKSKFSGGNAYDRAEKSNSFYGGAAESGEFDSNRYDVGGGNAGGGSFNCGLDHSVIEQETRDLRLKVRRLETLLAEKESELARCKARMNDSAKCHDGLDGDRYRSAQMHAEKLLDAREQSHRQQVLRLENQISMLREQLAQEAKRRQQYILLSSKANREMQHLRSTLGDSLRNVSQHPVDPHLLESESRRLDSAVSMSLPPSSCRDYDRD
Protein: glucan 1,3-beta-glucosidase (EC 3.2.1.58) (Exo-1,3-beta-glucanase) (Q6FTS0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- glucan 1,3-beta-glucosidase
- glucan 1,3-beta-glucosidase
- 1,3-beta-glucan synthase
- 1,3-beta-glucan synthase
- 1,3-beta-glucan synthase
Sequence:
MRFSTVAALAFGASQVAAIGELAFNLGVKNNDGTCKTTNDYENDLKVLKSYTSTVKVYAASDCNTLENLGPAAEAEGFNIFLGIWPNDEAHFQAEKNALSSFLPNLKSSTIAGFLVGSEALYRDDLTASQLADKINDIRNYVSNIKDSQGNSYSGKQVGTVDSWNVLVAGYNAPVITASDFVMANAFSYWQGQTMQNASYSFFDDIMQALQTIQGVKGSTDITFWVGETGWPTDGTNFEASYPSVDNAKQFWKEGICAMRAWGVNVIVFEAFDEDWKPNTSGTSDVEKHWGVWTSGDNLKYSLDCSFN
Protein: Metaxin 2 (C9JAZ1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLVAEAFVSQIAAAEPWPENATLYQQLKGEQILLSDNAASLAVQAFLQMCNLPIKVVCRANAEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAKGHSLSDGLEEVQKAEMKAYMELVNNMLLTAELYLQWCDEATVGEWEVKRKMKAIGWGKKTLDQVLEDVDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRIEQH
Protein: ATP synthase subunit b, chloroplastic (ATP synthase F(0) sector subunit b) (ATPase subunit I) (Q6ENH8)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01398}.
Interaction partners:
- ATP synthase subunit a, chloroplastic
- ATP synthase epsilon chain, chloroplastic
- ATP synthase subunit c, chloroplastic
- ATP synthase subunit alpha
- ATP synthase subunit delta', mitochondrial
- ATP synthase subunit alpha, chloroplastic
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit O
- ATP synthase subunit beta, chloroplastic
Sequence:
MKNVTHSFVFLAHWPSAGSFGLNTDILATNLINLTVVVGVLIYFGKGVLKDLLDNRKQRILSTIRNSEELRRGTIEQLEKARIRLQKVELEADEYRMNGYSEIEREKANLINATSISLEQLEKSKNETLYFEKQRAMNQVRQRVFQQAVQGALGTLNSCLNTELHFRTIRANISILGAMEWKS
Protein: Serine decarboxylase (AtSDC) (EC 4.1.1.-) (Protein EMBRYO DEFECTIVE 1075) (Serine decarboxylase 1) (AtSDC1) (Q9MA74)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the biosynthesis of ethanolamine from serine. Highly specific for L-serine and does not attack D-serine, L-phosphoserine, phosphatidylserine, L-histidine L-glutamate L-tyrosine or L-tryptophan. Decarboxylation of free serine is the major source of ethanolamine production in plants and ethanolamine metabolism is crucial for the synthesis of choline, phosphatidylethanolamine (PE) and phosphatidylcholine (PC), and thus for plant growth.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:22489147}.
