wanglab/gogpt-training-data huggingface dataset:
Protein: N-acetylneuraminate epimerase (EC 5.1.3.24) (N-acetylneuraminate anomerase NanM) (N-acetylneuraminate mutarotase) (Neu5Ac mutarotase) (Sialic acid epimerase) (P39371)
Organism: Escherichia coli (strain K12)
Function: Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses. Forms linear aceneuramate during interconversion of Neu5Ac anomers.
Subcellular location: Periplasm {ECO:0000269|PubMed:18063573}.
Interaction partners:
- N-acetylneuraminic acid outer membrane channel protein NanC
- Probable 9-O-acetyl-N-acetylneuraminic acid deacetylase
- Sialic acid transporter NanT
- Putative N-acetylmannosamine-6-phosphate 2-epimerase
- N-acetylneuraminate lyase
- Sialic acid transporter NanX
- 2,7-anhydro-N-acetylneuraminate hydratase
- N-acetylneuraminate anomerase NanQ
- N-acetylmannosamine kinase
Sequence:
MNKTITALAIMMASFAANASVLPETPVPFKSGTGAIDNDTVYIGLGSAGTAWYKLDTQAKDKKWTALAAFPGGPRDQATSAFIDGNLYVFGGIGKNSEGLTQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTFVHNGKAYVTGGVNQNIFNGYFEDLNEAGKDSTAIDKINAHYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAVFELDFTGNNLKWNKLAPVSSPDGVAGGFAGISNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSTDIHLWHNGKWDKSGELSQGRAYGVSLPWNNSLLIIGGETAGGKAVTDSVLITVKDNKVTVQN
Protein: RuvB-like protein 1 (EC 3.6.4.12) (49 kDa TATA box-binding protein-interacting protein homolog) (AtTIP49a) (Ruv DNA-helicase-like protein) (Q9FMR9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. Has single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity suggesting a role in nuclear processes such as recombination and transcription (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- SWR1-complex protein 4
- RuvB-like helicase
- Protein EIN6 ENHANCER
- Actin-related protein 5
- Actin-related protein 4
- Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1
- SWR1 complex subunit 6
- Actin-related protein 9
- SWR1 complex subunit 2
- DNA-binding protein-like
Sequence:
MEKVKIEEIQSTAKKQRIATHTHIKGLGLEPTGIPIKLAAGFVGQLEAREAAGLVVDMIKQKKMAGKALLLAGPPGTGKTALALGISQELGSKVPFCPMVGSEVYSSEVKKTEVLMENFRRAIGLRIKETKEVYEGEVTELSPEETESLTGGYGKSISHVVITLKTVKGTKHLKLDPTIYDALIKEKVAVGDVIYIEANSGAVKRVGRSDAFATEFDLEAEEYVPLPKGEVHKKKEIVQDVTLQDLDAANARPQGGQDILSLMGQMMKPRKTEITDKLRQEINKVVNRYIDEGVAELVPGVLFIDEVHMLDMECFSYLNRALESSLSPIVIFATNRGVCNVRGTDMPSPHGVPIDLLDRLVIIRTQIYDPSEMIQIIAIRAQVEELTVDEECLVLLGEIGQRTSLRHAVQLLSPASIVAKMNGRDNICKADIEEVTSLYLDAKSSAKLLHEQQEKYIS
Protein: Transcriptional repressor tup11 (Q09715)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Transcriptional repressor.
