wanglab/gogpt-training-data huggingface dataset:
Protein: Putative GTP diphosphokinase RSH1, chloroplastic (EC 2.7.6.5) (RelA/SpoT homolog 1) (AtRSH1) (ppGpp synthetase RSH1) (F4JHA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in a rapid plant ppGpp (guanosine 3'-diphosphate 5'-diphosphate)-mediated response to pathogens and other stresses (By similarity). Unable to functionally complement E.coli relA mutants.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18535838}.
Interaction partners:
- Nucleoside diphosphate kinase II, chloroplastic
- Nucleoside diphosphate kinase III, chloroplastic/mitochondrial
- Nucleoside diphosphate kinase 1
- Nucleoside diphosphate kinase IV, chloroplastic/mitochondrial
- Inosine triphosphate pyrophosphatase
- Alkaline-phosphatase-like family protein
- Large ribosomal subunit protein bL31c
- Large ribosomal subunit protein bL28c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- GTP-binding protein OBGC, chloroplastic
Sequence:
MTSASSMSVSVECVNICNLTKGDGNARSDCSALSCAWKAPRALTGFLASTAHPPVCSVYSCGRNGRKSRMKACAWQRYEYEVGFSEAPYFVNVRNILKSRLSCGGHKRWELYCVSAESSSGASSDVTVETLWEDLFPSISYLPRKELEFVQKGLKLAFEAHHGQKRRSGEPFIIHPVAVARILGELELDWESIVAGLLHDTVEDTNFITFEKIEEEFGATVRHIVEGETKVSKLGKLKCKTESETIQDVKADDLRQMFLAMTDEVRVIIVKLADRLHNMRTLCHMPPHKQSSIAGETLQVFAPLAKLLGMYSIKSELENLSFMYVSAEDYDRVTSRIANLYKEHEKELTEANRILVKKIEDDQFLDLVTVNTDVRSVCKETYSIYKAALKSKGSINDYNQIAQQLRIVVKPKPSVGVGPLCSPQQICYHVLGLVHEIWKPIPRTVKDYIATPKPNGYQSLHTTVIPFLYESMFRLEVQIRTEEMDLIAERGIAVYYNGKSLSTGLVGNAVPLGRNSRGKTGCLNNADFALRVGWLNAIREWQEEFVGNMSSREFVDTITRDLLGSRVFVFTPKGEIKNLPKGATVVDYAYLIHTEIGNKMVAAKVNGNLVSPTHVLENAEVVEIVTYNALSSKSAFQRHKQWLQHAKTRSARHKIMRFLREQAAQCAAEITQDQVNDFVADSDSDVEDLTEDSRKSLQWWEKILVNVKQFQSQDKSRDTTPAPQNGSVWAPKVNGKHNKAIKNSSSDEPEFLLPGDGIARILPANIPAYKEVLPGLDSWRDSKIATWHHLEGQSIEWLCVVSMDRKGIIAEVTTVLAAEGIALCSCVAEIDRGRGLAVMLFQIEANIESLVSVCAKVDLVLGVLGWSSGCSWPRSTENAQVLEC
Protein: Protein transport protein sec20 (O42852)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: SNARE required for targeting and fusion of Golgi-derived retrograde transport vesicles with the ER.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- Protein transport protein tip20
- Protein transport protein use1
- Protein transport protein sec22
- Protein transport protein bos1
- Integral membrane protein sed5
- Vesicular-fusion protein sec18
- Syntaxin ufe1
- t-SNARE affecting a late Golgi compartment protein 1
- Probable coatomer subunit gamma
- Vacuolar protein sorting-associated protein 54
Sequence:
