wanglab/gogpt-training-data huggingface dataset:
Protein: All trans-polyprenyl-diphosphate synthase PDSS1 (All-trans-decaprenyl-diphosphate synthase subunit 1) (EC 2.5.1.91) (Decaprenyl-diphosphate synthase subunit 1) (Solanesyl-diphosphate synthase subunit 1) (Trans-prenyltransferase 1) (TPT 1) (Q33DR2)
Organism: Mus musculus (Mouse)
Function: Heterotetrameric enzyme that catalyzes the condensation of farnesyl diphosphate (FPP), which acts as a primer, and isopentenyl diphosphate (IPP) to produce prenyl diphosphates of varying chain lengths and participates in the determination of the side chain of ubiquinone. Supplies nona and decaprenyl diphosphate, the precursors for the side chain of the isoprenoid quinones ubiquinone-9 (Q9)and ubiquinone-10 (Q10) respectively. The enzyme adds isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q5T2R2}.
Interaction partners:
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS2
- Geranylgeranyl pyrophosphate synthase
- Protein farnesyltransferase subunit beta
- Dehydrodolichyl diphosphate synthase complex subunit Dhdds
- Farnesyl pyrophosphate synthase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Dehydrodolichyl diphosphate synthase complex subunit Nus1
- Squalene synthase
- Ubiquinone biosynthesis protein COQ9
Sequence:
MAMRWSCWRRGCSWRPTAVGSPRRERPGCVEPLGTRAASDTRAQIPYFSLMKILMSASPTMHSISQFHQRTPAMCSCRQTQSGEKYSDPFKLGWRDLKGLYEDIRKELHISTRELKDMSEYYFDGKGKAFRPIIVVLMARACNIHHNNAREMQASQRSIALVAEMIHTATLVHDDVIDDASSRRGKHTVNKIWGEKKAVLAGDLILSAASVALARIGNTAVVSMLAQVIEDLVRGEFLQLGSKENENERFAHYLEKTFKKTASLIANSCKAVSVLGCPDPVVHEIAYQYGKNVGIAFQLIDDVLDFTSCSDQMGKPTSADLKLGIATGPVLFACQQFPEMNAMIMRRFSLPGDVDRARQYVLQSDGVQQTTYLAQQYCHKAVREIRKLRPSTERDALIQLSESVLTRDK
Protein: Arginine/serine-rich protein PNISR (PNN-interacting serine/arginine-rich protein) (SR-related protein) (SR-rich protein) (Serine/arginine-rich-splicing regulatory protein 130) (SRrp130) (Splicing factor, arginine/serine-rich 130) (Splicing factor, arginine/serine-rich 18) (Q8TF01)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:14578391}.
Interaction partners:
- Luc7-like protein 3
- Pinin
- Serine/arginine-rich splicing factor 11
- Protein SCAF11
- NK-tumor recognition protein
- Splicing factor U2AF 65 kDa subunit
- Pre-mRNA-processing factor 39
- RNA-binding protein 39
- Serine/arginine-rich splicing factor 2
- Arginine and glutamate-rich protein 1
Sequence:
MWDQGGQPWQQWPLNQQQWMQSFQHQQDPSQIDWAALAQAWIAQREASGQQSMVEQPPGMMPNGQDMSTMESGPNNHGNFQGDSNFNRMWQPEWGMHQQPPHPPPDQPWMPPTPGPMDIVPPSEDSNSQDSGEFAPDNRHIFNQNNHNFGGPPDNFAVGPVNQFDYQHGAAFGPPQGGFHPPYWQPGPPGPPAPPQNRRERPSSFRDRQRSPIALPVKQEPPQIDAVKRRTLPAWIREGLEKMEREKQKKLEKERMEQQRSQLSKKEKKATEDAEGGDGPRLPQRSKFDSDEEEEDTENVEAASSGKVTRSPSPVPQEEHSDPEMTEEEKEYQMMLLTKMLLTEILLDVTDEEIYYVAKDAHRKATKAPAKQLAQSSALASLTGLGGLGGYGSGDSEDERSDRGSESSDTDDEELRHRIRQKQEAFWRKEKEQQLLHDKQMEEEKQQTERVTKEMNEFIHKEQNSLSLLEAREADGDVVNEKKRTPNETTSVLEPKKEHKEKEKQGRSRSGSSSSGSSSSNSRTSSTSSTVSSSSYSSSSGSSRTSSRSSSPKRKKRHSRSRSPTIKARRSRSRSYSRRIKIESNRARVKIRDRRRSNRNSIERERRRNRSPSRERRRSRSRSRDRRTNRASRSRSRDRRKIDDQRGNLSGNSHKHKGEAKEQERKKERSRSIDKDRKKKDKEREREQDKRKEKQKREEKDFKFSSQDDRLKRKRESERTFSRSGSISVKIIRHDSRQDSKKSTTKDSKKHSGSDSSGRSSSESPGSSKEKKAKKPKHSRSRSVEKSQRSGKKASRKHKSKSRSR
