wanglab/gogpt-training-data huggingface dataset:
Protein: V-type proton ATPase subunit H (V-ATPase subunit H) (V-ATPase 54 kDa subunit) (Vacuolar proton pump subunit H) (P41807)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments. This subunit is essential for activity, but not assembly, of the enzyme complex. This subunit is also required for silencing the ATPase activity of V-ATPase when V1 is detached from V0.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:8349704}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit c
- V-type proton ATPase subunit a, vacuolar isoform
- V-type proton ATPase subunit a, Golgi isoform
- V-type proton ATPase subunit G
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit D
- V-type proton ATPase subunit E
- V-type proton ATPase subunit C
- V-type proton ATPase subunit F
- V-type proton ATPase catalytic subunit A
Sequence:
MGATKILMDSTHFNEIRSIIRSRSVAWDALARSEELSEIDASTAKALESILVKKNIGDGLSSSNNAHSGFKVNGKTLIPLIHLLSTSDNEDCKKSVQNLIAELLSSDKYGDDTVKFFQEDPKQLEQLFDVSLKGDFQTVLISGFNVVSLLVQNGLHNVKLVEKLLKNNNLINILQNIEQMDTCYVCIRLLQELAVIPEYRDVIWLHEKKFMPTLFKILQRATDSQLATRIVATNSNHLGIQLQYHSLLLIWLLTFNPVFANELVQKYLSDFLDLLKLVKITIKEKVSRLCISIILQCCSTRVKQHKKVIKQLLLLGNALPTVQSLSERKYSDEELRQDISNLKEILENEYQELTSFDEYVAELDSKLLCWSPPHVDNGFWSDNIDEFKKDNYKIFRQLIELLQAKVRNGDVNAKQEKIIIQVALNDITHVVELLPESIDVLDKTGGKADIMELLNHSDSRVKYEALKATQAIIGYTFK
Protein: SH3 and cysteine-rich domain-containing protein 2 (24b2/STAC2) (Src homology 3 and cysteine-rich domain-containing protein 2) (Q8R1B0)
Organism: Mus musculus (Mouse)
Function: Plays a redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity. Slows down the inactivation rate of the calcium channel CACNA1C.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29467163}. Cell membrane {ECO:0000269|PubMed:25548159}; Peripheral membrane protein {ECO:0000305|PubMed:25548159}; Cytoplasmic side {ECO:0000305|PubMed:25548159}. Cell membrane, sarcolemma {ECO:0000269|PubMed:29467163}; Peripheral membrane protein {ECO:0000269|PubMed:29467163}; Cytoplasmic side {ECO:0000269|PubMed:29467163}. Note=Colocalizes with CACNA1C at the plasma membrane of transfected cells. {ECO:0000269|PubMed:25548159}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent L-type calcium channel subunit alpha-1C
Sequence:
MTEMSEKENEPDDAATHTPPGTVSTLQETKLQRFKRSLSLKTILRSKSVENFFLRSGSELKCPTEVLLTPPTPLPPPSPPPASTDRGLPTPTPSPCPVPRPLAPLKPVRLHSFQEHVFKRASPCELCHQLIVGNSKQGLRCKTCKVSVHLWCSEEISHQQCPGKTSTSFRRNFSSPLLVHAPPPACAMNKESPPTGTSGKVDPVYETLRYGTSLALMNRSSFSSTSESPTRSLSERDELTEDGEGSIRSSEEGPGDSVFTAPAESEGSGPEEKSPGQQPPKLPLRKDVGPMYSYVALYKFLPQENNDLALQPGDRIMLVDDSNEDWWKGKIGDRVGFFPANFVQRVRPGENVWRCCQPFSGNKEQGYMSLKENQICVGVSRSKDSDGFIRVSSGKKRGLVPADSLAEI