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- General transcriptional corepressor ssn6
- Transcription factor atf1
- Transcriptional repressor tup12
- Iron-sensing transcriptional repressor
- Transcription factor pcr1
- Zinc finger protein rst2
- Dual specificity protein kinase lkh1
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Set1 complex component ash2
- Set1 complex component swd1
Sequence:
MASVEDATKVQEMLDALKAEYNALAHHSFASKARGNDYESSMIQSQIQEIEAFRKTVDDMYEKQKSIRETYEKDINKLKRELEELGVEANTASYRNRGERSELAASNNQVTHIDQEHPSQTKSTSQPPSNHLPAFQQIPPIHQSAYPQNNVAEVLMPPIPPSVEASSGQNFNQGIASQNPAISTSNLPSTTPLYIPPVNYGANQVSQQPNPQLPGVSNYYNPSATSKPAVNVQPPRIPTKATPSAEPSMTASANAGSISQAGPDGEYQGREQIAPVSDTEAARKTTSQSWYVTYNPACKRVFNINLVHTLEHPSVVCCVKFSNNGKYLATGCNQAANVFDVQTGKKLFTLHEESPDPSRDLYVRTIAFSPDGKYLVTGTEDRQIKLWDLSTQKVRYVFSGHEQDIYSLDFSHNGRFIVSGSGDRTARLWDVETGQCILKLEIENGVTAIAISPNDQFIAVGSLDQIIRVWSVSGTLVERLEGHKESVYSIAFSPDSSILLSGSLDKTIKVWELQATRSVGLSAIKPEGICKATYTGHTDFVLSVAVSPDSRWGLSGSKDRSMQFWDLQTGQSYLTCQGHKNSVISVCFSPDGRQFASGSGDLRARIWSIDPASP
Protein: Purine nucleoside phosphorylase (PNP) (Pu-NPase) (EC 2.4.2.1) (Inosine phosphorylase) (Inosine-guanosine phosphorylase) (P9WP01)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
Interaction partners:
- Adenine phosphoribosyltransferase
- Thymidine phosphorylase
- Uracil phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
- Cytidine deaminase
- Probable nucleoside hydrolase IunH
- Probable phosphomannomutase PmmB
- Adenosine deaminase
- Adenosine kinase
- NAD-dependent protein deacylase
Sequence:
MADPRPDPDELARRAAQVIADRTGIGEHDVAVVLGSGWLPAVAALGSPTTVLPQAELPGFVPPTAAGHAGELLSVPIGAHRVLVLAGRIHAYEGHDLRYVVHPVRAARAAGAQIMVLTNAAGGLRADLQVGQPVLISDHLNLTARSPLVGGEFVDLTDAYSPRLRELARQSDPQLAEGVYAGLPGPHYETPAEIRMLQTLGADLVGMSTVHETIAARAAGAEVLGVSLVTNLAAGITGEPLSHAEVLAAGAASATRMGALLADVIARF
Protein: Bax inhibitor 1 (BI-1) (Testis-enhanced gene transcript protein) (Transmembrane BAX inhibitor motif-containing protein 6) (Q9D2C7)
Organism: Mus musculus (Mouse)
Function: Suppressor of apoptosis (By similarity). Modulates unfolded protein response signaling (By similarity). Modulates ER calcium homeostasis by acting as a calcium-leak channel (By similarity). Negatively regulates autophagy and autophagosome formation, especially during periods of nutrient deprivation, and reduces cell survival during starvation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P55061}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P55061}.
Interaction partners:
- Desumoylating isopeptidase 1
- Bcl-2-like protein 1
- Serine/threonine-protein kinase/endoribonuclease IRE1
- Apoptosis regulator Bcl-2
- Protein lifeguard 1
- Growth hormone-inducible transmembrane protein
Sequence:
MNIFDRKINFDALLKFSHITPSTQQHLKKVYASFALCMFVAAAGAYVHVVTHFIQAGLLSALGSLALMIWLMATPHSHETEQKRLGLLAGFAFLTGVGLGPALELCIAVNPSILPTAFMGTAMIFTCFSLSALYARRRSYLFLGGILMSAMSLMLLSSLGNLFFGSIWLFQANLYLGLLVMCGFVLFDTQLIIEKAEHGDKDYIWHCVDLFLDFVTLFRKLMLILAFNEKDKKKEKK
Protein: F-box/WD repeat-containing protein 4 (F-box and WD-40 domain-containing protein 4) (Protein hagoromo) (Q9JMJ2)
Organism: Mus musculus (Mouse)
Function: Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. Likely to be involved in key signaling pathways crucial for normal limb development. May participate in Wnt signaling.