MADVLNALEEKVVELQQSESVEVIKRHFREFRKIWETARVELEYSSIQLDSVLRYEKAVQEYIRLNRRYRNKIASGEPWLPIAQEIGKIVDEEEITSPSDGSLQKRSMDNSGSWQSDDIYLTSASQVTAAMRDIHAQMVQAVDMSAENAMELSSSTNLLETLQEKYFGVEDVLYTSKRIIKSLKLSDRSDYFLVVSGFGFFIFVVVYLLFKRIVWPILSMFLWFLR
Protein: LIM/homeobox protein Lhx6 (LIM homeobox protein 6) (LIM/homeobox protein Lhx6.1) (Q9UPM6)
Organism: Homo sapiens (Human)
Function: Probable transcription factor required for the expression of a subset of genes involved in interneurons migration and development. Functions in the specification of cortical interneuron subtypes and in the migration of GABAergic interneuron precursors from the subpallium to the cerebral cortex (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- LIM domain-binding protein 1
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
- Ras-related protein Rab-2A
- Somatostatin
- Homeobox protein Nkx-2.1
- Single-stranded DNA-binding protein 4
- Single-stranded DNA-binding protein 3
- Homeobox protein DLX-2
- Calretinin
- Parvalbumin alpha
Sequence:
MAQPGSGCKATTRCLEGTAPPAMAQSDAEALAGALDKDEGQASPCTPSTPSVCSPPSAASSVPSAGKNICSSCGLEILDRYLLKVNNLIWHVRCLECSVCRTSLRQQNSCYIKNKEIFCKMDYFSRFGTKCARCGRQIYASDWVRRARGNAYHLACFACFSCKRQLSTGEEFGLVEEKVLCRIHYDTMIENLKRAAENGNGLTLEGAVPSEQDSQPKPAKRARTSFTAEQLQVMQAQFAQDNNPDAQTLQKLADMTGLSRRVIQVWFQNCRARHKKHTPQHPVPPSGAPPSRLPSALSDDIHYTPFSSPERARMVTLHGYIESQVQCGQVHCRLPYTAPPVHLKADMDGPLSNRGEKVILFQY
Protein: Protein TBATA (Protein SPATIAL) (Stromal protein associated with thymii and lymph node) (Thymus, brain and testes-associated protein) (Q7TSD4)
Organism: Mus musculus (Mouse)
Function: Isoform 1 and isoform 2 may play a role in spermatid differentiation. Isoform 1 and isoform 2 regulate thymus function by modulating stromal cell proliferation via interference with the NEDD8 pathway.
Subcellular location: [Isoform 1]: Cytoplasm, cytosol {ECO:0000269|PubMed:17196196}. Note=Located throughout the cytosol of early round spermatids. By the end stages of round spermatid development, concentrated at the side of the cell near the nascent flagellum and in the manchette. In mature sperm, located in the principle piece of the tail. {ECO:0000269|PubMed:17196196}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:17196196}. Note=Located throughout the cytosol of early round spermatids. By the end stages of round spermatid development, concentrated at the side of the cell near the nascent flagellum and in the manchette. In mature sperm, located in the principle piece of the tail. {ECO:0000269|PubMed:17196196}.; SUBCELLULAR LOCATION: [Isoform 6]: Nucleus {ECO:0000269|PubMed:11196687}.; SUBCELLULAR LOCATION: [Isoform 7]: Nucleus {ECO:0000269|PubMed:11196687}.