Protein: Anthrax toxin receptor 2 (Q00IM8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MVAGRSRARSPGSWLFPGLWLLTVGGPGSLLQAQEQPSCKKAFDLYFVLDKSGSVANNWIEIYNFVHQLTERFVSPEMRLSFIVFSSQATIILPLTGDRYKISKGLEDLKAVQPVGETYIHEGLKLANEQIQNAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKKSRSLGASVYCVGVLDFEQAQLERIADSKDQVFPVKGGFQALKGIINSILAQSCTEILELSPSSVCVGETFQVVLSGRAVMSIRDDGSVLCTFTANSTYTKNEKPVSVQPGSILCPAPVLNKAGETLEVSIAFNDGKSAVSRSLTITATECSNGIAAIIAILVLLLLLGAALMWWFWPLCCKVVIKDPPPPPSPPKEEEEEEPLPNKKWPTVDASYYGGRGVGGIKRMEVRWGDKGSTEEGARLEKAKNAVVMIPEEEIPVPSRPPRPKPTHQAPQTKWYTPIKGRLDALWALILKQYDRVSLMRPQEGDEGRCINFSRVPHQ
Protein: Extracellular superoxide dismutase [Cu-Zn] (EC-SOD) (EC 1.15.1.1) (P08294)
Organism: Homo sapiens (Human)
Function: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Subcellular location: Secreted, extracellular space. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O09164}. Note=99% of EC-SOD is anchored to heparan sulfate proteoglycans in the tissue interstitium, and 1% is located in the vasculature in equilibrium between the plasma and the endothelium.
Interaction partners:
- Copper chaperone for superoxide dismutase
- Copper transport protein ATOX1
- Parkinson disease protein 7
- Catalase
- Copper-transporting ATPase 1
- Superoxide dismutase, mitochondrial
- Superoxide dismutase
- Glutathione peroxidase 3
- Probable glutathione peroxidase 8
- Glutathione peroxidase 7
Sequence:
MLALLCSCLLLAAGASDAWTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALHAACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGDLSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVVHAGEDDLGRGGNQASVENGNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA
Protein: Ribose-phosphate pyrophosphokinase (RPPK) (EC 2.7.6.1) (5-phospho-D-ribosyl alpha-1-diphosphate synthase) (Phosphoribosyl diphosphate synthase) (Phosphoribosyl pyrophosphate synthase) (P-Rib-PP synthase) (PRPP synthase) (PRPPase) (P0A717)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
Interaction partners:
- Amidophosphoribosyltransferase
- Bifunctional protein GlmU
- Transketolase 1
- Ribokinase
- Ribose-5-phosphate isomerase A
- Transketolase 2
- Ribose-5-phosphate isomerase B
- Orotate phosphoribosyltransferase
- Phosphopentomutase
- Phosphoglucomutase
Sequence:
MPDMKLFAGNATPELAQRIANRLYTSLGDAAVGRFSDGEVSVQINENVRGGDIFIIQSTCAPTNDNLMELVVMVDALRRASAGRITAVIPYFGYARQDRRVRSARVPITAKVVADFLSSVGVDRVLTVDLHAEQIQGFFDVPVDNVFGSPILLEDMLQLNLDNPIVVSPDIGGVVRARAIAKLLNDTDMAIIDKRRPRANVSQVMHIIGDVAGRDCVLVDDMIDTGGTLCKAAEALKERGAKRVFAYATHPIFSGNAANNLRNSVIDEVVVCDTIPLSDEIKSLPNVRTLTLSGMLAEAIRRISNEESISAMFEH
Protein: Titin (O97791)
Organism: Oryctolagus cuniculus (Rabbit)
Interaction partners:
Sequence:
MTTQAPTFTQPLQSVVVLEGSAATFEAHVSGFPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLTIPAVTKANSGRYSLRATNGSGQATSTAELLVTAETAPPNFVQRLQSMTVRQGSQVRLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATSTAELLVQGEEVVPAKRTKTIVSTAQISETRQTRIEKKIEAHFDARSIATVEMVVDGATGQQLPHKTPPRIPPKPKSRSPTPPSIAAKAQLARQQSPSPIRHSPSPVRHVRAPTPSPVRSVSPAGRISTSPIRSVKSPLLVRKTQTTTMATGPEVPPPWKQEGYVASSTEAEMRETTMTSSTEIRREERWEGRYGLQEQVTITGAAGAAAAVSTSAAFAGLGSWFATGAKEVKQEADKSAAVATVVAAVDMARVREPVISAVEQTAQRTTTTAVHIQPAQEQVRKEAEKIAVSKVVVAADKAKEQELKSRTREIITTKQEQMHITHEQLRKETEKAFVPKVVISAAKAKEQETRITGEITTKQEQKQITQETMMKETRKTVVPKVIVATPKVKEQDLVSRSREGISTKREQVQITQEKMRKEAEKTALSTIAVATAKATEQETVLRTREGMATRQEQIQVTHGKVGVGKKAEAVATVVAAVDQARVREPREPGLPEDSYAQQTTLEYGYKEHISATKVAEHPKRPASEPHVVPKAVKPVVIQAPSETHIKTTEQVGMHISSQIKKTTDVTSERLVHVDKRPRTASPHFTVSKISVPKTEHGYEASIAGSAIATLQKELSATSSAQKITKSVKAPTVKPAEARVRAEPTPSPQFPFAATPDTYKSQAGIEVKKEVGVSITGSAVREERLEVLHGREAKVTEMARVPAPAEIPVTPPTLVSGLKNMTVIEGESVTLECHISGYPSPTVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDRGRFTCSAVNEAGTVSTSCYLAVQVSEEFEKETTVAEKLTTEEKRFVESRDVVMTDTTITEEQAMPGEPAAPFFITKPVVQKLVEGGSVVFECQIGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGECKLVISMTFADDAGEYTIVIRNKHGETSASASLLEEAEYESLMKSQQEMLYQTQMTAFVQEPKVGEIAPGFVYSEYEKEYEKEQALIRKKMAKDTVMVRTFVEDQEFHISSFEERLIKEIEYRIIKTTLEELLEEDGEEKMAVDISESEAIESGFELRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIKPGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYVEPAAPLGAPTYIPTPEPVSRIRSVSPRSVSRSPIRMSPARMSPARMSPGRRLEETDESQLERLYKPVFVLKPTSFKCLEGQSARFDLKVVGRPMPETFWFHNGQQVVNDYTHKVVIKEDGTQSLIIVPATPSDSGEWTVVAQNRAGKSTISVILTVEAVEHQVKPVFVEKLKNVNVKEGARLEMKVRATGNPNPDIVWLKNSDIIVPHKYPKIIIEGTKGQAALKIDSTVSQDSAWYTATAINKAGRDTTRCKVNVEVEFAEPEPERRLIIPRGTYRAKEIAAPALEPLHLRYGQEQWEEGDLYDKEKQQKPFFKKKLSSLRLKRFGPAHFECRLTPIGDPTMVVEWLHDGKPLEAANRLRMINEFGYCSLDYGVAYSRDSGVITCRATNKYGTDHTSATLIVKDEKSLVEESQLPEGRKGLQRIEELERMAHEGALTGVTADQKEKQKPDIVLYPEPVRVLEGETARFRCRVTGYPQPKLNWYLNGQLIRKSKRFRVRYDGIHYLDIVDCKSYDTGEVKVTAENPEGVIEHKVKLEIQQREDFRSVLRRAPEPKPEFHIHESGKLQFEVQKVDRPVDTSETKEVVKLKRAERITHEKVSEESEELRSKFKRRTEEGYYEAITAVELKSRKKDESYEELLKKTKDELLHWTKELTAEEKKAL
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (dUTP-pyrophosphatase-like 1) (AtDUT1) (Q9STG6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP, preventing uracil incorporation into DNA.