Interaction partners:
- Cullin-1
- S-phase kinase-associated protein 1
- DNA polymerase lambda
Sequence:
MAEDAAEDAAAAAVEPATRPAAGPALWRLPEELLLLICSYLDTRALGRLAQVCRWLRRFTSCDLLWRPIARASLNTGFTRLGTDLMAGIPVKERVKLSQNWRLGRCRDRILLKWRYSQMPWMQLQDASLYLSQANFILAYQFRPDGASLNRRPFRVFSGHDEDVCHFVLANSHIVSAGGDGKIGVHKIHSTFTVKYSAHEQEVNCVDCKGGIIVSGSRDRTAKVWPLASGRLGQCLHTIQTEDRVWSIAISPLLSSFVTGTACCGHFSPLRIWDLNSGQLITHLGSDFPPGAGVLDVMYESPSTLLSCGYDTYVRYWDLRTSTRKCVMEWEEPHDSTFYCLQTDGNHLLATGSSYYGLVRLWDRRQRACLHAFSLTSTPLSSPVYCLRFTTRHLYAALSYNLHVLDFQNP
Protein: Transcription factor (A0A8I6A8L4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR009404, ECO:0000256|RuleBase:RU003796}.
Interaction partners:
Sequence:
MIISTPQRITNSGSVLIGSPYTPAPAMVTQTHIAEAAGWVPSDRKRAREFIDSDFSESKRSKKGDKNGKGLRHFSMKVCEKVQRKGTTSYNEVADELVSEFTNASNHLAADSQAYDQKNIRRRVYDALNVLMAMNIISKEKKEIKWIGLPTNSAQECQNLEIEKQRRIERIKQKRAQLQELLLQQIAFKNLVQRNRQNEQQNQGPPAVNSTIQLPFIVINTSRKTVIDCSISSDKFEYLFNFDNTFEIHDDIEVLKRMGMSFGLESGKCSLEDLKIAKSLVPKALEGYITDVSTGPSWLNQGLLLNSTQSVSNLDPTTGATVPQSSVNQGLCLDAEVALATGQFLAPNSHQSSTAASQFSESRGETPCSFNDEEEEDEEEDPSSPE
Protein: Transmembrane protein (Q9XXU0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGNSASAKQVADQVAYGVISCITVGVLIVMLYMSVFGQRVRATAVRWHVLNCSLWGILHLISYASFAEKAPWPNYITNQNWRDTARQVECFTRSVFPAGMVFVYLEQIILTIAPKLANSIVFNAIFFILLIPFLNGLMIFLYYAHFMDIVWWYEPIDLFNLATYLIFTTFTFIYFLFCLFGTCLCCATMTSKKPSSRTTGTFADMWLLFPYGLIPSIMYGPSFGMTSVSFAMQHLLTWVLESGLLTGGGGSSSGGSFIDMNLLMQVATNAILAMPWFVLLFPLVQSILALVCLRMFREQFFFMISCGRIFEGKRAKIGMTEWNVTSIGPPPLYPNSPSEKQEA
Protein: Citrate lyase alpha chain (Citrase alpha chain) (EC 4.1.3.6) (Citrate (pro-3S)-lyase alpha chain) (Citrate CoA-transferase subunit) (EC 2.8.3.10) (P75726)
Organism: Escherichia coli (strain K12)
Function: Represents a citrate:acetyl-ACP transferase.
Subcellular location: Cytoplasm.
