wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger MYND domain-containing protein 10 homolog (Q9VU41)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in axonemal structure organization and motility. May be involved in axonemal pre-assembly of inner and outer dynein arms (IDA and ODA, respectively) for proper axoneme building for cilia motility.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23891471}. Cell projection, cilium {ECO:0000269|PubMed:23891471}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q5FWU8}. Note=Localizes mainly to the cytoplasm. Present in the cell bodies of Ch neurons. Present at low level in the cilium.
Interaction partners:
- Dynein axonemal assembly factor 5
- Dynein, axonemal, intermediate chain 2, isoform C
- Spag1 axonemal dynein assembly factor
- Putative inner dynein arm light chain, axonemal
- AT19426p
- Uncoordinated 79, isoform C
- Protein tilB
- GH13165p
- Dynein axonemal assembly factor 3 homolog
- Armadillo repeat-containing protein gudu
Sequence:
MVNFVHPEEMYLFVESIRPFEVREVGSPKWLEVHEMILGLSQQAALELSQNREEEVKEFLISRDKLRVLIHEAYCVTLWKTRVLPHLLEIDPNPQATFLIYTVLYHEAALVALLDVCLYHPSGCETLQESVLDLIDYCAQAISQVIGLVSMGYHENETKLDVDEAVLTELERQKRDFIYKIGLRCISVLNYIADNVTLFHLSAARRLLVTHDIPWLMADVLSFRPWQRKTSKGIQKFIDEKWTNVDDVTKIVKPEAQAWFCVRQLLLNPQIMENYAFNEARCKQLHKLLGLMHEPLLDQLPPLIELKVFLSRLTLSGNTAKTQPLLLEDIPQIQEELLKDVEENGGFYQIAQDQDSVFLSKNKENICALATRLSKAYGTDLLCELEQNMDDLKMGEAKDAGAGGDGDTDHTCATCQAKAKKKCACCKKVHYCSRDCQLKDWPQHKLVCLKT
Protein: CDP-diacylglycerol--serine O-phosphatidyltransferase (EC 2.7.8.8) (Phosphatidylserine synthase) (PSS) (P08456)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Microsome membrane {ECO:0000269|PubMed:6274497}; Multi-pass membrane protein {ECO:0000269|PubMed:6274497}. Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane {ECO:0000269|PubMed:3005242}; Multi-pass membrane protein {ECO:0000269|PubMed:3005242}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Phosphatidylserine decarboxylase proenzyme 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Phosphatidate cytidylyltransferase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidylethanolamine N-methyltransferase
- Cardiolipin synthase
- Choline/ethanolaminephosphotransferase 1
- Lysophospholipid acyltransferase
Sequence:
MVESDEDFAPQEFPHTDTDVIVNEHRDENDGYASDEVGGTLSRRASSIFSINTTPLAPPNATDIQKFTSDEHHFSMMRNLHMADYITMLNGFSGFYSIVSCLRFTLTGKPHYVQRAHFFILLGMCFDFLDGRVARLRNRSSLMGQELDSLADLVSFGVAPAAIAFAIGFQTTFDVMILSFFVLCGLARLARFNVTVAQLPKDSSTGKSKYFEGLPMPTTLALVLGMAYCVRKGLIFDNIPFGIFREDQILEFHPIILVFFIHGCGMISKSLKIPKP