Protein: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (Q9P1Z3)
Organism: Homo sapiens (Human)
Function: Hyperpolarization-activated potassium channel. May also facilitate the permeation of sodium ions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16043489}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
- BTB/POZ domain-containing protein KCTD3
- PEX5-related protein
Sequence:
MEAEQRPAAGASEGATPGLEAVPPVAPPPATAASGPIPKSGPEPKRRHLGTLLQPTVNKFSLRVFGSHKAVEIEQERVKSAGAWIIHPYSDFRFYWDLIMLLLMVGNLIVLPVGITFFKEENSPPWIVFNVLSDTFFLLDLVLNFRTGIVVEEGAEILLAPRAIRTRYLRTWFLVDLISSIPVDYIFLVVELEPRLDAEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPMLQDFPPDCWVSINHMVNHSWGRQYSHALFKAMSHMLCIGYGQQAPVGMPDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADTRQRIHEYYEHRYQGKMFDEESILGELSEPLREEIINFTCRGLVAHMPLFAHADPSFVTAVLTKLRFEVFQPGDLVVREGSVGRKMYFIQHGLLSVLARGARDTRLTDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDHFNAVLEEFPMMRRAFETVAMDRLLRIGKKNSILQRKRSEPSPGSSGGIMEQHLVQHDRDMARGVRGRAPSTGAQLSGKPVLWEPLVHAPLQAAAVTSNVAIALTHQRGPLPLSPDSPATLLARSAWRSAGSPASPLVPVRAGPWASTSRLPAPPARTLHASLSRAGRSQVSLLGPPPGGGGRRLGPRGRPLSASQPSLPQRATGDGSPGRKGSGSERLPPSGLLAKPPRTAQPPRPPVPEPATPRGLQLSANM
Protein: Oxidoreductase, short-chain dehydrogenase/reductase family (Q7D6M3)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTSLDLTGRTAIITGASRGIGLAIAQQLAAAGAHVVLTARRQEAADEAAAQVGDRALGVGAHAVDEDAARRCVDLTLERFGSVDILINNAGTNPAYGPLLEQDHARFAKIFDVNLWAPLMWTSLVVTAWMGEHGGAVVNTASIGGMHQSPAMGMYNATKAALIHVTKQLALELSPRIRVNAICPGVVRTRLAEALWKDHEDPLAATIALGRIGEPADIASAVAFLVSDAASWITGETMIIDGGLLLGNALGFRAAPSTEH
Protein: RIKEN cDNA 2310061I04 gene (F6X1P1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XAQALNSLSMVLPPRKREKGPGPELHSGCLDGLRSLFEGPPCPYPGAVIPFQAPGPSHSSPTTPSGDESMEEHLAVMHERLRQELPTLFLRSHDYTIYSMDVEFINEILNIRTKGRTFYVMSLTLCRFLVWNYFAQFRLEILQLTRHPENWTLQARWRLIGLPIHMLFLRFYRRDKEDLYRTFDAFSTFYLNSSGLICRHHLDKPPLTCLCS
Protein: GDP-mannose 4,6-dehydratase (EC 4.2.1.47) (GDP-D-mannose dehydratase) (F1QPT3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAQCTATTTGGGMNGDSKRKRKVAIITGITGQDGSYLAELLLAKGYEVHGILRRSSSFNTGRIEHLYHNPQTHTEGSIGATKDHMKLHYGDLTDSTCLVKIINEVKPTEIYNLGAQSHVKISFDLAEYTADVDGVGTLRLLDAVKTCGLTDTVRFYQASTSELYGKVQEIPQKETTPFYPRSPYGAAKLYAYWIVINFREAYNLFAVNGILFNHESPRRGSNFVTRKISRSVAKIHLGQLECFSLGNLDSMRDWGHAKDYVEAMWLMLQQEEPVDFVIATGEVHSVREFVERAFKHVGKTIVWEGKDEKEVGRCQETGVIHVRVDPKYYRPTEVDYLQGDSSKAFKVLGWKPRVTFEELVKEMVDADIKLMQNNPNA
Protein: Brefeldin A-inhibited guanine nucleotide-exchange protein 3 (BIG3) (ARF guanine-nucleotide exchange factor BIG3) (Protein EMBRYO SAC DEVELOPMENT ARREST 10) (Q9LPC5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activates the ARF proteins by exchanging bound GDP for free GTP. Plays a role in vesicular protein sorting (By similarity). Involved both in the nuclear division phase and in the nuclear fusion phase.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Soluble and partially membrane-bound. {ECO:0000250}.