Interaction partners:
- Citrate lyase acyl carrier protein
- Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase
- Citrate lyase subunit beta
- [Citrate [pro-3S]-lyase] ligase
- 2-
- Citrate/succinate antiporter
Sequence:
MTQKIEQSQRQERVAAWNRRAECDLAAFQNSPKQTYQAEKARDRKLCANLEEAIRRSGLQDGMTVSFHHAFRGGDLTVNMVMDVIAKMGFKNLTLASSSLSDCHAPLVEHIRQGVVTRIYTSGLRGPLAEEISRGLLAEPVQIHSHGGRVHLVQSGELNIDVAFLGVPSCDEFGNANGYTGKACCGSLGYAIVDADNAKQVVMLTEELLPYPHNPASIEQDQVDLIVKVDRVGDAAKIGAGATRMTTNPRELLIARSAADVIVNSGYFKEGFSMQTGTGGASLAVTRFLEDKMRSRDIRADFALGGITATMVDLHEKGLIRKLLDVQSFDSHAAQSLARNPNHIEISANQYANWGSKGASVDRLDVVVLSALEIDTQFNVNVLTGSDGVLRGASGGHCDTAIASALSIIVAPLVRGRIPTLVDNVLTCITPGSSVDILVTDHGIAVNPARPELAERLQEAGIKVVSIEWLRERARLLTGEPQPIEFTDRVVAVVRYRDGSVIDVVHQVKE
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (A0A384MTS1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAESGSDFQQRRRRRRDPEEPEKTELSERELAVAVAVSQENDEENEERWVGPLPVEATLAKKRKVLEFERVYLDNLPSASMYERSYMHRDVITHVVCTKTDFIITASHDGHVKFWKKIEEGIEFVKHFRSHLGVIESIAVSSEGALFCSVGDDKAMKVFDVVNFDMINMLKLGYFPGQCEWIYCPGDAISSVAASEKSTGKIFIYDGRGDNQPLHIFDKLHTSPLTQIRLNPVYKAVVSSDKSGMIEYWTGPPHEYKFPKNVNWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVFDESLSMFTELQQMRQQLPDMEFGRRMAVERELEKVDAVRLINIVFDETGHFVLYGTMLGIKVINVETNRCVRILGKQENIRVMQLALFQGIAKKHRAATTIEMKASENPVLQNIQADPTIVCTSFKKNRFYMFTKREPEDTKSADSDRDVFNEKPSKEEVMAATQAEGPKRVSDSAIIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPKTDKPYEDVSIINITVK
Protein: Mediator of RNA polymerase II transcription subunit 21 (D4AA11)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU366036}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 28
- Mediator complex subunit 12
Sequence:
MADRLTQLQDAVNSLADQFCNAIGVLQQCGPPASFSNIQTAINKDQPANPTEEYAQLFAALIARTAKDIDVLIDSLPSEESTAALQAASLYKLEEENHEAATCLEDVVYRGDMLLEKIQSALADIAQSQLKTRSVTHSQSLPDS
Protein: Probable alcohol dehydrogenase (EC 1.1.1.1) (P37686)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Aldehyde dehydrogenase B
- Acetaldehyde dehydrogenase
- Aldehyde reductase Ahr
- Alcohol dehydrogenase, propanol-preferring
- Aldehyde reductase YahK
- S-
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Probable alcohol dehydrogenase EutG
- N-succinylglutamate 5-semialdehyde dehydrogenase
- Acetaldehyde dehydrogenase
Sequence:
MAASTFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKDACGFTNPIQATHEEIVAIYRAAM
Protein: LIM domain-binding protein 1 (LDB-1) (Carboxyl-terminal LIM domain-binding protein 2) (CLIM-2) (LIM domain-binding factor CLIM2) (hLdb1) (Nuclear LIM interactor) (Q86U70)
Organism: Homo sapiens (Human)
Function: Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. Plays a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1. Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P70662}. Note=Colocalizes with SLK at leading edges. {ECO:0000250|UniProtKB:P70662}.
Interaction partners:
- LIM/homeobox protein Lhx3
- Rhombotin-2
- T-cell acute lymphocytic leukemia protein 1
- Insulin gene enhancer protein ISL-1
- Erythroid transcription factor
- Transcription factor E2-alpha
- Single-stranded DNA-binding protein 2
- Rhombotin-1
- Endothelial transcription factor GATA-2
- Protein CBFA2T3