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- dCMP deaminase
- Thymidine kinase b
- Thymidine kinase a
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Thymidylate kinase
- Nucleoside diphosphate kinase 1
- Nucleoside diphosphate kinase II, chloroplastic
- Nucleoside diphosphate kinase III, chloroplastic/mitochondrial
Sequence:
MACVNEPSPKLQKLDRNGIHGDSSPSPFFKVKKLSEKAVIPTRGSPLSAGYDLSSAVDSKVPARGKALIPTDLSIAVPEGTYARIAPRSGLAWKHSIDVGAGVIDADYRGPVGVILFNHSDADFEVKFGDRIAQLIIEKIVTPDVVEVDDLDETVRGDGGFGSTGV
Protein: Pcdha6 protein (Q05C01)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MPSLRGGPEVRQCLLLLLPFLAAWEAGNGQLHYSVPEEAKHGTFVGRIAQDLGLELTELVPCLFRVASKDRGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVRDINDNPPRFPMTEKTIQFSESRSLDSRFPLEGASDADIGVNALLSYKLSPSELFFLDVQTSDELSQSLFLVLGKSLDREEDAEVKLLLVATDGGKPELTGTVQILIKVLDVNDNEPTFPQSVYKVQLLENTANGTLVMKLNASDADEGSNSEIVYSLGSDVSSTTRTKFQIDPNSGEVRTKGELDYEERTSYEIQVIASDKGTPAMSGHCKISVKLVDINDNTPEVSITSLSLPVQENAPLGAVIALISVSDRDSGVNGQVTCSLSPHVPFKLVSTFKNYYSLVLDSALDREATADYKVMVTARDGGSPSLRATASVSVEVADVNDNAPVFAQPEYTVFVKENNPPGAHIFTVSAMDADAQENALVSYSLVERRVGERLLSSYVSVHAESGKVFALQPLDHEELELLQFQVTARDAGVPALGSNVTLQVFVLDENDNAPLLLPQGAVGVGGSVSELVPRSVGSGHVVTKVRAVDADSGYNAWLSYELQSTVGMRSLFRVGLYTGEISTTRALDEVDAPRQRLLVLVKDHGEPSLTATATVLVSLVENSQAPKTSSRALVDAAGQEASLVTVNVYLVIAICAVSSLLVLTLLLYTALRCSAMPTDGACAPGRPMLVCSSAVGSWSYSQQRRQRVCSGEGPPKTDLMAFSPSLSQGPESAEERQPPLEAEYLGKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEETKKKKKK
Protein: Proteasome (Prosome, macropain) 26S subunit, non-ATPase, 14 (Proteasome 26S subunit, non-ATPase 14) (Psmd14 protein) (Q4V8E2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome regulatory subunit 7
- Proteasome subunit alpha type-4
- 26S proteasome regulatory subunit 6A
- 26S proteasome non-ATPase regulatory subunit 2
- Proteasome subunit alpha type-2
- 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 1
- Proteasome
- 26S proteasome regulatory subunit 4
Sequence:
MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK
Protein: Cholinergic receptor nicotinic alpha 1 subunit (B8ZZD3)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEPWPLLLLFSLCSAGLVLGSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPNWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAAEWKYVAMVMDHILLGVFMLVCIIGTLAVFAGRLIELNQQG
Protein: Transcriptional regulatory protein RXT3 (Q07458)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcriptional regulatory protein RXT2
- Histone deacetylase complex subunit CTI6
- Transcriptional regulatory protein UME1
- Transcriptional regulatory protein SDS3
- Transcriptional regulatory protein SIN3
- Histone deacetylase RPD3
- Transcriptional regulatory protein UME6
- Transcriptional regulatory protein DEP1
- Transcriptional regulatory protein SAP30
- Transcriptional regulatory protein PHO23
Sequence:
MSVSEQDPNRAYRETQSQIYKLQETLLNSARTKNKQEEGQESNTHSFPEQYMHYQNGRNSAYDLPNVSSQSVLAFTEKHYPNKLKNLGTLYYNRFKEGSFDEDSTSYSDRHSFPYNLYDNTLPPPFLPAIGIQNINNIATLKITYEDIQASFNNIESPRKRNNEIWGCDIYSDDSDPILVLRHCGFKIGAPSGGSFHKLRRTPVNVTNQDNVTGNLPLLEGTPFDLEVELLFLPTLQKYPSVKRFDITSREWGSEATVIHDGLSYGIYSIVIKQRLDRDKPHEPNGYIKNLKWT
Protein: UPF0397 protein SP_0482 (Q97SA4)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01572}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01572}.