Interaction partners:
- BOS complex subunit NCLN
- DENN domain-containing protein 3
Sequence:
MTTEVNQLSEHPLVSPKAEPQPETKPENLPRSHGDVGLQKETVVPGIVDFELIHEELKTTKPQTSQPTPSAYRFGRLSHHSFFSRHHPQPQRVTHIQVTGREDLEHSLPLTTSFQLLQAPGVQPMDLTPSADIAGKPVCVVRDEFSLSALTQPTFLSRCLMGMPTISVPIGDPQSNRNPQLSTSDTWRKKLKDLASRVTVFTKEIQPKPDEQKEEPPLREPPPREQGAKYSAETGRLIPASSQALTRRNRQGQRVHPSSKDGGVQASILQDQELLILELLCQILQTDSLRAIQFWLLYAPSKEKDLALGLLQTAVAQLIPQPLSSIPAEKLWNHLQELQEPQETQEAAYSPSLKKTRSPPLPKTDKPEYIGKAQVLLVHPSEDPEEKTTKAES
Protein: J domain-containing protein (Q38FZ1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDVVVLAQSVLDCPDEAVLQLLSLAPELPVVTIETSVADARRNYIRLAGILHPDKLKNRFEKATEVFQKLVRAFEKVADPKYRKTLQAQKAKEEKQKNKRKTVEGGVKKAKPKQLVEVAARGTTHTSTLQKQEAVKKIIPQRTKPIVEDDFVLRDDEGDMSSDKDEDTNGEDTADSDAGNEDFMFLASAVPPSVSTNRALIGTPRVGGIYNRTVVRCPQCRTSWEPDSKQHYTLFMGPAGKKVHCETCLCRFGCATALHACPNCQRGFDYDVTMYDTEVKCGSCKKAFGFPYYPVNQHLIDLVGLEEWRERAEREKAVERTQRAARRRAGESDAQDELHTLVGTCIVEEQCPICKKAVVSRHRQHVEACLKISPADRKASQSKPSRSGGPGKPTLKPSVSKSSISKKAPTTSGSAKKAPTKRVVKPVKKAGKKRPRRGSSDSNSEEEEEEEEPSFEETSSDDDD
Protein: Cyclin-dependent kinase 16 (EC 2.7.11.22) (CRK5) (Cell division protein kinase 16) (PCTAIRE-motif protein kinase 1) (Serine/threonine-protein kinase PCTAIRE-1) (Q04735)
Organism: Mus musculus (Mouse)
Function: Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Can phosphorylate CCNY at 'Ser-336' (in vitro) (By similarity). Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Regulates GH1 release by brain neurons. Phosphorylates NSF, and thereby regulates NSF oligomerization. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26305884}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q63686}. Cell membrane {ECO:0000269|PubMed:26305884}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q00536}; Cytoplasmic side {ECO:0000250|UniProtKB:Q00536}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q63686}. Note=Colocalizes with insulin in pancreas islets. Recruited to the cell membrane by CCNY. {ECO:0000250|UniProtKB:Q00536}.
Interaction partners:
- Cyclin-Y
- Cyclin-Y-like protein 1
Sequence:
MDRMKKIKRQLSMTLRGGRGIDKTNGVPEQIGLDESGGGGGSDLGEAPTRIAPGELRSVRGPLSSAPEIVHEDMKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNVINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFRTYNYPKYRAEALLSHAPRLDSDGADLLTKLLQFEGRNRISAEDARKHPFFLSLGERIHKLPDTTSIFALKEVQLQKEANIRSTSMPDSGRPAFRVVDTEF
Protein: Methylenetetrahydrofolate dehydrogenase [NAD(+)] (EC 1.5.1.15) (Q9P786)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Serine hydroxymethyltransferase, mitochondrial
- Probable aminomethyltransferase, mitochondrial
- Phosphoribosylglycinamide formyltransferase
- Probable thymidylate synthase
- Probable serine hydroxymethyltransferase, cytosolic
- Probable 5-formyltetrahydrofolate cyclo-ligase
- Methylenetetrahydrofolate reductase 2
- Methylenetetrahydrofolate reductase 1
- C-1-tetrahydrofolate synthase, cytoplasmic
- C-1-tetrahydrofolate synthase, mitochondrial
Sequence:
MSNTNKSEPNHSCKVVYASRVAETFVEQLKQHVNLFEFAPKLVGFLSNSDPAARMYADWTNKTCTEIGFQYELREVPKDDLEDAIVEANNDPSVNGIMIYFPVFNDGQDQYLQQVVSPDKDVEGLCHKYVMNMYHNIRHLDPEKTKKSILPCTPLAIVKILEYLGVYNKIINYGNRLYGKTITIVNRSEIVGRPLAALLANDGAKVYSVDIHNVQCFTRGAGIRSKKHDVADTNFKLEDVAPISDVIICGVPSANYKFPSNLVRDGAVCICFSSEKNFDAASLKEHAGIYVPSIGKVTIAMLLRNLIRLTSYQLNKPVDI
Protein: Glutathione S-transferase U7 (AtGSTU7) (EC 2.5.1.18) (GST class-tau member 7) (Glutathione S-transferase 25) (Q9ZW24)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase DHAR2
- Glutathione S-transferase DHAR1, mitochondrial
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Glutathione S-transferase F8, chloroplastic
- Glutathione S-transferase F7
- Glutathione synthetase, chloroplastic
- Glutathione S-transferase T1
- Glutathione reductase, chloroplastic
- Glutathione S-transferase DHAR3, chloroplastic
- Probable glutathione peroxidase 3, mitochondrial
Sequence:
MAERSNSEEVKLLGMWASPFSRRIEIALTLKGVSYEFLEQDITNKSSLLLQLNPVHKMIPVLVHNGKPISESLVILEYIDETWRDNPILPQDPYERTMARFWSKFVDEQIYVTAMKVVGKTGKERDAVVEATRDLLMFLEKELVGKDFLGGKSLGFVDIVATLVAFWLMRTEEIVGVKVVPVEKFPEIHRWVKNLLGNDVIKKCIPPEDEHLKYIRARMEKLNIKSA
Protein: UDP-N-acetylmuramoylalanine--D-glutamate ligase (EC 6.3.2.9) (D-glutamic acid-adding enzyme) (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase) (P14900)
Organism: Escherichia coli (strain K12)
Function: Cell wall formation (Probable). Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
Subcellular location: Cytoplasm.