Sequence:
MSVGCACPGCSSKSFKLYSPKEPPNGNAFPPFHPGTMLDRDVGPTPMYPPTYLEPGIGRHTPYGNQTDYRIFELNKRLQNWTEECDNLWWDAFTTEFFEDDAMLTITFCLEDGPKRYTIGRTLIPRYFRSIFEGGATELYYVLKHPKEAFHSNFVSLDCDQGSMVTQHGKPMFTQVCVEGRLYLEFMFDDMMRIKTWHFSIRQHRELIPRSILAMHAQDPQMLDQLSKNITRCGLSNSTLNYLRLCVILEPMQELMSRHKTYSLSPRDCLKTCLFQKWQRMVAPPAEPTRQQPSKRRKRKMSGGSTMSSGGGNTNNSNSKKKSPASTFALSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQFDAANGIDDEDSFNNSPALGANSPWNSKPPSSQESKSENPTSQASQ
Protein: Homeobox protein knotted-1-like 5 (Homeodomain-containing protein 1) (Protein KNAT5) (P48002)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein KNATM
- Homeobox protein BEL1 homolog
- BEL1-like homeodomain protein 2
- At4g32030
- At4g32050
- Armadillo repeat-containing protein LFR
- Homeobox-leucine zipper protein ATHB-23
Sequence:
MSFNSSHLLPPQEDLPLRHFTDQSQQPPPQRHFSETPSLVTASFLNLPTTLTTADSDLAPPHRNGDNSVADTNPRWLSFHSEMQNTGEVRSEVIDGVNADGETILGVVGGEDWRSASYKAAILRHPMYEQLLAAHVACLRVATPVDQIPRIDAQLSQLHTVAAKYSTLGVVVDNKELDHFMSHYVVLLCSFKEQLQHHVCVHAMEAITACWEIEQSLQSLTGVSPSESNGKTMSDDEDDNQVESEVNMFDGSLDGSDCLMGFGPLVPTERERSLMERVKKELKHELKQGFKEKIVDIREEIMRKRRAGKLPGDTTSVLKEWWRTHSKWPYPTEEDKAKLVQETGLQLKQINNWFINQRKRNWNSNSSTSSTLTKNKRKRTGKS
Protein: Fatty acid elongase 1 (EC 2.3.1.-) (Beta-ketoacyl-CoA synthase) (Elongation of fatty acids protein) (Q57UP8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q4DUK7}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Fatty acid desaturase, putative
- Putative enoyl-CoA reductase
- very-long-chain
- Fatty acid desaturase, putative
- Short-chain dehydrogenase, putative
- beta-ketoacyl-[acyl-carrier-protein] synthase I
Sequence:
MFFTPPQLQKLEQDWNGLAVRDWMIANVDVVLYISFLYLGFVFIGPKLFAKLVGTNPAAAAAGARSADGTGSPIVRRSMVVWNLALSIFSIFGTSTVTPVLLRNLANKGFYGATCDFKETEFYTTNVGFWMGIFALSKIPELVDTIFLVLQGKQELPFLHWYHHVTVLLFSWHTYCVGSSAYIWVAAMNYSVHSVMYLYFALAALGYKRVVRPLAPYITIIQILQMVVGCYVTIFALQELHGEGGRGCGVSPANMRIQLVMYASYLYLFSKMFVASYIRPPKRPTVGGPSSTAGVSNGSVEKKVK
Protein: Beta-defensin 114 (Beta-defensin 14) (DEFB-14) (Defensin, beta 114) (Q30KQ6)
Organism: Homo sapiens (Human)
Function: Has a salt-sensitive antimicrobial activity against Gram-negative bacteria, including E.coli, Gram-positive, including S.aureus, and fungi, including C.albicans. Binds to and neutralizes bacterial lipopolysaccharides (LPS), abolishing TNF production by macrophages challenged with LPS. Rescues the LPS-induced reduction of sperm motility in vitro and may protect from LPS-induced lethality.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Beta-defensin 127
- Defensin beta 118
- Beta-defensin 125
- Beta-defensin 126
- Beta-defensin 134
- Beta-defensin 135
- Beta-defensin 128
- Beta-defensin 124
- Beta-defensin 110
- Beta-defensin 103
Sequence:
MRIFYYLHFLCYVTFILPATCTLVNADRCTKRYGRCKRDCLESEKQIDICSLPRKICCTEKLYEEDDMF
Protein: Sperm protein associated with the nucleus on the X chromosome B1 (Cancer/testis antigen 11.2) (CT11.2) (Nuclear-associated protein SPAN-Xb) (SPANX-B) (SPANX family member B1) (SPANX family member F1) (Q9NS25)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10906052}. Nucleus {ECO:0000269|PubMed:10906052}. Note=Associated with nuclear craters.