Interaction partners:
Sequence:
MEIKFTIKQVVAVGIGAALFVVIGMINIPTPVPNTSIQLQYAVQALLSIIFGPIIGLLVGLIGHAIKDSLVGYGLWWTWIIASGLFGLVVGLFRKYVRVINGVFDWKDILIFNLIQLLANALVWGVLAPLGDVVIYQEAAEKVFAQGIVAGIANGVSVAIAGTLLLLAYAGTQTRAGSLKKD
Protein: Methylecgonone reductase (MecgoR) (EC 1.1.1.334) (E7C196)
Organism: Erythroxylum coca (Coca plant)
Function: Catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis. Can also use 6-hydroxytropinone, tropinone and nortropinone as substrates, but not 8-thiabicyclo[3.2.1]octan-3-one (TBON), cyclohexanone, cyclooctanone or N-methyl-4-piperidone. NADH can substitute for NADPH, but with a decreased activity.
Interaction partners:
Sequence:
MERQVPRVLLNSGHEMPVIGFGTAIDPLPEPEQLVSAILHAIEVGYRHFDTASAYMTEEPVGRAISEAMKRGLIKGREELFVTSKLWCADAHRDLIIPALKETLKRLGLDYLDLYLIHFPVRLKKEAVSLEHEIDDFRFEDHELLPFDIKGTWEAMEECSRLGLTKSIGVSNYGTVKISQLLQHATIPPAVNQVEMNVAWQQKKLREFCSKKGIHVTAWSPLAGIGAFWGSTVVIESKTLKEIAAAKGKSVAQVALRWIQDQGASCIVKSMNKDRMKQNLEIFGWKLSDEDGRKIEQIKQSRLYPAKLFINENSPYPSLEALWDGDL
Protein: Spastin (EC 5.6.1.1) (A0A2U3TZR0)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Membrane {ECO:0000256|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03021}. Midbody {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000256|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Localizes to endoplasmic reticulum tubular network. {ECO:0000256|HAMAP-Rule:MF_03021}.