Interaction partners:
- ADP-ribosylation factor 1
- ADP-ribosylation factor
- Coatomer subunit gamma
- ADP-ribosylation factor 2-B
- ADP-ribosylation factor GTPase-activating protein AGD3
- V-type proton ATPase subunit a1
- Phospholipid-transporting ATPase 3
- Auxin efflux carrier component 2
- Sorting nexin 1
- Ras-related protein RABG3f
Sequence:
MASTEVDSRLGRVVIPALDKVIKNASWRKHSKLAHECKSVIERLRSPENSSPVADSESGSSIPGPLHDGGAAEYSLAESEIILSPLINASSTGVLKIVDPAVDCIQKLIAHGYVRGEADPTGGPEALLLSKLIETICKCHELDDEGLELLVLKTLLTAVTSISLRIHGDSLLQIVRTCYGIYLGSRNVVNQATAKASLVQMSVIVFRRMEADSSTVPIQPIVVAELMEPMDKSESDPSTTQSVQGFITKIMQDIDGVFNSANAKGTFGGHDGAFETSLPGTANPTDLLDSTDKDMLDAKYWEISMYKSALEGRKGELADGEVEKDDDSEVQIGNKLRRDAFLVFRALCKLSMKTPPKEDPELMRGKIVALELLKILLENAGAVFRTSDRFLGAIKQYLCLSLLKNSASNLMIIFQLSCSILLSLVSRFRAGLKAEIGVFFPMIVLRVLENVAQPDFQQKMIVLRFLDKLCVDSQILVDIFINYDCDVNSSNIFERMVNGLLKTAQGVPPGTVTTLLPPQEAAMKLEAMKCLVAVLRSMGDWVNKQLRLPDPYSAKMLEIVDRNLEEGSHPVENGKGDGGHGGFERSDSQSELSSGNSDALAIEQRRAYKLELQEGISIFNQKPKKGIEFLIKANKVGDSPEEIAAFLKDASGLNKTLIGDYLGEREDLSLKVMHAYVDSFEFQGMEFDEAIRAFLRGFRLPGEAQKIDRIMEKFAERFCKCNPKDFSSADTAYVLAYSVILLNTDAHNPMVKSKMTADGFIRNNRGIDDGKDLPEEYLRALYERISRNEIKMKDDGLGPQQKQPTNSSRLLGLDTILNIVVPRRGDDMNMETSDDLIRHMQERFKEKARKSESVYYAASDVIILRFMVEVCWAPMLAAFSVPLDQSDDAVITTLCLEGFHHAIHVTSVMSLKTHRDAFVTSLAKFTSLHSPADIKQKNIEAIKAIVKLAEEEGNYLQDAWEHILTCVSRFEHLHLLGEGAPPDATFFAFPQTESGNSPLAKPNSVPAIKERAPGKLQYAASAMIRGSYDGSGVAGKASNTVTSEQMNNLISNLNLLEQVGDMSRIFTRSQRLNSEAIIDFVKALCKVSMDELRSPSDPRVFSLTKIVEIAHYNMNRIRLVWSSIWHVLSDFFVTIGCSDNLSIAIFAMDSLRQLSMKFLEREELANYNFQNEFMKPFVVVMRKSGAVEIRELIIRCVSQMVLSRVDNVKSGWKSMFMIFTTAAHDAHKNIVFLSFEMVEKIIRDYFPHITETETTTFTDCVNCLVAFTNCKFEKDISLQAIAFLQYCARKLAEGYVGSSLRRNPPLSPQGGKIGKQDSGKFLESDEHLYSWFPLLAGLSELSFDPRAEIRKVALKVLFDTLRNHGDHFSLALWERVFESVLFRIFDYVRQDVDPSEDDSTDQRGYNGEVDQESWLYETCSLALQLVVDLFVNFYKTVNPLLKKVLMLFVSLIKRPHQSLAGAGIAALVRLMRDVGHQFSNEQWLEVVSCIKEAADATSPDFSYVTSEDLMEDVSNEDETNDNSNDALRRRNRQLHAVVTDAKSKASIQIFVIQAVTDIYDMYRMSLTANHMLMLFDAMHGIGSNAHKINADLLLRSKLQELGSSLESQEAPLLRLENESFQTCMTFLDNLISDQPVGYNEAEIESHLISLCREVLEFYINISCSKEQSSRWAVPSGSGKKKELTARAPLVVAAIQTLGNMGESLFKKNLPELFPLIATLISCEHGSGEVQVALSDMLQTSMGPVLLRSCC