Interaction partners:
- Sperm protein associated with the nucleus on the X chromosome C
Sequence:
MGQQSSVRRLKRSVPCESNEANEANEANKTMPETPTGDSDPQPAPKKMKTSESSTILVVRYRRNVKRTSPEELLNDHARENRINPDQMEEEEFIEITTERPKK
Protein: Presequence protease, mitochondrial (PreP) (EC 3.4.24.-) (Metalloprotease of 112 kDa) (Pitrilysin metalloproteinase) (Protease M) (P32898)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Degrades mitochondrial transit peptides after their cleavage in the intermembrane space or in the matrix, and presequence peptides; clearance of these peptides is required to keep the presequence processing machinery running. Preferentially cleaves the N-terminal side of paired basic amino acid residues. Also degrades other unstructured peptides. May function as an ATP-dependent peptidase as opposed to a metalloendopeptidase.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15606766, ECO:0000269|PubMed:15772085}. Mitochondrion matrix {ECO:0000269|PubMed:21621546}.
Interaction partners:
- Mitochondrial intermediate peptidase
- A-factor-processing enzyme
- Mitochondrial-processing peptidase subunit beta
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
- Pyruvate dehydrogenase complex protein X component, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- mRNA-binding protein PUF3
- Mitochondrial-processing peptidase subunit alpha
Sequence:
MLRFQRFASSYAQAQAVRKYPVGGIFHGYEVRRILPVPELRLTAVDLVHSQTGAEHLHIDRDDKNNVFSIAFKTNPPDSTGVPHILEHTTLCGSVKYPVRDPFFKMLNKSLANFMNAMTGPDYTFFPFSTTNPQDFANLRGVYLDSTLNPLLKQEDFDQEGWRLEHKNITDPESNIVFKGVVYNEMKGQISNANYYFWSKFQQSIYPSLNNSGGDPMKITDLRYGDLLDFHHKNYHPSNAKTFTYGNLPLVDTLKQLNEQFSGYGKRARKDKLLMPIDLKKDIDVKLLGQIDTMLPPEKQTKASMTWICGAPQDTYDTFLLKVLGNLLMDGHSSVMYQKLIESGIGLEFSVNSGVEPTTAVNLLTVGIQGVSDIEIFKDTVNNIFQNLLETEHPFDRKRIDAIIEQLELSKKDQKADFGLQLLYSILPGWTNKIDPFESLLFEDVLQRFRGDLETKGDTLFQDLIRKYIVHKPCFTFSIQGSEEFSKSLDDEEQTRLREKITALDEQDKKNIFKRGILLQEKQNEKEDLSCLPTLQIKDIPRAGDKYSIEQKNNTMSRITDTNGITYVRGKRLLNDIIPFELFPYLPLFAESLTNLGTTTESFSEIEDQIKLHTGGISTHVEVTSDPNTTEPRLIFGFDGWSLNSKTDHIFEFWSKILLETDFHKNSDKLKVLIRLLASSNTSSVADAGHAFARGYSAAHYRSSGAINETLNGIEQLQFINRLHSLLDNEETFQREVVDKLTELQKYIVDTNNMNFFITSDSDVQAKTVESQISKFMERLPHGSCLPNGPKTSDYPLIGSKCKHTLIKFPFQVHYTSQALLGVPYTHKDGSALQVMSNMLTFKHLHREVREKGGAYGGGASYSALAGIFSFYSYRDPQPLKSLETFKNSGRYILNDAKWGVTDLDEAKLTIFQQVDAPKSPKGEGVTYFMSGVTDDMKQARREQLLDVSLLDVHRVAEKYLLNKEGVSTVIGPGIEGKTVSPNWEVKEL
Protein: thioredoxin-disulfide reductase (EC 1.8.1.9) (H0YBI6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MERSPPQSPGPGKAGDAPNRRSGHVRGARVLSPPGRRARLSSPGPSRSSEAREELRRHLVGLIERSRVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQKLLQEDLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGIQGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEKGSPGKLKVLAKSTEGTETIEGVYNTVLLAIGRDSCTRKIGLEKIGVKINEKSGKIPVNDVEQTNVPYVYAVGDILEDKPELTPVAIQSGKLLAQRLFGASLEKIYHTLFWPLEWTVAGRENNTCYAKIICNKFDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSGLDITQKGCCG
Protein: Acid-sensing ion channel 1 (ASIC1) (Acid-sensing ionic channel) (ASIC) (Amiloride-sensitive cation channel 2, neuronal) (Brain sodium channel 2) (P55926)
Organism: Rattus norvegicus (Rat)
Function: Proton-gated sodium channel; it is activated by a drop of the extracellular pH and then becomes rapidly desensitized. Generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Can also transport potassium ions, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 discrimates stronger than isoform 1 between monovalent cations. Isoform 3 can flux Ca(2+) while isoform 1 cannot. Heteromeric channels composed of isoform 2 and isoform 3 are active but have a lower pH-sensitivity. Mediates glutamate-independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11842212, ECO:0000269|PubMed:9062189, ECO:0000269|PubMed:9707631}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P78348}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q6NXK8}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6NXK8}. Note=Isolated in synaptosomes from the dendritic synapses of neurons. {ECO:0000250|UniProtKB:Q6NXK8}.