Protein: RING/FYVE/PHD-type zinc finger family protein (F4J5R1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein TRAUCO
- Histone H4
- Protein RBL
Sequence:
MAFHVACPITCRKICFCVLGFSRNLHGNEVKDVYLKEIHSLQEFVRNPWDAEVSKDGTVQIHVPKLAVFDTGPRIAARNVGVGSDSAMEVVAASSNLVPAKRTLVLQKKAVEVYAANDCSGDLEESVFVRKRVFSDVDYLYLVSVKDLNEEDHDHHSASITCHMCYLVEVGKSERAKMLSCKCCGKKYHRNCVKSWAQHRDLFNWSSWACPSCRICEGCGTLGDPKKFMFCKRCDDAYHCDCQHPRHKNVSSGPYLCPKHTKCYSCESTVPGNGQSLRWFLGHTCCDACGRLFVKGNYCPVCLKVYRDSEATPMVCCDFCQRWVHCQCDGISDEKYMQFQVDGNLQYKCSTCRGESYQVKDLEDAVQEIWKRKDMADKDLIASLKASARVVGQTGGAPLMNQPGSVERKVSEKAMVNGEEEKPLRVLRIKSSRPQDSDSEKFGKHATELSTVKAKKLVISIGPRKTGVTNSTSCDVSKTASKSNGKQEKLQAEETFSREERRSLLGKNSDEKRGSRGEVTTLKAEGGFIGRHSDGKGDLNSGSHDSSQKDSRRLLKLKIKKHNPEGQESEAPSIVYERSKSGKGHRSKRKRASPPAEKSAFNEDEDVSLSREDSLLDEMLDASWILKKLGKDAKGKKVQIHEASDDSWEKGVVSEVGGAGGTSKLMVTLENGKVKTVELGKQGVRFVPQKQKRTRT
Protein: RAB11 family interacting protein 1 (E7EX40)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MRNNMTASMFDLSMKDKSRNPFGKLKDKIKGKNKDSGSDTASAIIPSTTPSVDSDDESVVKDKKKKSKIKTLLSKSNLQKTPLSQSMSVLPTSKPEKVLLRPGDFQSQWDEDDNEDESSSASDVMSHKRTASTDLKQLNQVNFTLPKKEGLSFLGGLRSKNDVLSRSNVCINGNHVYLEQPEAKGEIKDSSPSSSPSPKGFRKKHLFSSTENLAAGSWKEPAEGGGLSSDRQLSESSTKDSLKSMTLPSYRPAPLVSGDLRENMAPANSEATKEAKESKKPESRRSSLLSLMTGKKDVAKGSEGENPLTVPGREKEGMLMGVKPGEDASGPAEDLVRRSEKDTAAVVSRQGSSLNLFEDVQITEPEAEPESKSEPRPPISSPRAPQTRAVKPRLHPVKPMNAMATKVANCSLGTATIISENLNNEVMMKKYSPSDPAFAYAQLTHDELIQLVLKQKETISKKEFQVRELEDYIDNLLVRVMEETPNILRIPTQVGKKAGKM
Protein: DNA (cytosine-5)-methyltransferase CMT2 (EC 2.1.1.37) (Chromomethylase 2) (Protein CHROMOMETHYLASE 2) (Q94F87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the CpXpG methylation and in gene silencing.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- ATP-dependent DNA helicase DDM1
- DNA
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH4
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH5
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH6
- DNA glycosylase/AP lyase ROS1
- Transcriptional activator DEMETER
- Adenosylhomocysteinase 1
- Adenosylhomocysteinase 2
- DNA
Sequence:
MLSPAKCESEEAQAPLDLHSSSRSEPECLSLVLWCPNPEEAAPSSTRELIKLPDNGEMSLRRSTTLNCNSPEENGGEGRVSQRKSSRGKSQPLLMLTNGCQLRRSPRFRALHANFDNVCSVPVTKGGVSQRKFSRGKSQPLLTLTNGCQLRRSPRFRAVDGNFDSVCSVPVTGKFGSRKRKSNSALDKKESSDSEGLTFKDIAVIAKSLEMEIISECQYKNNVAEGRSRLQDPAKRKVDSDTLLYSSINSSKQSLGSNKRMRRSQRFMKGTENEGEENLGKSKGKGMSLASCSFRRSTRLSGTVETGNTETLNRRKDCGPALCGAEQVRGTERLVQISKKDHCCEAMKKCEGDGLVSSKQELLVFPSGCIKKTVNGCRDRTLGKPRSSGLNTDDIHTSSLKISKNDTSNGLTMTTALVEQDAMESLLQGKTSACGAADKGKTREMHVNSTVIYLSDSDEPSSIEYLNGDNLTQVESGSALSSGGNEGIVSLDLNNPTKSTKRKGKRVTRTAVQEQNKRSICFFIGEPLSCEEAQERWRWRYELKERKSKSRGQQSEDDEDKIVANVECHYSQAKVDGHTFSLGDFAYIKGEEEETHVGQIVEFFKTTDGESYFRVQWFYRATDTIMERQATNHDKRRLFYSTVMNDNPVDCLISKVTVLQVSPRVGLKPNSIKSDYYFDMEYCVEYSTFQTLRNPKTSENKLECCADVVPTESTESILKKKSFSGELPVLDLYSGCGGMSTGLSLGAKISGVDVVTKWAVDQNTAACKSLKLNHPNTQVRNDAAGDFLQLLKEWDKLCKRYVFNNDQRTDTLRSVNSTKETSGSSSSSDDDSDSEEYEVEKLVDICFGDHDKTGKNGLKFKVHWKGYRSDEDTWELAEELSNCQDAIREFVTSGFKSKILPLPGRVGVICGGPPCQGISGYNRHRNVDSPLNDERNQQIIVFMDIVEYLKPSYVLMENVVDILRMDKGSLGRYALSRLVNMRYQARLGIMTAGCYGLSQFRSRVFMWGAVPNKNLPPFPLPTHDVIVRYGLPLEFERNVVAYAEGQPRKLEKALVLKDAISDLPHVSNDEDREKLPYESLPKTDFQRYIRSTKRDLTGSAIDNCNKRTMLLHDHRPFHINEDDYARVCQIPKRKGANFRDLPGLIVRNNTVCRDPSMEPVILPSGKPLVPGYVFTFQQGKSKRPFARLWWDETVPTVLTVPTCHSQALLHPEQDRVLTIRESARLQGFPDYFQFCGTIKERYCQIGNAVAVSVSRALGYSLGMAFRGLARDEHLIKLPQNFSHSTYPQLQETIPH
Protein: Sodium-dependent phosphate transporter 1 (Gibbon ape leukemia virus receptor 1) (GLVR-1) (Leukemia virus receptor 1 homolog) (Phosphate transporter 1) (PiT-1) (Solute carrier family 20 member 1) (Q61609)
Organism: Mus musculus (Mouse)
Function: Sodium-phosphate symporter which plays a fundamental housekeeping role in phosphate transport, such as absorbing phosphate from interstitial fluid for normal cellular functions such as cellular metabolism, signal transduction, and nucleic acid and lipid synthesis. May play a role in extracellular matrix and cartilage calcification as well as in vascular calcification.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8WUM9}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium-dependent phosphate transport protein 2A
Sequence:
MESTVATITSTLAAVTASAPPKYDNLWMLILGFIIAFVLAFSVGANDVANSFGTAVGSGVVTLKQACILASIFETVGSALLGAKVSETIRNGLIDVELYNETQDLLMAGSVSAMFGSAVWQLVASFLKLPISGTHCIVGATIGFSLVANGQKGVKWSELIKIVMSWFVSPLLSGIMSGILFFLVRAFILRKADPVPNGLRALPIFYACTIGINLFSIMYTGAPLLGFDKLPLWGTILISVGCAVFCALIVWFFVCPRMKRKIEREVKSSPSESPLMEKKSNLKEDHEETKMAPGDVEHRNPVSEVVCATGPLRAVVEERTVSFKLGDLEEAPERERLPMDLKEETSIDSTINGAVQLPNGNLVQFSQTVSNQINSSGHYQYHTVHKDSGLYKELLHKLHLAKVGDCMGDSGDKPLRRNNSYTSYTMAICGMPLDSFRAKEGEQKGDEMETLTWPNADTKKRIRMDSYTSYCNAVSDLHSESEMDMSVKAEMGLGDRKGSSGSLEEWYDQDKPEVSLLFQFLQILTACFGSFAHGGNDVSNAIGPLVALYLVYKQEASTKAATPIWLLLYGGVGICMGLWVWGRRVIQTMGKDLTPITPSSGFSIELASALTVVIASNIGLPISTTHCKVGSVVSVGWLRSKKAVDWRLFRNIFMAWFVTVPISGVISAAIMAVFKYIILPV
Protein: Elongin-C (Q6PHW7)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ubiquitin-like domain-containing protein.
- Cullin-5
- Ubiquitin-like domain-containing protein.
- E3 ubiquitin-protein ligase RBX1
- CULLIN_2 domain-containing protein
- Cullin-2
- Leucine rich repeat protein 1 L homeolog isoform X1
- Suppressor of cytokine signaling 1
- RING-type domain-containing protein.