Protein: Uncharacterized protein (A0A1D8PQI2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MSLHISPFSVATNALVLSLAGIASAQNLGGLDTPPQAKTDTTKATENTSSILIKTEENSQDTTNEKTTEPNTTTQETTTQEATTTPETTKAESTDQIKTSQIVQTTKITQTQVETSTTQVVQTIQASSGGTTPQVLTKQSTITAAGTQTTLVTQTLVVVDGQSQKHSTVTLQSASTVSPITPNESTTVWWTPSTTQLNSGSLGKYGSATPVTENESTTIWWTPSTQITSSTTSGKASDTTSQKSDTGSNTKSSGGSSDTKSVWIATTGSDFASQSNSDSSSTASRNSSSSASRQAVIIGSKDLTWKKTLLCGGVIGVSLLLNLL
Protein: Excitatory amino acid transporter 5 (Solute carrier family 1 member 7) (Q8JZR4)
Organism: Mus musculus (Mouse)
Function: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (By similarity). Acts primarily as an inhibitory glutamate-gated chloride channel being a major inhibitory presynaptic receptor at mammalian rod bipolar cell axon terminals. Glutamate binding gates a large Cl(-) conductance that mediates inhibition, affecting visual processing in the retina.
Subcellular location: Photoreceptor inner segment membrane {ECO:0000269|PubMed:16973698}; Multi-pass membrane protein {ECO:0000255}. Synaptic cell membrane {ECO:0000269|PubMed:16973698}; Multi-pass membrane protein {ECO:0000255}. Note=Located in both cone and rod photoreceptor terminals and in axon terminals of rod bipolar cells. {ECO:0000269|PubMed:16973698}.
Interaction partners:
- Excitatory amino acid transporter 2
Sequence:
MVLDAVLARGRTVCKHNGLLILSVLSVIVGCLLGFFLRTQRLSPQEISYFQFPGELLMRMLKMLILPLVVSSLMSGLASLDAKTSSRLGILTVAYYLWTTFLAVVVGIIMVSIIHPGGAAQKETTEQSGKPVMSSADALLDLVRNMFPANLVEATFKQYRTKTTPVIKSPRGAAEEAPRRIVIYGVQEDNGSRVQNFALDLTPPPEIVYKSEPGTSDGMNVLGIVIFSATMGIMLGRMGDSGTPLVSFCQCLNESVMKIVAVAGWYFPFGIVFLIAGKILEMDDPKAVGKKLGFYAVTVVCGLVVHGLLILPLLYFLITKKNPIVFIRGVLQALLIALATSSSSATLPITFKCLLENNHIDRRIARFVLPVGATINMDGTALYEAVAAIFIAQVNNYELDFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDINLIIAVDWALDRFRTMINVLGDALAAGIMAHICRKDFAQDMGTEKLLPCETKPVTLQEIVAAQQNGCVKSVAEASELTLGPTCPHHIPVQVEQDEDPAAASLDHCTIEISELETNV
Protein: Acireductone dioxygenase (Acireductone dioxygenase (Fe(2+)-requiring)) (ARD') (Fe-ARD) (EC 1.13.11.54) (Acireductone dioxygenase (Ni(2+)-requiring)) (ARD) (Ni-ARD) (EC 1.13.11.53) (Q03677)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site (By similarity). Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway (By similarity).