Interaction partners:
- UDP-N-acetylmuramate--L-alanine ligase
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- Peptidoglycan D,D-transpeptidase FtsI
- Probable peptidoglycan glycosyltransferase FtsW
- Glutamate racemase
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- D-alanine--D-alanine ligase B
- UDP-N-acetylenolpyruvoylglucosamine reductase
Sequence:
MADYQGKNVVIIGLGLTGLSCVDFFLARGVTPRVMDTRMTPPGLDKLPEAVERHTGSLNDEWLMAADLIVASPGIALAHPSLSAAADAGIEIVGDIELFCREAQAPIVAITGSNGKSTVTTLVGEMAKAAGVNVGVGGNIGLPALMLLDDECELYVLELSSFQLETTSSLQAVAATILNVTEDHMDRYPFGLQQYRAAKLRIYENAKVCVVNADDALTMPIRGADERCVSFGVNMGDYHLNHQQGETWLRVKGEKVLNVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGLPHRFEVVLEHNGVRWINDSKATNVGSTEAALNGLHVDGTLHLLLGGDGKSADFSPLARYLNGDNVRLYCFGRDGAQLAALRPEVAEQTETMEQAMRLLAPRVQPGDMVLLSPACASLDQFKNFEQRGNEFARLAKELG
Protein: Protein LOL1 (Protein LSD ONE LIKE 1) (AtLOL1) (Putative zinc finger LOL1) (Q93ZB1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Positive regulator of reactive oxygen-induced cell death. May be involved in the repression of the copper/zinc superoxide dismutase CSD1 and CSD2 that detoxify accumulating superoxide before the reactive oxygen species (ROS) can trigger a cell death cascade. LSD1 and LOL1 have antagonistic effects on CSD1 and CSD2 accumulation to regulate oxidative stress-induced cell death.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 24 homolog 1
- Putative vacuolar protein sorting-associated protein 24 homolog 2
- Vacuolar protein sorting-associated protein 32 homolog 1
- Vacuolar protein sorting-associated protein 32 homolog 2
- Protein SUPPRESSOR OF K
- Vacuolar protein sorting-associated protein
- Transmembrane protein
- Vacuolar protein sorting-associated protein 60.2
- Vacuolar protein sorting-associated protein 60.1
- ESCRT-related protein CHMP1A
Sequence:
MPVPLAPYPTPPAPALAPSYNTPPANGSTSGQSQLVCSGCRNLLMYPVGATSVCCAVCNAVTAVPPPGTEMAQLVCGGCHTLLMYIRGATSVQCSCCHTVNLALEANQVAHVNCGNCMMLLMYQYGARSVKCAVCNFVTSVGGSTSTTDSKFNN
Protein: Protein phosphatase inhibitor 2 (IPP-2) (P41236)
Organism: Homo sapiens (Human)
Function: Inhibitor of protein-phosphatase 1.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 1 regulatory subunit 1A
- Serine/threonine-protein kinase LMTK2
- Protein phosphatase 1 regulatory subunit 7
- E3 ubiquitin-protein ligase PPP1R11
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Protein phosphatase 1 regulatory subunit 3A
Sequence:
MAASTASHRPIKGILKNKTSTTSSMVASAEQPRGNVDEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPSTPYHSMMGDDEDACSDTEATEAMAPDILARKLAAAEGLEPKYRIQEQESSGEEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDDEDEEMLETADGESMNTEESNQGSTPSDQQQNKLRSS
Protein: DNA-directed RNA polymerase III subunit RPC6 (RNA polymerase III subunit C6) (C34) (DNA-directed RNA polymerase III 36 kDa polypeptide) (P32910)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Involved in recruitment of Pol III to the preinitiation complex. Involved in the configuration of an initiation-competent form of RNA polymerase.