- von Hippel-Lindau disease tumor suppressor
Sequence:
MDGEEKTYGGCEGPDAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Protein: RNA-binding protein 45 (Developmentally-regulated RNA-binding protein 1) (RB-1) (RNA-binding motif protein 45) (Q8IUH3)
Organism: Homo sapiens (Human)
Function: RNA-binding protein with binding specificity for poly(C). May play an important role in neural development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12220514}. Nucleus {ECO:0000269|PubMed:12220514}. Note=Predominantly cytoplasmic. May shuttle between cytoplasm and nucleus.
Interaction partners:
- GDH/6PGL endoplasmic bifunctional protein
- RNA binding protein fox-1 homolog 3
- Glucose-6-phosphate 1-dehydrogenase
- Ribose-5-phosphate isomerase
- Ribulose-phosphate 3-epimerase-like protein 1
- Transaldolase
- TAR DNA-binding protein 43
- Ribulose-phosphate 3-epimerase
- Nestin
- Dynein regulatory complex subunit 2
Sequence:
MDEAGSSASGGGFRPGVDSLDEPPNSRIFLVISKYTPESVLRERFSPFGDIQDIWVVRDKHTKESKGIAFVKFARSSQACRAMEEMHGQCLGPNDTKPIKVFIAQSRSSGSHRDVEDEELTRIFVMIPKSYTEEDLREKFKVYGDIEYCSIIKNKVTGESKGLGYVRYLKPSQAAQAIENCDRSFRAILAEPKNKASESSEQDYYSNMRQEALGHEPRVNMFPFVGEQQSEFSSFDKNDSRGQEAISKRLSVVSRVPFTEEQLFSIFDIVPGLEYCEVQRDPYSNYGHGVVQYFNVASAIYAKYKLHGFQYPPGNRIGVSFIDDGSNATDLLRKMATQMVAAQLASMVWNNPSQQQFMQFGGSSGSQLPQIQTDVVLPSCKKKAPAETPVKERLFIVFNPHPLPLDVLEDIFCRFGNLIEVYLVSGKNVGYAKYADRISANDAIATLHGKILNGVRLKVMLADSPREESNKRQRTY
Protein: Alpha-lactalbumin (Lactose synthase B protein) (G9G9X6)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMSFVSLLLVGILFHATQAEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDHNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL
Protein: Protein GrpE (HSP-70 cofactor) (P28609)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}.
Interaction partners:
- Chaperone protein DnaK
- Chaperonin GroEL
- Chaperone protein DnaJ
- Heat shock protein 70
- Co-chaperonin GroES
- ATP-dependent protease ATPase subunit HslU
- ATP-dependent protease subunit HslV
- ATP-dependent Clp protease proteolytic subunit 1
- Heat shock protein
- Chaperone protein HtpG
Sequence:
MEKKETKSESEKTNKQDNKNTKSQKKENLNLVNSDKKIAELENEISNLKDLYLRKQAEFENFRKRLEKEKDNFVKFANETIMKDVVNFLDNLERAINSSKKSKDFDNLLTGISMIENEILSIFDKKYNLKKFGENGENFDPSRHEAISIEEKEGLKNPEIVEVYQKGYCYNDRILRTAKVKVAQSKN
Protein: Uncharacterized protein (Q3UZU4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MYLKPASNNLTVPQGHAGCHTSFTGQGTNSSETPATRMSIIQTDNFPAEPNYMGSRQQFVQSSSTFKDPERASLRDGGHGDSDQADSDQDTNKGSCCDMSVREALKMKTTSTKSQPLEQGE
Protein: Beta-defensin 22 (Defb22) (Q8BVC1)
Organism: Mus musculus (Mouse)
Function: Probable component of sperm glycocalyx. Likely protects and facilitates transport of sperm in the female reproductive tract. Probably released from the sperm surface during capacitation.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:18787081}. Secreted, extracellular space {ECO:0000269|PubMed:18787081}. Note=In the corpus epididymis, located in vesicles below the apical surface of the plasma membrane. Secreted by epididymal cells and absorbed to the surface of sperm during transit through the epididymis. Coats the entire surface of ejaculated sperm although presence on the equatorial segment is less intense. {ECO:0000269|PubMed:18787081}.