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Enolase-phosphatase E1
- Methylthioribulose-1-phosphate dehydratase
- Polyol phosphate phosphatase PYP1
- Aromatic/aminoadipate aminotransferase 1
- Methylthioribose-1-phosphate isomerase
- S-methyl-5'-thioadenosine phosphorylase
Sequence:
MVKVYIHDNKVDSDYRAPHNSGTELSLDELAKLGVIYKYCANEEEVNEIARQREYKNRDVVNICEGSFKSEAEFNEKLATFYQEHLHEDEEIRYCLEGAGYFDVRDASTPENWIRCLVESGDLLILPPGIYHRFTLTTSNHIKALRLFKDEPKWQAINRSNQADSLPVRKDYIALINQY
Protein: Ctenidin-1 (Ctenidin-2) (P86798)
Organism: Cupiennius salei (American wandering spider)
Function: Antimicrobial protein with bacteriostatic activity against the Gram-negative bacterium E.coli, and very weak activity against the Gram-positive bacterium S.aureus. Lacks activity against the yeast C.albicans.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8I948}.
Interaction partners:
Sequence:
MKHLIPLIVMASVVLAVYADRGYGGGRRGGGYGGGGYGGGGYGGGGGGYGGGVGGGRGGGGGLGGGRGGGGGVIDGKDDVGLGGGGYGGGLGGGQGGGGGLGGGQGGGGGLGGGRGGGGYGGGGGGYGGGKYGGGKYGGK
Protein: Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1 (P1) (Q9H1E3)
Organism: Homo sapiens (Human)
Function: Chromatin-associated protein involved in DNA repair by promoting homologous recombination (HR). Binds double-stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures, but with less affinity than RAD51AP1.
Subcellular location: Nucleus {ECO:0000269|PubMed:11298763, ECO:0000269|PubMed:26323318}. Chromosome {ECO:0000269|PubMed:26323318}.
Interaction partners:
- Ras-related protein Rab-7L1
- Solute carrier family 41 member 1
- N-fatty-acyl-amino acid synthase/hydrolase PM20D1
- Solute carrier family 45 member 3
- Phosphorylated adapter RNA export protein
Sequence:
MSRPVRNRKVVDYSQFQESDDADEDYGRDSGPPTKKIRSSPREAKNKRRSGKNSQEDSEDSEDKDVKTKKDDSHSAEDSEDEKEDHKNVRQQRQAASKAASKQREMLMEDVGSEEEQEEEDEAPFQEKDSGSDEDFLMEDDDDSDYGSSKKKNKKMVKKSKPERKEKKMPKPRLKATVTPSPVKGKGKVGRPTASKASKEKTPSPKEEDEEPESPPEKKTSTSPPPEKSGDEGSEDEAPSGED
Protein: Protein BONZAI 3 (Q5XQC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of cell death and defense responses. Repress a number of R genes and may have effects in promoting growth and development. May function in membrane trafficking and in fusion of vesicles with plasma membrane (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Protein kinase family protein
- Alpha/beta-Hydrolases superfamily protein
- ACD11 homolog protein
- Protein LAZ1
Sequence:
MGGCLSGDVKGGKQAIGGVQQRPTSSTIANNAAHNDAVDFFFRSRGQYPLFSQIELTLSASNLLDCDITSKSDPMAVMYLRKKDGRLEEIGRTEVILNNLNPKWIEKITVSFQFEAVQTLVFHVYDVDTRYHNVPVKTLKLKDQDFLGEGTCVLSEIMTRQNRTLTLTLTGNVRAGVNRNLGTLSIQAEETVASKTVAEINFRCVNLDNKDLFSKSDPFLRISRVVETSAAVPICRTEVVDNNLNPMWRPVCLTMQQFGSKDTPLVIECLDFNTSGNHELIGKTEKSVAELERLCLQKEAANFVYPSLSHGRNKVLKGQLIVDRYVEKVQYSFLDYISSGFELNFMVAVDFTASNGDPRTPSSLHYIDPSGRLNSYQQAIMEVGEVIQFYDSDKRFPAWGFGGRTSDGSVSHAFNLNGASYGDEVVGVEGIMVAYASALRNVSLAGPTLFSNVVDKAAHTASQSLSQNSPKYFVLLIITDGVLTDMAGTVDALVRASDLPLSVLIVGVGNTDFKQMEMLDADNGRRLESSTGRIATRDIVQFVPMKDIHSGLVSVVQALLEELPGQFLTYVRSRKINPIGAPAI