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor IIIB 70 kDa subunit
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase III subunit RPC8
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase III subunit RPC7
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerase III subunit RPC5
Sequence:
MSGMIENGLQLSDNAKTLHSQMMSKGIGALFTQQELQKQMGIGSLTDLMSIVQELLDKNLIKLVKQNDELKFQGVLESEAQKKATMSAEEALVYSYIEASGREGIWSKTIKARTNLHQHVVLKCLKSLESQRYVKSVKSVKFPTRKIYMLYSLQPSVDITGGPWFTDGELDIEFINSLLTIVWRFISENTFPNGFKNFENGPKKNVFYAPNVKNYSTTQEILEFITAAQVANVELTPSNIRSLCEVLVYDDKLEKVTHDCYRVTLESILQMNQGEGEPEAGNKALEDEEEFSIFNYFKMFPASKHDKEVVYFDEWTI
Protein: Chemotaxis protein CheA (EC 2.7.13.3) (Q1CXR4)
Organism: Myxococcus xanthus (strain DK1622)
Interaction partners:
- Fibril biogenesis regulator DifD
- Fibril biogenesis regulator DifC
- Methyl-accepting chemotaxis protein DifA
- Chemotaxis protein CheW
- Fibril biogenesis regulator DifG
- Chemotaxis protein CheW
- Chemotaxis protein CheW
- Chemotaxis protein, CheW
- Chemotaxis protein CheW
- Methyl-accepting chemotaxis protein
Sequence:
MTMDMSRYLGLFISEATDHLEALGRDLVELEREGSSSAVDSMFRHAHSVKGMASSMGFEPIAIVAHRVEDLVDAVRQDRGRLDRDLVDLLLTAADTMLAQVRAVAEGKQPDDSAALLTQLSQRVTTMTGQAPAATRVAKVTALKPEGGGSDGTGGGSDGSGTAGGSGTAGGSGTTGGAGGSGTTGGGSDGSGTTGGGPDGSGTAGGAGGSSGTTGGAGGGSGTAGGAGGSGPTGAGASPASTHGGGAAGSGTRSCVDGGSGAAGGSASPGVASGTGVDGAGPGPASPNLMNGGPGTSATSSAPNGAHGTSAPLSPDGATGGVVVPLSTRRASDVPGTDAGSAAPTPDLANSLKAAASAPLPETLAQRWAVRLRIAPTCQVPGVRAFLVHKRLTNLGTLVELRPALEELKAGRIPDGNIQLELETPAGEAGIHAALKNVAEVEVLSVKPAVAAPVVQPTLVPVPDGARASSDTASRTVRVRTELLDYFLDTVGELMLATARLREVGKVLPENTRPALEEGVYRLHTLVKDLHDKVMTARMTPLSLITDRLPRAARDIARRKEREVDLVITGAEIELDRAILEELSDPLLHLLRNCIDHGLEAPEDRAAAKKGPRGRVLVAVKRARDRVIIELEDDGRGMDPAKLKNAAVSRGLLSAEAAVRLTDREAFMLSCLPGVSTAKDITDISGRGVGMDAVKRVVENVGGTLEIDSERGRGTRFTLRLPLTVAVVHLLLVEVGEEVFGLPIAKVVGATEADGESLSRSRETALLPHGNSLLPVHSLDALVGVPAPRRLGARPFVVMDGDSGRVALAVDRLLGQEEVVLKPLSRPLDLLPGLSGVTILGSGRPVFILDVPRLLSA
Protein: Epididymis secretory sperm binding protein (A0A384NQ31)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MGSCCSCPDKDTVPDNHRNKFKVINVDDDGNELGSGIMELTDTELILYTRKRDSVKWHYLCLRRYGYDSNLFSFESGRRCQTGQGIFAFKCARAEELFNMLQEIMQNNSINVVEEPVVERNNHQTELEVPRTPRTPTTPGFAAQNLPNGYPRYPSFGDASSHPSSRHPSVGSARLPSVGEESTHPLLVAEEQVHTYVNTTGVQEERKNRTSVHVPLEARVSNAESSTPKEEPSSIEDRDPQILLEPEGVKFVLGPTPVQKQLMEKEKLEQLGRDQVSGSGANNTEWDTGYDSDERRDAPSVNKLVYENINGLSIPSASGVRRGRLTSTSTSDTQNINNSAQRRTALLNYENLPSLPPVWEARKLSRDEDDNLGPKTPSLNGYHNNLDPMHNYVNTENVTVPASAHKIEYSRRRDCTPTVFNFDIRRPSLEHRQLNYIQVDLEGGSDSDNPQTPKTPTTPLPQTPTRRTELYAVIDIERTAAMSNLQKALPRDDGTSRKTRHNSTDLPMLAWK