Interaction partners:
Sequence:
MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKMQPVLPFSKSQTDVYNDSTNLACRNGHLQSESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
Protein: STRA6-like (Zgc:162946 protein) (A3KP50)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MFLLSLVQRRARAQPFEDRFPYLKGRFGIVVPLDFIGSLSNRWSYGFAFGAIAPSVIQLFSESYAPFYVPNWAKAIVYLIGAIEVGVAYLPFFACLSTPHRVLGGILGLLYTLMWLIVRLYDTITCPAGKILGPYEKPIILWPFYLCLFFLLGRFVYIIVKAVRIHLKLQADENEEDLHSHQFRYVQTLLRRPPESPEPKSWFRRKVYDWDPYFKFPNRMIGTSIISFIGLYMMTLADYRLSEYTFDKLDSLKDSLEQIALSCNQTESVFTYLIPSINEFSIVARRSWLATTIFSTLTSVTYTFHVLVCYRKHLKRLWRGQKSFLPEKFHTPSPAVSVAAITRYSGWQIAFTLWGFLIVHFVQFLFALMFVYGVVLPIQKGHILSWLSNVGIILLTIFIVIALVVLQIILVQVFFLQDKLSPEDKEKPLAINNRKAFHSFNYFFFFYNVIMGLSNCVLRLVSSCIVGTWLVSRIDRTIMQRGYESMDPGYSTWIGMIFADHYHSNPVMVSFCHLLLGRTLEKGGPAACSYATFSNNTGCSVGGRVRLRWLVLYALLRNPSLILLRKTKKLPQTDSPDPLLLARAITSQAQQADAVCNKTAETEPAPLDI
Protein: Interferon regulatory factor 3 (F9UKT9)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSQSKPLLIPWLREQINSGRYPGVTWTNQEQTEFCIPWKHALRQDSCSDDVLIFKAWAEVSNGRVQGDHSIWKRNFRSALRAKGFKMLHDNKNDAANPNKLFQWPDEAPTGGSQQPEHDLYQDPSPLQQSHGLPCFNDLYLAAEETVYTAEGISTTINQDLLQKCLQGLNIEQTEAIRGYELPVEELQYPMEGTIGGHGLLGQQQNPVVMEDAVGGAVLPPQPVYPMDGAVGGAHEQRMVEQLTNELSRTMVDENFKAHFRVSVYYRGVKMPEQLVENEAGFRLVYRPELTQPLLDPDSGLNLVSLPSPPPVRDETQAKLTEDILALLGEGLGVGASGSIIYGLRKGEIKAFWSLDKFDNSRRPQGVSKCPEPLYQAKDFYGGLLKFINNEGKCPPFSLFFCLGEKWPDPDNRPWEKKLVMVEVVLTSLELLKSMAVEGGASSPQSVELQLSLQEYLQEMMDLC
Protein: D-alanine--D-alanine ligase (EC 6.3.2.4) (D-Ala-D-Ala ligase) (D-alanine:D-alanine ligase) (D-alanylalanine synthetase) (P9WP31)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the ATP-driven ligation of two D-alanine molecules to form the D-alanyl-D-alanine dipeptide. This molecule is a key building block in peptidoglycan biosynthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}.
Interaction partners:
- Alanine racemase
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
- UDP-N-acetylmuramate--L-alanine ligase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- Cell division protein FtsZ
- Probable peptidoglycan glycosyltransferase FtsW
- UDP-N-acetylenolpyruvoylglucosamine reductase
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
Sequence:
MSANDRRDRRVRVAVVFGGRSNEHAISCVSAGSILRNLDSRRFDVIAVGITPAGSWVLTDANPDALTITNRELPQVKSGSGTELALPADPRRGGQLVSLPPGAGEVLESVDVVFPVLHGPYGEDGTIQGLLELAGVPYVGAGVLASAVGMDKEFTKKLLAADGLPVGAYAVLRPPRSTLHRQECERLGLPVFVKPARGGSSIGVSRVSSWDQLPAAVARARRHDPKVIVEAAISGRELECGVLEMPDGTLEASTLGEIRVAGVRGREDSFYDFATKYLDDAAELDVPAKVDDQVAEAIRQLAIRAFAAIDCRGLARVDFFLTDDGPVINEINTMPGFTTISMYPRMWAASGVDYPTLLATMIETTLARGVGLH
Protein: Serine protease Do-like HtrA (EC 3.4.21.107) (Q9LA06)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Function: Degrades abnormal exported proteins and responsible for the propeptide processing of a natural pro-protein and for the maturation of a native protein. It also plays a prominent role in stress (heat shock, ethanol, puromycin and NaCl) resistance during active exponential growth.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAKANIGKLLLTGVVGGAIALGGSAIYQSTTNQSANNSRSNTTSTKVSNVSVNVNTDVTSAIKKVSNSVVSVMNYQKDNSQSSDFSSIFGGNSGSSSSTDGLQLSSEGSGVIYKKSGGDAYVVTNYHVIAGNSSLDVLLSGGQKVKASVVGYDEYTDLAVLKISSEHVKDVATFADSSKLTIGEPAIAVGSPLGSQFANTATEGILSATSRQVTLTQENGQTTNINAIQTDAAINPGNSGGALINIEGQVIGITQSKITTTEDGSTSVEGLGFAIPSNDVVNIINKLEADGKISRPALGIRMVDLSQLSTNDSSQLKLPSSVTGGVVVYSVQSGLPAASAGLKAGDVITKVGDTAVTSSTDLQSALYSHNINDTVKVTYYRDGKSNTADVKLSKSTSDLETSSPSSSN
Protein: Si:dkeyp-93d12.1 (Transcription cofactor vestigial-like protein 2a) (Q4V8U0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSCLDVMYQVYGPPQPYFAAAYTPYHHQKLAFYSKMQESPETVSGSSSSFSNLSGPPIKEEDCGREKDHPPEAEYISSRCVLFTYFQGDISSVVDEHFSRALSQSSSYAPGSTNSKTARGAASWRDGSFPMSQRSFPPSFWNSAYQPSVAASLSSALGSSHTDLPFPTDPYSSASLHSHLHQTTPEPWHPSHHHHPYSLSGAIGTQGSTYPRPSVHDMYGTHFDPRYGSLLVPSVRPHRLPSATVHAPGSSPCDISKSEAGSSGWTGAFTATSSDMSLNMDTGLQSQDKSKDLYWF
Protein: SH3 domain-containing protein (E6N0W0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MCGISSRSANNTPELEPGAEPPQKSPAPKTFEDKRQDNLSKGQAELERRRRVLEEEEQRRRAEVEKKEREEEAKKNRERQEKERQAEVERQAELERQRIIEAQREEEEKKRRLEMERRREEDEKMRKVQMEKAKVKQMQNQKQQENERLAQRQQREKTLQFQLQALDEKVIDVEVDIGKAKEAVAEVTGFIERMRSTRDEKVARIKELQETNQKTAIESQELGHQLLQKQSAHKETTQRKSELEALRRKRDAIRKAIEDAALELSTEKEKSYNQTEILKTNKEKYKTDVYSKLVAKREEYRNSFELLVHAQTHARSKIGEFEAKSAPASAAPAPAPAPAPTTTNGFPANFNDAFGEFDKTDASQRFDADFGATSTADPFAQIAQAPAHSKGAVDQSAFNIHDTYKCRALFAFEARSEDELSFEPGDVIIVFQSHAAEPGWRAGQLREKVGWFPEAFVEAIAAVPTPGGDPPIQNMPPNMTPSSSVDQIGVKAARKAEIAAAMGLTEGGAPPASSAPAAAAVISQCIAQFQWRARNEEDLSFAKGDTIEVLEKQEMKWKGRNPAGEIGWFPKSYVKEVGATTSTTTPIVSPSKASAGAPGAAAGAQYDVVPSDVTLQASETAPQQQLYTVIYDFEAVETTDLALHVGDTILVLEKNDEWWKGRCNGREGIFPANYVEISVQQAGDPTPPTQAPTPAAPPTVLCEAKVVVDFVASAPNQLGIKVGEIVKIREKSAAGWWEGELIRNGKPIAGWFPGEYVKVLEEAASPATRATAVYDYEASQPDELGFKTGDVIIVTDKSEAEWWSGHREQDPSKSGLFPSNYVQQQ