Protein: Lysosome membrane protein 2a (Lysosome membrane protein II) (Scavenger receptor class B, member 2) (Q8JGR8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Tetraspanin
- Scavenger receptor class B, member 2c
- Lysosome membrane protein 2 isoform X1
- Apolipoprotein Ba.
Sequence:
MTRRSCTIYATGIVCAHLLILGIALLLAQVFQTMIQERIKKEITLAENSRVLDGWINPPPPVYMQYFFFNVTNPDEFLAGKEKAKVTQMGPYTYREYRPRENVTYLENGTKIFATNPKSFVFLRNMSAGDPEVDRVTTVNIPMIAVMNELNSYSFFVRTAVSMYMGSMGMGLFMNRTVHEILWGFKDPLLTKLHAMRPEVDEHFGLMYNKNGTHEGEFVFHTGEKNYMNYGKIDTWNGISQMNWWSSNQSNMINGTDGSVFHTFLSRKELLYIFAADLCRSIHLGYVRDMEVKGIPAFRFAPPSDVLAPPDENPANAGFCVPAGDCLGKGVLKVSVCRQGAPIVVSFPHFYQADERYINAIEGMNPNEEEHETYLDINPTTGVPIRACKRAQLNIILKRVRGFPNTKFLNETIFPIMYVNETATIDDESAAQMRMLLLIVTVVSNFPVIILALGVILLVVLIFLVCRNRQRKNEVKRIDFTEAFHSFATTKDETAYTQVSNQAEDSPENRNNQPLRNGSYIAMSPVEAQKC
Protein: Clotting factor B (EC 3.4.21.85) (Coagulation factor B) [Cleaved into: Clotting factor B light chain; Clotting factor B heavy chain] (Q27081)
Organism: Tachypleus tridentatus (Japanese horseshoe crab)
Function: This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system which may play important roles in both hemostasis and host defense mechanisms. Its active form catalyzes the activation of proclotting enzyme. Does not activate the mammalian coagulation factors factor IX, factor X, prothrombin, plasminogen, protein C or prekallikrein. Does not hydrolyze fibrinogen. Does not catalyze the activation of factor C or coagulogen.
Subcellular location: Secreted {ECO:0000305}. Note=Secreted in hemolymph. {ECO:0000305}.
Interaction partners:
Sequence:
MTWICVITLFALASATLGNKVSRVGVLFPKTRNDNECTARGGLKGSCKSLIDCPSVLATLKDSFPVVCSWNGRFQPIVCCPDAIAPPPVTTTAVTVISTKEPKLPRLHISGCGKRKVKIDITTVGRSGSPILPPISTPQNSTGGRGIIAGGVEAKIGAWPWMAAVFVKNFGIGRFHCAGSIISNKYILSAAHAFLIGGRKLTPTRLAVRVGGHYIKRGQEYPVKDVIIHPHYVEKENYNDIAIIELKEELNFTDLVNPICLPDPETVTDPLKDRIVTAAGWGDLDFSGPRSQVLREVSIPVVPVDKCDQAYEKLNTPSLKNGITNNFLCAGLEEGGKDACQGDSGGPLMLVNNTRWIVVGVVSFGHKCAEEGYPGVYSRVASYLDWIAKVTNSLDHAVTN
Protein: Cleavage and polyadenylation specificity factor subunit 7 (Cleavage and polyadenylation specificity factor 59 kDa subunit) (CPSF 59 kDa subunit) (Cleavage factor Im complex 59 kDa subunit) (CFIm59) (Pre-mRNA cleavage factor Im 59 kDa subunit) (Q8N684)
Organism: Homo sapiens (Human)
Function: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation. The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs. CPSF7 activates directly the mRNA 3'-processing machinery. Binds to pA signals in RNA substrates.