Interaction partners:
- Beta-defensin 20
Sequence:
MKSLLSTLVIIMFLAHLVTGGWYVKKCANTLGNCRKMCRDGEKQTEPATSKCPIGKLCCVLDFKISGHCGGGGQNSDNLVTAGGDEGSSAKASTAAMVGAAAMAGTPTKTSAPAKTSAPAKTSTTTKASNAAKASTTTKASNAAKASAATMAGNTTKVSTAAIASTPAQASTPTKANST
Protein: Jitterbug, isoform C (Jitterbug, isoform G) (Jitterbug, isoform H) (Jitterbug, isoform J) (Jitterbug, isoform K) (MIP03348p) (Q8MME5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSPGLTALGESTRLVPANTPAVFEILPPPGQSLSKGECVATVLTPSKSKLNARVTHEAANGAARIEFVPTEVGTHVIDASINGTKIAGGPLIAKVYDSSLIQVTEVNGGVVGQACQFRVDASAAGEGQLEISINEGEVPNHVQVVGGGRCLVSFTPEQAKSHLIDIKFNGETVRGCPFVCAVADTSRVLLNLSNLELIPVNRPSSFHITVSGGGAAELAVSVRGPQGELPVRVTGDIHAGFTAEFTPTTVGGHSINVEYNGFAVQGTPFLAKSYDASKVVVGSVSRGTMGRPVQFTVDAGDAGEGNLEITISAKGQNIPTQVHPQGSARFSVSFVPTESCEHTINVSFNKMPVPGCPITVSISGGVAGPQVSLGGPGPVHQTNSFVINHNGGRLEDIEVNVEGRRNLLY
Protein: Trans-Golgi network-localized SYP41-interacting protein 1 (TGN-localized SYP41-interacting protein 1) (F4I9A2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Tethering factor involved in vesicle fusion at the trans-Golgi network (TGN) thus being required for efficient protein trafficking to the vacuole. Implicated in resistance to salt and osmotic stresses. Modulates the cell morphology (e.g. epidermal cell file rotation (CFR) and cell expansion) in mature regions of roots and the base of hypocotyls as well as root skewing, a process leading to root movement within the soil in order to maximize anchorage and nutrient acquisition, probably by regulating microtubule stabilization independently of their orientation.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21521696}; Single-pass type IV membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MHEKDDLPQDSIADGIENDDESNGQEEEELDPDQGTAFVDSKEDMFVDAPEELNFDTPSKEALTTDDDDNDDLGTHFNIEKGDWEKELAGLQEQFKLLTGENDLTGEDGNTTVDIVSRFSKFLKTAKEERIQHEVALKELHGVISGRDDEIADLTTKISELSSSQPVSEMGDQAQNLEHLEAATDRIMVSLSNVFGEGELQYGSSISEKLAHLENRVSFLGAKYTEFYYGADQLRKCLASDVLDLSFQEDFGSALGAACSELFELKQKEAAFFERLSHLEDENRNFVEQVNREKEMCESMRTEFEKLKAELELEKTKCTNTKEKLSMAVTKGKALVQNRDALKHQLSEKTTELANRLTELQEKEIALESSEVMKGQLEQSLTEKTDELEKCYAELNDRSVSLEAYELTKKELEQSLAEKTKELEECLTKLQEMSTALDQSELDKGELAKSDAMVASYQEMLSVRNSIIENIETILSNIYTPEEGHSFDIVEKVRSLAEERKELTNVSQEYNRLKDLIVSIDLPEEMSQSSLESRLAWLRESFLQGKDEVNALQNRIESVSMSLSAEMEEKSNIRKELDDLSFSLKKMEETAERGSLEREEIVRRLVETSGLMTEGVEDHTSSDINLLVDRSFDKIEKQIRDSSDSSYGNEEIFEAFQSLLYVRDLEFSLCKEMLGEGELISFQVSNLSDELKIASQELAFVKEEKIALEKDLERSEEKSALLRDKLSMAIKKGKGLVQDREKFKTQLDEKKSEIEKLMLELQQLGGTVDGYKNQIDMLSRDLERTKELETELVATKEERDQLQQSLSLIDTLLQKVMKSVEIIALPVDLASEDPSEKIDRLAGYIQEVQLARVEEQEEIEKVKSEVDALTSKLAETQTALKLVEDALSTAEDNISRLTEENRNVQAAKENAELELQKAVADASSVASELDEVLATKSTLEAALMQAERNISDIISEKEEAQGRTATAEMEQEMLQKEASIQKNKLTEAHSTINSLEETLAQTESNMDSLSKQIEDDKVLTTSLKNELEKLKIEAEFERNKMAEASLTIVSHEEALMKAENSLSALQGEMVKAEGEISTLSSKLNVCMEELAGSSGNSQSKSLEIITHLDNLQMLLKDGGLISKVNEFLQRKFKSLRDVDVIARDITRNIGENGLLAGEMGNAEDDSTEAKSLLSDLDNSVNTEPENSQGSAADEDEISSSLRKMAEGVRLRNKTLENNFEGFSTSIDTLIATLMQNMTAARADVLNIVGHNSSLEEQVRSVENIVREQENTISALQKDLSSLISACGAAARELQLEVKNNLLELVQFQENENGGEMESTEDPQELHVSECAQRIKELSSAAEKACATLKLFETTNNAAATVIRDMENRLTEASVALEKAVLERDLNQTKVSSSEAKVESLEELCQDLKLQLENLRVKEEKWHEKEVELSTLYDKLLVQEQEAKENLIPASDMRTLFDKINGIEVPSVDLVNGLDPQSPYDVKKLFAIVDSVTEMQHQIDILSYGQKELNSTLAEKDLEIQGLKKATEAESTTELELVKAKNELSKLISGLEKLLGILASNNPVVDPNFSESWTLVQALEKKITSLLLESESSKSRAQELGLKLAGSEKLVDKLSLRVKEFEEKLQTKAIQPDIVQERSIFETPRAPSTSEISEIEDKGALGIKSISPVPTAAQVRTVRKGSTDHLSINIDSESEHLMNNNETDEDKGHVFKSLNMSGLIPTQGKIIADRVDGIWVSGGRVLMSRPQARLGVMVYSLLLHLWLLASIL
Protein: Serine protease inhibitor Kazal-type 4 (Peptide PEC-60 homolog) (O60575)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Regenerating islet-derived protein 4
- Calcium-activated chloride channel regulator 1
Sequence:
MAVRQWVIALALAALLVVDREVPVAAGKLPFSRMPICEHMVESPTCSQMSNLVCGTDGLTYTNECQLCLARIKTKQDIQIMKDGKC
Protein: 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) (P9WP25)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}.
Interaction partners:
- 4-hydroxy-tetrahydrodipicolinate reductase
- Aspartate-semialdehyde dehydrogenase
- Diaminopimelate epimerase
- Homoserine dehydrogenase
- Diaminopimelate decarboxylase
- Aspartokinase
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- Putative succinyl-diaminopimelate desuccinylase DapE
- Ribonuclease J
- Flavin-dependent thymidylate synthase
Sequence:
MTTVGFDVAARLGTLLTAMVTPFSGDGSLDTATAARLANHLVDQGCDGLVVSGTTGESPTTTDGEKIELLRAVLEAVGDRARVIAGAGTYDTAHSIRLAKACAAEGAHGLLVVTPYYSKPPQRGLQAHFTAVADATELPMLLYDIPGRSAVPIEPDTIRALASHPNIVGVKDAKADLHSGAQIMADTGLAYYSGDDALNLPWLAMGATGFISVIAHLAAGQLRELLSAFGSGDIATARKINIAVAPLCNAMSRLGGVTLSKAGLRLQGIDVGDPRLPQVAATPEQIDALAADMRAASVLR