Protein: Solute carrier family 35 member C2 (B2RYM9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Solute carrier family 35 member C1
- Solute carrier family 35 member B4
- Adenosine 3'-phospho 5'-phosphosulfate transporter 2
- Solute carrier family 35 member D1
- Transmembrane protein 144
- Probable UDP-sugar transporter protein SLC35A4
- Solute carrier family 35, member A5
- Solute carrier family 35, member D3
- Solute carrier family 35 member A1
- Solute carrier family 35 member A2
Sequence:
MGRWALDVAFVWKAALTLGLVLLYYCFSIGITFYNKWLTKSFHFPLFMTMLHLAVIFLFSALSRALVQCSSHRARVVLSWTDYLRRVAPTALATALDVGLSNWSFLYITVSLYTMTKSSAVLFILIFSLIFKLEELRAALVLVVLLIAGGLFMFTYKSTQFNVEGFALVLGASFIGGIRWTLTQMLLQKADLGLQNPIDTMFHLQPLMFLGLFPLFAVFEGLHLSTSEKIFRFQDPGLLLWVLGSLLLGGILAFGLGFSEFLLVSRTSSLTLSIAGIFKEVCTLLLAAHLLGDQISLLNWLGFALCLSGISLHVALKALHSRGDGGPKPRKGLGSSADLELLLQSSQQEEDNGEEEYFMTQGQQ
Protein: Carboxysome assembly protein CcmN (Carbon dioxide concentrating mechanism protein CcmN) (P72757)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Required for carboxysome formation; the N-terminus interacts with CcmM which itself binds RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS). May also contact shell protein CcmK to help assemble the carboxysome (By similarity).
Subcellular location: Carboxysome {ECO:0000305|PubMed:17993516}. Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000305|PubMed:17993516}.
Interaction partners:
- Carboxysome assembly protein CcmM
- Carboxysome shell vertex protein CcmL
- Carboxysome shell protein CcmK1
- Carboxysome shell protein CcmK2
- Carboxysome shell protein CcmK3
- RuBisCO chaperone RbcX
- Ribulose bisphosphate carboxylase large chain
- Carboxysome shell protein CcmK4
- Carboxysome assembly protein CcmO
- Ribulose bisphosphate carboxylase small subunit
Sequence:
MQLPPVHSVSLSEYFVSGNVIIHETAVIAPGVILEAAPDCQITIEAGVCIGLGSVISAHAGDVKIQEQTAIAPGCLVIGPVTIGATACLGSRSTVFQQDIDAQVLIPPGSLLMNRVADVQTVGASSPTTDSVTEKKSPSTANPIAPIPSPWDNEPPAKGTDSPSDQAKESIARQSRPSTAEAAEQISSNRSPGESTPTAPTVVTTAPLVSEEVQEKPPVVGQVYINQLLLTLFPERRYFSS
Protein: Gap junction epsilon-1 protein (Connexin-23) (U3JA75)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Has significant hemichannel activity. However, has only low-efficiency gap junction activity and probably does not function as a gap junction channel in vivo.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18068130}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protocadherin 1 gamma b 2.