Subcellular location: Nucleus {ECO:0000269|PubMed:19864460, ECO:0000305|PubMed:20695905}. Cytoplasm {ECO:0000269|PubMed:19864460}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm) (PubMed:19864460). {ECO:0000269|PubMed:19864460}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 5
- Cleavage and polyadenylation specificity factor subunit 6
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage stimulation factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 3
- Splicing factor U2AF 65 kDa subunit
- Cleavage and polyadenylation specificity factor subunit 4
- pre-mRNA 3' end processing protein WDR33
- Symplekin
Sequence:
MSEGVDLIDIYADEEFNQDPEFNNTDQIDLYDDVLTATSQPSDDRSSSTEPPPPVRQEPSPKPNNKTPAILYTYSGLRNRRAAVYVGSFSWWTTDQQLIQVIRSIGVYDVVELKFAENRANGQSKGYAEVVVASENSVHKLLELLPGKVLNGEKVDVRPATRQNLSQFEAQARKRECVRVPRGGIPPRAHSRDSSDSADGRATPSENLVPSSARVDKPPSVLPYFNRPPSALPLMGLPPPPIPPPPPLSSSFGVPPPPPGIHYQHLMPPPPRLPPHLAVPPPGAIPPALHLNPAFFPPPNATVGPPPDTYMKASAPYNHHGSRDSGPPPSTVSEAEFEDIMKRNRAISSSAISKAVSGASAGDYSDAIETLLTAIAVIKQSRVANDERCRVLISSLKDCLHGIEAKSYSVGASGSSSRKRHRSRERSPSRSRESSRRHRDLLHNEDRHDDYFQERNREHERHRDRERDRHH
Protein: Dual specificity protein phosphatase (EC 3.1.3.16) (EC 3.1.3.48) (Q7TNL7)
Organism: Mus musculus (Mouse)
Interaction partners:
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 11
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
Sequence:
MESLSRSCLWLRQELSSPRPQLLLLDCRSRELYESARICGALSVALPSLMLRRLRRGSMSVRSLLPGPPLQPPPPAPVLLYDQGSSGQCHREAAEAEAKAEPKAEAEAEPKAEAEAEPKAEAENEAEAKAEAKAEAKAEAKAEAKAEAKAEAKAEAKAEAKAEAKEEWDADSVLGVLLQKLREEGYPAYYLQGGFSKFQAECPHLCETSFSGRAGSGLGSMSSPVPVVGLGGLCLSSDFSDAESEADRDTLSCGLDSENTTSPPAGLLPPFPVQILPNLYLGSARDSANLESLAKLGIRYILNVTPNLPNLFEKNGDFHYKQIPISDHWSQNLSQFFPEAIAFIDEALSQNCGVLVHCLAGVSRSVTVTVAYLMQKLHLSLNDAYDLVKRKKSNISPNFNFMGQLLDFERSLRLGGKRSGGRGSGGPESTVSDPPSFFTTPTSDGVFELDPT
Protein: Ribonuclease E (RNase E) (EC 3.1.26.12) (Q1ZS71)
Organism: Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 / CCUG 15956))
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}. Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00970}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00970}.