Protein: FAD-binding PCMH-type domain-containing protein (Q9I6H4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Glycolate oxidase iron-sulfur subunit
- Electron transfer flavoprotein subunit alpha
Sequence:
MTREALIESLKPLVEPGKLLDDAASLDAYGKDWTKHFAPAPLAIVFPKSVEQVQAIVRWANQHKVGLVPSGGRTGLSAAAVAANGEVVVAFDYMNRILDFNAFDRTVVCQPGVVTKQLQTFAEENGLYYPVDFASSGSSQIGGNIGTNAGGIKVIRYGMTRNWVAGMKVVTGKGDLLELNKDLIKNATGYDMRQLFIGAEGTLGFVVEATMRLERTPKNLTAMVLGTPDFDSIMPVLHAFQSKLDLTAFEFFSDKALAKVLARGDVPRAFETDCPFYALLEFEATTEEVANEALATFEHCVEQGWVLDGVMSQSEQQLQNLWKLREYISETISHWTPYKNDISVTVSRVPAFLKDIDAIVEANYPDFEVVWFGHIGDGNLHLNILKPENLGKDEFFAKCATVNKWVFETVEKYNGSISAEHGVGMTKRDYLTYTRSETEIAYMKALKAVFDPNGIMNPGKIFAE
Protein: Uncharacterized protein (Q387J5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPPKKDVAMGKQPRIGAPQEPDVDEELELNERSQPSPANGFSPPVEVSPGTRSNTKPCVWRVQQTEGRRKEALKAMLSPTLAGRRAAVWLQEWDRGSRSVRLRILEAFLTLHSESNSRRIEVDLGDASILFFTRITAWLRLTYKLGVGLRSVLSAISVFIRGVRYLTCFAEVGGATTLADTLATGTLCVEDRQEAVLLLLYIANAGRVYREMICDENGVELLIEAMRREEDEKILDLFSALFLAVGEGSSRSLNSPVYLGLIRLLPNEETTAAAALYAARTLRTYQTSWEKKYMDSVAANNAENTGSVPVVGINPEDPVGSAQVLLDSLFALLYHSELTVRAEGSELLALVSKNLQLTGKILSRCLDVVDENRLVVEIDDDVEAIHNLRRHQITLGTTAVKVMLTDWDFEARRRIIVGLVARRSTHFTLLKFLRLLGVAQNTNAVDCCRLVQLLCREAVQQNQRGREDGEGSAGSCISLDKFSKHIHDVVGSALYSVILHEDLVDEQIEAIVRSIMSSD
Protein: Preprofallaxidin-9 [Cleaved into: Fallaxidin-2.1; Fallaxidin-3.2] (B5LUR1)
Organism: Litoria fallax (Eastern dwarf tree frog) (Hylomantis fallax)
Function: Fallaxidin-1.3 shows no antibacterial activity against Gram-positive or Gram-negative bacteria. Does not inhibit the formation of NO by neuronal nitric oxide synthase. Has no effect on splenocyte proliferation or smooth muscle contraction.
Subcellular location: Secreted {ECO:0000269|PubMed:18803332}.
Interaction partners:
Sequence:
MASLKKSLFLVLFLGLVSLSICEEEKRENEEDAEDENHEEESEEKRGLLDFAKHVIGIASKLGKRSEEKRFWPFMGKRSEEKRFWPFMGKRSEE
Protein: At1g74010 (Calcium-dependent phosphotriesterase superfamily protein) (Putative strictosidine synthase) (Q9C9C2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Vacuole {ECO:0000256|ARBA:ARBA00004116}.