- Gap junction protein
- Protocadherin 1 gamma 18.
- Cell adhesion molecule 2a.
Sequence:
MSLNYIKNFYEGCLRPPTVIGQFHTLFFGSVRTFFLGVLGFAVYGNEALHFSCDPDKRELNLYCYNQFRPITPQVFWALQLVTVLVPGAVFHLYAACKNIDQEEILHRPMSTVFYIISVLLRIILEVLAFWLQSHLFGFLVDPIFMCDVTGLGKILNVSKCMVPEHFEKTIFLSAMYTFTIITILLCIAEIFEILFRRLGYLNQPMT
Protein: Cathepsin L2 (EC 3.4.22.43) (Cathepsin U) (Cathepsin V) (O60911)
Organism: Homo sapiens (Human)
Function: Cysteine protease. May have an important role in corneal physiology.
Subcellular location: Lysosome {ECO:0000305}.
Interaction partners:
- Cystatin-A
- Apoptosis regulator Bcl-2
- BH3-interacting domain death agonist
- Bcl-2-like protein 1
- Procathepsin L
- Serpin B13
- Signal peptide, CUB and EGF-like domain-containing protein 2
- Metalloproteinase inhibitor 1
Sequence:
MNLSLVLAAFCLGIASAVPKFDQNLDTKWYQWKATHRRLYGANEEGWRRAVWEKNMKMIELHNGEYSQGKHGFTMAMNAFGDMTNEEFRQMMGCFRNQKFRKGKVFREPLFLDLPKSVDWRKKGYVTPVKNQKQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRPQGNQGCNGGFMARAFQYVKENGGLDSEESYPYVAVDEICKYRPENSVANDTGFTVVAPGKEKALMKAVATVGPISVAMDAGHSSFQFYKSGIYFEPDCSSKNLDHGVLVVGYGFEGANSNNSKYWLVKNSWGPEWGSNGYVKIAKDKNNHCGIATAASYPNV
Protein: Ubiquitin thioesterase OTUB1 (EC 3.4.19.12) (Deubiquitinating enzyme OTUB1) (OTU domain-containing ubiquitin aldehyde-binding protein 1) (Otubain-1) (hOTU1) (Ubiquitin-specific-processing protease OTUB1) (Q96FW1)
Organism: Homo sapiens (Human)
Function: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:B2RYG6}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 N
- Polyubiquitin-C
- Ubiquitin-conjugating enzyme E2 D1
- E3 ubiquitin-protein ligase RNF128
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-conjugating enzyme E2 D2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin carboxyl-terminal hydrolase 8
- Ubiquitin-conjugating enzyme E2 variant 2
- TNF receptor-associated factor 6
Sequence:
MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYRPGHYDILYK
Protein: Type 3 secretion system stator protein (T3SS stator protein) (Yop proteins translocation protein L) (Q01253)
Organism: Yersinia enterocolitica
Function: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells. Acts as a regulator of the YscN/SctN ATPase activity. Overexpression of YscL/SctL abolishes type III secretion and down-regulates the expression of secretion apparatus components.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:20453832}.
Interaction partners:
Sequence:
MSQTCQTGYAYMQPFVQIIPSNLSLACGLRILRAEDYQSSLTTEELISAAKQDAEKILADAQEVYEQQKQLGWQAGMDEARTLQATLIHETQLQCQQFYRHVEQQMSEVVLLAVRKILNDYDQVDMTLQVVREALALVSNQKQVVVRVNPDQAGTIREQIAKVHKDFPEISYLEVTADARLDQGGCILETEVGIIDASIDGQIEALSRAISTTLGQMKVTEEE