Interaction partners:
Sequence:
MKRMLINATQKEELRVALVDGQKLFDLDIESPGHESKKANIYKGRITRIEPSLEAAFVDYGAERHGFLPLKEVAKDYFPANYSYQGRPNIKEVLKEGQEVIVQVDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGEERTQLKAALSTLDLPQGMGLIVRTAGVGKSGEELEWDLNVLLNHWNAVKEAADSQSAPFLIHQESNVIARAIRDYLRRDIGEILIDSPKIFDRARDHIKLVRPDFLSRVKRYEGEVPLFSHYQIESQIDSAFQREVRLPSGGSVVIDPTEALTSIDINSARATKGGDIEETALQTNLEAADEIARQLRLRDLGGLVVIDFIDMTPVRHQREVENRLREAVRMDRARVQIGRISRFGLLEMSRQRLSPSLAEASHHVCPRCSGTGVVRDNESLSLSILRLIEEEALKDNSSQVLAIVPVPVASYLLNEKRRSVQHIEKYHGVRVVIVPNSDMETPHFEVLRIREGEEQDTLSYHIPKTLEALKEAEAIEAPQPERVIKKREEPVLQGFTAPKQPAPVAKPAAKPTPKVTAKPATESTKKPGLLSRFFSALASFFSGSPEQQQEKPVEAKVEQNNNQNNRRNNNRRNDRSDNRRNNRDNSRDNNRRNNRQDNNDVENNDERQERNNEQRQNRRRNDRNDKNRQQQNDKAAKAPRQNRNNDEAKEQKRQSRKEEIQAQKQQRQQQGEQTAKATTEQPADAQRDSEEKAVKVKQRRQRRQLRKKVRITDNVEKSVEQQNATVDAVEKVEAVETAVEQTPSPLMALGTSIAKEAQDKPEKTQVVSDEQTDNEEQEGTQRRNRRSPRHLRASGQRRRRMRDTRVEKSDFVTNEEANAIEQAAIDAADSISEMVNVVSIVEKPKTMRPTSGVAIPEMAMGKVWSRIKPAVEAPVEKNITQEKADTADMIDEVETNDIIINTPVVEAKSEIVAVETTTLSGVAIPEMAMGKVIPRYTAEETTVEMKSEPAPEQVIEKPVIVEEVAAPVIKTEETVEIKSPVTAVVDLPAVAKAVMATSPRGFHAASAMTKAPAPEEHVSGSVVQAAPLRERSNTRAAGSQTATNSAAAPMTKPSFD
Protein: 3 beta-hydroxysteroid dehydrogenase type 7 (3 beta-hydroxysteroid dehydrogenase type VII) (3-beta-HSD VII) (3-beta-hydroxy-Delta(5)-C27 steroid oxidoreductase) (C(27) 3-beta-HSD) (EC 1.1.1.-) (Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase) (EC 1.1.1.181) (Q9H2F3)
Organism: Homo sapiens (Human)
Function: The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. HSD VII is active against four 7-alpha-hydroxylated sterols. Does not metabolize several different C(19/21) steroids as substrates. Involved in bile acid synthesis. Plays a key role in cell positioning and movement in lymphoid tissues by mediating degradation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC): 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells.
Subcellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein.
Interaction partners:
- Aldo-keto reductase family 1 member D1
- Cytochrome P450 7B1
- 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase
- Cytochrome P450 7A1
- 24-hydroxycholesterol 7-alpha-hydroxylase
- Ubiquitin-like protein FUBI
- Cholesterol 25-hydroxylase
- Alpha-methylacyl-CoA racemase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Lanosterol 14-alpha demethylase
Sequence:
MADSAQAQKLVYLVTGGCGFLGEHVVRMLLQREPRLGELRVFDQHLGPWLEELKTGPVRVTAIQGDVTQAHEVAAAVAGAHVVIHTAGLVDVFGRASPKTIHEVNVQGTRNVIEACVQTGTRFLVYTSSMEVVGPNTKGHPFYRGNEDTPYEAVHRHPYPCSKALAEWLVLEANGRKVRGGLPLVTCALRPTGIYGEGHQIMRDFYRQGLRLGGWLFRAIPASVEHGRVYVGNVAWMHVLAARELEQRATLMGGQVYFCYDGSPYRSYEDFNMEFLGPCGLRLVGARPLLPYWLLVFLAALNALLQWLLRPLVLYAPLLNPYTLAVANTTFTVSTDKAQRHFGYEPLFSWEDSRTRTILWVQAATGSAQ