Interaction partners:
- Protein STRICTOSIDINE SYNTHASE-LIKE 12
- Protein STRICTOSIDINE SYNTHASE-LIKE 11
- Phenylacetaldehyde synthase
- 1-deoxy-D-xylulose-5-phosphate synthase, chloroplastic
- Tropinone reductase homolog At2g29340
- Tropinone reductase homolog At2g29260, chloroplastic
- Tropinone reductase homolog At1g07450
- Tropinone reductase homolog At2g29360
- Tropinone reductase homolog At5g06060
- Tropinone reductase homolog At2g29310
Sequence:
MASFVFVISLLLLSFSSAVFSDDASFQKLPVPDKRSGPESFAFDSTGGFYTGVSGGKILKYVPGKGYVDFAQITDSSNSAWCNGALGTAFAGKCGRPAGIALNSKTGDLYVADAPLGLHVISPAGGLATKLADSVDGKPFKFLDGLDVDPTTGVVYFTSFSSKFGPREVLIAVGLKDASGKLFKYDPATKAVTELMEGLSGAAGCAVSSDGSFVLVSEFIKSNIKKYWIKGPKAGTIEDFSSLVSNPDNIRRVGSTGNFWVASVVNKVVMPTDPRAVKLDANGKVLQTIFLKNEFGNTLLSEVNEFNGHLYIGTLTGPFAGVMKL
Protein: Probable transposase (P71639)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- ORC1/DEAH AAA+ ATPase domain-containing protein
- Uncharacterized protein Rv3786c
Sequence:
MAVGDDEEKVRAERARAIGLFRYQLIWEAADAAHSTKQRGKMVRELASREHTDPFGRRVRISRQTIDRWIRGWRAGGFDALVPNPRQCTPRTPAEVLELAVALRRENPQRTAAAIRRILRTQLGWAPDERTLQRNFHRLGLTGATTGSAPAVFGRFEAEHPNALWTGDVLHGIRIDLRKTYLFAFLDDHSRLVPGYRWGHAEDTVRLAAALRPALASRGVPNAVYVDNGSPYVDAWLLRACAKLGVRLVHSTPGRPQGRGKIERFFRTVREQFLVEITGEPDVVGRHYVADLAELNRLFTAWVETVYHRSVHSETGQTPLARWSAGGPIPLPAPETLTEAFLWEEHRRVTKTATVSLHGNRYEIDPALVGRKVELVFDPFDLTRIEVRLAGAPMRRAIPYHIGRHSHPKAKPETPTAPPKPSGIDYAQLIETAHAAELARGVNYTALTGAADQIPGQLDLLTGQEAQPK
Protein: Universal stress protein C (P46888)
Organism: Escherichia coli (strain K12)
Function: Required for resistance to DNA-damaging agents.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Universal stress protein E
- Universal stress protein UP12
- Universal stress protein F
- Sensor protein KdpD
- Outer membrane porin F
- Cell division protein FtsN
- Outer membrane porin C
- Cell division protein ZapB
- Protein AsmA
- Z-ring associated protein G
Sequence:
MSYSNILVAVAVTPESQQLLAKAVSIARPVKGHISLITLASDPEMYNQLAAPMLEDLRSVMHEETQSFLDKLIQDAGYPVDKTFIAYGELSEHILEVCHKHHFDLVICGNHNHSFFSRASCSAKRVIASSEVDVLLVPLTGD
Protein: Uncharacterized protein (Q38FB2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAHCCFLIYPLAKVADESFLQLLFDDSVKRSAFLGYPPRRFAIVELEESQNEAVLRAIGARDDDGRVEAREDNADTPFVDLFTRTGAKKGTDRNEPIGLRMGCIPHLSQVRFRRTYLRVIVSPVTIDELFGCVQKDSNHVKKEKRSLKRSRHTDEDAGPWVPRWPVANGDPTLAGRVEVVSMTGASRAGLSGDPEDERYREPYAECSGGPVCNMSPPKTFLSDDSAGDAAGRRALDVSVQNLIRELGFDK
Protein: D-galactonate dehydratase family member SSLG_02014 (EC 4.2.1.-) (D-mannonate dehydratase) (EC 4.2.1.8) (D9UNB2)
Organism: Streptomyces sp. (strain SPB78)
Function: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- Carbohydrate kinase
- Mandelate racemase/muconate lactonizing protein
- glucarate dehydratase
Sequence:
MASSAHSDSASADASAEIPAEILAPAPWSTPADDSEHLRITAVRTFLTAPQGCPYVIVRVETNQPGLYGLGCASDPQRTLAIRSVVDDYYAPMLLGRDPSDIEDLHRLLFNSGYWRGGSIGQNALAGVDVALWDIKGKVAGLPLHQLLGGRAREAADAYTHVDGDNAGEIAEKVLAAHERGYRHVRVQVSVPGTDTYGTAPRDAAEARRRELRAGSWDSLAYLRHVPPVLREIRERVGTGVELLHDAHERLTPSQARELVHEVEDARLFFLEDALAPEDAAHFDQLRAAGSVPLAVGELYHDVMMYLPLLQRQVIDFARIRIPTLGGLTPTRKLVAAVELFGARTAPHGPGDVSPVGMAANLGLDLSSPAFGVQEAATFREATREVFPGTPVPERGRFHGTGLPGLGVDFDEAAARKYPVPEPLRHDRWALLRNGDGSVQRP