Protein: DNA ligase 6 (AtLIG6) (DNA ligase VI) (EC 6.5.1.1) (Ligase 1) (F4HPZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair (Probable). Required to maintain seed viability (e.g. longevity and storability) and during seed germination, probably by repairing DNA damage accumulated during seed development, storage and/or imbibition. Facilitates seed germination in cold conditions (2 degrees Celsius) and under oxidative stress (e.g. menadione, a genotoxic agent). Involved in repair of X-ray-induced damage.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- ATP-dependent DNA helicase 2 subunit KU80
- ATP-dependent DNA helicase 2 subunit KU70
- DNA polymerase lambda
- Proliferating cellular nuclear antigen 1
- Proliferating cell nuclear antigen 2
- DNA-repair protein XRCC1
- Flap endonuclease 1
- DNA repair protein RAD50
- Double-strand break repair protein MRE11
- Chlorophyll a-b binding protein 3, chloroplastic
Sequence:
MASDSAGATISGNFSNSDNSETLNLNTTKLYSSAISSISPQFPSPKPTSSCPSIPNSKRIPNTNFIVDLFRLPHQSSSVAFFLSHFHSDHYSGLSSSWSKGIIYCSHKTARLVAEILQVPSQFVFALPMNQMVKIDGSEVVLIEANHCPGAVQFLFKVKLESSGFEKYVHTGDFRFCDEMRFDPFLNGFVGCDGVFLDTTYCNPKFVFPSQEESVGYVVSVIDKISEEKVLFLVATYVVGKEKILVEIARRCKRKIVVDARKMSMLSVLGCGEEGMFTEDENESDVHVVGWNVLGETWPYFRPNFVKMNEIMVEKGYDKVVGFVPTGWTYEVKRNKFAVRFKDSMEIHLVPYSEHSNYDELREFIKFLKPKRVIPTVGVDIEKFDCKEVNKMQKHFSGLVDEMANKKDFLLGFYRQSYQKNEKSDVDVVSHSAEVYEEEEKNACEDGGENVPSSRGPILHDTTPSSDSRLLIKLRDSLPAWVTEEQMLDLIKKHAGNPVDIVSNFYEYEAELYKQASLPTPSLNNQAVLFDDDVTDLQPNPVKGICPDVQAIQKGFDLPRKMNLTKGTISPGKRGKSSGSKSNKKAKKDPKSKPVGPGQPTLFKFFNKVLDGGSNSVSVGSETEECNTDKKMVHIDASEAYKEVTDQFIDIVNGSESLRDYAASIIDEAKGDISRALNIYYSKPREIPGDHAGERGLSSKTIQYPKCSEACSSQEDKKASENSGHAVNICVQTSAEESVDKNYVSLPPEKYQPKEHACWREGQPAPYIHLVRTFASVESEKGKIKAMSMLCNMFRSLFALSPEDVLPAVYLCTNKIAADHENIELNIGGSLISSALEEACGISRSTVRDMYNSLGDLGDVAQLCRQTQKLLVPPPPLLVRDVFSTLRKISVQTGTGSTRLKKNLIVKLMRSCREKEIKFLVRTLARNLRIGAMLRTVLPALGRAIVMNSFWNDHNKELSESCFREKLEGVSAAVVEAYNILPSLDVVVPSLMDKDIEFSTSTLSMVPGIPIKPMLAKIAKGVQEFFNLSQEKAFTCEYKYDGQRAQIHKLLDGTVCIFSRNGDETTSRFPDLVDVIKQFSCPAAETFMLDAEVVATDRINGNKLMSFQELSTRERGSKDALITTESIKVEVCVFVFDIMFVNGEQLLALPLRERRRRLKEVFPETRPGYLEYAKEITVGAEEASLNNHDTLSRINAFLEEAFQSSCEGIMVKSLDVNAGYCPTKRSDSWLKVKRDYVDGLGDTLDLVPIGAWYGNGRKAGWYSPFLMACFNPETEEFQSVCRVMSGFSDAFYIEMKEFYSEDKILAKKPPYYRTGETPDMWFSAEVVWEIRGADFTVSPVHSASLGLVHPSRGISVRFPRFISKVTDRNPEECSTATDIAEMFHAQTRKMNITSQH