Interaction partners:
- Histidinol dehydrogenase, chloroplastic
- Ethanolamine-phosphate cytidylyltransferase
- Cytochrome b561 and DOMON domain-containing protein At3g25290
- Probable choline kinase 2
- Phosphoethanolamine N-methyltransferase 2
- Probable choline kinase 3
- Probable choline kinase 1
- Phosphoethanolamine N-methyltransferase 3
- Choline/ethanolaminephosphotransferase 2
- 1-
Sequence:
MVGSLESDQTLSMATLIEKLDILSDDFDPTAVVTEPLPPPVTNGIGADKGGGGGEREMVLGRNIHTTSLAVTEPEVNDEFTGDKEAYMASVLARYRKTLVERTKNHLGYPYNLDFDYGALGQLQHFSINNLGDPFIESNYGVHSRPFEVGVLDWFARLWEIERDDYWGYITNCGTEGNLHGILVGREMFPDGILYASRESHYSVFKAARMYRMECEKVDTLMSGEIDCDDLRKKLLANKDKPAILNVNIGTTVKGAVDDLDLVIKTLEECGFSHDRFYIHCDGALFGLMMPFVKRAPKVTFNKPIGSVSVSGHKFVGCPMPCGVQITRMEHIKVLSSNVEYLASRDATIMGSRNGHAPLFLWYTLNRKGYKGFQKEVQKCLRNAHYLKDRLREAGISAMLNELSSTVVFERPKDEEFVRRWQLACQGDIAHVVVMPSVTIEKLDNFLKDLVKHRLIWYEDGSQPPCLASEVGTNNCICPAHK
Protein: Urease accessory protein G (AtUREG) (O64700)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the maturation and activation of urease via the functional incorporation of the urease nickel metallocenter.
Interaction partners:
- Urease accessory protein D
- Urease
- Urease accessory protein F
- Metal-dependent protein hydrolase
- Large ribosomal subunit protein uL23m
- Probable calcium-binding protein CML49
Sequence:
MASHDHHHHHHDHEHDHEKSDGGEGKASWVGKDGKVYHSHDGLAPHSHEPIYSPGYFSRRAPPLHDRNFSERAFTVGIGGPVGTGKTALMLALCRFLRDKYSLAAVTNDIFTKEDGEFLVKNGALPEERIRAVETGGCPHAAIREDISINLGPLEELSNLFKADLLLCESGGDNLAANFSRELADYIIYIIDVSAGDKIPRKGGPGITQADLLVINKTDLAAAVGADLSVMERDSLRMRDGGPFVFAQVKHGLGVEEIVNHVMHSWEHATGKKRQ
Protein: FAD-dependent urate hydroxylase (EC 1.14.13.113) (Flavoprotein urate hydroxylase) (A1TFU9)
Organism: Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii)
Function: Catalyzes the hydroxylation of urate to 5-hydroxyisourate (HIU). Is likely to be involved in the urate degradation pathway to allantoin. Prefers NADH over NADPH as the electron donor.
Interaction partners:
- FAD dependent oxidoreductase
- 
- Xanthine dehydrogenase, molybdenum binding subunit apoprotein
- Molybdopterin dehydrogenase, FAD-binding protein
- 5-hydroxyisourate hydrolase
- 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
- Uracil-xanthine permease
Sequence:
MKVVIVGAGMGGMSAAIALRQIGIDTVVYERVTENKPVGAAISVWSNGVKCLNYLGLQEETAELGGKVETMSYVDGHTGDTMCRFSMHPLIEQVGQRPYPIARAELQLMLMKAYGIDDINFGMKMVGVENDTAGSAAKATFADGTTVSADVIIGADGAGSITREYVLGGPVSRRYAGYVNYNGLVSTDDAIGPATEWTTYVGDGKRVSVMPVSDDRFYFFFDVVEPQGSPYEEGRVREVLRAHFAGWTPGVQTLIDTLDPLATNRVEILDLDPFHTWVKGRVAVLGDAAHNTTPDIGQGGCSAMEDAIALQWAFKDHPDDVHAALAAYQSARTERAADLVLRARKRCDVTHAKDPQVTSRWYDELRNEDGTNIIRGIVGNIVGGPLTPVTAATEG