Interaction partners:
- Acid-sensing ion channel 2
- PRKCA-binding protein
- Acid-sensing ion channel 3
- Acid-sensing ion channel 4
Sequence:
MELKTEEEEVGGVQPVSIQAFASSSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFCYHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMADEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEACSAEDFKVVFTRYGKCYTFNSGQDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPFIDQLGFGVAPGFQTFVSCQEQRLIYLPSPWGTCNAVTMDSDFFDSYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLTRYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHRLCRRGKCQKEAKRSSADKGVALSLDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC
Protein: Translationally-controlled tumor protein homolog (TCTP) (Q5BFN9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in protein synthesis. Involved in microtubule stabilization (By similarity). Involved in osmoadaptation.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Elongation factor 1-beta
- 60S ribosomal protein L9, putative
- 60S acidic ribosomal protein P0
- GBLP_NEUCR Guanine nucleotide-binding protein beta subunit-like proteinGbeta like protein
- 40S ribosomal protein S8
- 60S ribosomal protein L30, putative
- 40S ribosomal protein S16
- Large ribosomal subunit protein P1
- 60S acidic ribosomal protein P2/allergen Asp F 8
- 40S ribosomal protein S10a
Sequence:
MIIYKDIISGDEVLSDTYNIKTVDGVLYECDCRKYLKKTNEDFELEGANPSAEGGDDEGGAEGGEVMVHDIEDQFRLVWLKAEDGAKPPKDAFKGHLKTYMKKVLKALQDKGAPDETINEFKKGAPAAVNKILKNYDNYDVLMGESMDGDAMHILIDFREDGVTPYATLWKHGLEEMKV
Protein: Translation initiation factor IF-3 (Q8IB86)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MLLKGFFFFIICVFYILIFYNNNVNCFYIPKICCTKYFYLKETSDAPAYSDGHERYIQEKKLKQLKHKMENKSVKQLRITPRIGMNDLLIKINSAKQFLLKRHRVKFILTLKGREYTNVENVKRIFSKISEELKSYGNSETMRQNGNIVSQLFNLKAKRKNEGGT
Protein: Ankyrin repeat-containing protein YIL001W (P40560)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Cullin-3
Sequence:
MADKLMDKNFEELCYSCRTGDMDNVDRLISTGVNVNSVDKFDNSPLFLASLCGHEAVVKLLLQRGAVCDRDRYEGARCIYGALTDTIRDTLLSYDISKAVDVKQPFATHISSMYNDEGFLKRDITFRVSNGKLFTAHKFLLCARSEILAEKMVNEWAKHEIVSLEVRPDIFDIFLKFLYLIPILHQIEPGQYEELIELSSKFDIELLPEFLDKARHTADPTEKSRLMSDYQYKFTEVARSQLLIFVNNCIFRSTVDLANSERRVFSLMNCPAYPDVQLMVKNRNGAIRIYPCHLAVLSRAEYFKVMFTNNFKEKVTYIKAKHVTGKYNSIIPQLTLPNCEFEVAEIILRYLYADNTDIPWMYAVDVLLLADILLEDRLKTIASTIITQSKEFIQQYNVFDVLYLSWEIGVERLEQFAAKFIAIHLQELYKDPEIKRAIMLSSQRISLRQETDTIELVDDIRYYLLRKYSFEPDDVELFENQDDLEYLKQVGYLEYRKDMGMLDNILADLELDV