wanglab/gogpt-training-data huggingface dataset:
Protein: General transcription and DNA repair factor IIH helicase subunit XPD (TFIIH subunit XPD) (EC 5.6.2.3) (CXPD) (DNA 5'-3' helicase XPD) (DNA excision repair protein ERCC-2) (DNA repair protein complementing XP-D cells) (Xeroderma pigmentosum group D-complementing protein) (O08811)
Organism: Mus musculus (Mouse)
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/ERCC2 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/ERCC2 acts by forming a bridge between CAK and the core-TFIIH complex. Involved in the regulation of vitamin-D receptor activity. As part of the mitotic spindle-associated MMXD complex it plays a role in chromosome segregation. Might have a role in aging process and could play a causative role in the generation of skin cancers.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P18074}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P18074}.
Interaction partners:
- General transcription factor IIH subunit 4
- General transcription factor IIH subunit 1
- General transcription factor IIH subunit 2
- General transcription factor IIH subunit 3
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- CDK-activating kinase assembly factor MAT1
- Cyclin-H
- Cyclin-dependent kinase 7
- General transcription factor IIE subunit 1
- General transcription factor IIE subunit 2
Sequence:
MKLNVDGLLVYFPYDYIYPEQFSYMLELKRTLDAKGHGVLEMPSGTGKTVSLLALIVAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLSFYEQQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQQDASLPHCRFYEEFDIHGRQMPLPAGIYNLDDLKALGQRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQSNLDTLQKTVLRIKETDEQRLRDEYRRLVEGLREASVARETDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSGLAQRVCIQRKPLRFCAERLRSLLHTLEIADLADFSPLTLLANFATLVSTYAKGFTIIIEPFDDRTPTIANPVLHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMATFTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFTSYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVARGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHAAQCVGRAIRGKTDYGLMVFADKRFARADKRGKLPRWIQEHLTDSNLNLTVDEGVQVAKYFLRQMAQPFHREDQLGLSLLSLEQLQSEETLQRIEQIAQQL
Protein: [histone H3]-trimethyl-L-lysine(9) demethylase (EC 1.14.11.66) (A0A0G2JXG2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSEDHSAQNPSCKIMTFRPTMDEFRDFNRYVAYIESQGAHRAGLAKIIPPKEWKPRQTYDDIDDVVIPAPIQQVVTGQSGLFTQYNIQKKAMTVGEYRRLANSEKYCTPRHQDFDDLERKYWKNLTFVSPIYGADISGSLYDDDVAQWNIGNLRSILDMVERECGTIIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAIGFFPGSSQGCDAFLRHKMTLISPIILKKYGIPFSRITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATLRWIDYGKVATQCTCRKDMVKISMDVFVRILQPERYEQWKQGRDLTVLDHTRPTALSSPELSSWSASRTSLKAKLLRRQISVKESRPWRKAEEERRREPTRRPGPASHRRRSQPKKSKPEDSRSPGEATAGVAGLDEARGCSRRETMPEEEEEEELSPSQGHEAEGVEEDGRGKPRPTKARSKKKTPSLLSPPLLSAPPALFPAEEVLRLPPQPKSPGPAMGPMAAEGGPPPTALNVVPPGVPGEETEVRPRPIIPMLYVLPRANSSDGDREHAAHPQLAPMELGPEEEDQAQAGDSQGTTSFSKLKVEIKKSRRHPLGRPPTRSPLSVVKQEASSDEEAFPFSGEDDGSDPEALRSLLSLQWKSKAASFQAERKLNAAAALSEPYCAVCTLFYPYSQSVQTERDSAVQPPSKSGQRTRPLIPEMCFTSSGENTEPLPANSYVGEDGTSPLISCAHCCLQVHASCYGVRPELAKEGWTCSRCAAHAWTAECCLCNLRGGALQRTTEHRWIHVICAIAVPEVRFLNVIERNPVDVSAIPEQRWKLKCVYCRKRMKRVSGACIQCSYEHCSTSFHVTCAHAAGVLMEPDDWPYVVSITCLKHRASGAGGQLLRTVSLGQIVITKNRNGLYYRCRVIGTTAQTFYEVNFDDGSYSDNLYPESITSRDCLRLGPPPEGELVELRWTDGNLYRARFISMATSLIYQVEFEDGSQLTVKRADIFTLEEELPKRVRSRLSLSTGTPQEPSFSGDGVKAAKRPRVATVLATTTEDTGRSPEYLAFMESLLQAQGQPGAPF
Protein: PvdG (Q9I156)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PvdL
- Probable non-ribosomal peptide synthetase
- Pyoverdine synthetase D
- Probable non-ribosomal peptide synthetase
- PvdJ
- Acyl-homoserine lactone acylase PvdQ
- Pyoverdine biosynthesis protein PvdE
- L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase, PvdH
- MbtH-like domain-containing protein
- Pyochelin synthetase PchE
Sequence:
MSPAVSLQLFCLPYSGASARLFRRWQPSLPGWIRLLPLELPGRGLRFGEALHTDAASLVAQLAGELQGTLDSASPYAFFGHSLGGLLAFELAHAMRRRGLEGPLALFLSGVSPPAENDVSGYRRAKADAELVAALRDYRGTPEAVLNDPSLMQMLLPVVRADFLVTGSYRYQAHGPLDAALHLFGGREDSLRSAELLGWLHEAGGDFTLDLLDGQHFFIREQQGQLLRLLRRYAGQHLLRWHKDKVRGSMRAAS
Protein: Chromosome associated protein H2, isoform F (Q9VGX5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MERILPEEAEAAYLSEAREQILEIAKNRPGTQVAKCIRAYDEQQDLASLVVLLEELSKNTDYSTDLRISLGYYIEELLRHCLGRNDVSRRSAIVAAGSALQYCGKIYGDRVEYLCQVVEHQIEALLTSELQKETPSGSAAPEKNERRPEETRKRHPKKLTNKEVDPYLLTLEPKRFKTMSDDKRFNAAGFVKCTRNRTIEYLYQDHTPPNLWKHAPIVDPHNPYDQDEKKQYKMFTYHVEHRYNTLLPDIPFERLNLIKEYVHTNQVNTTEILNEHMTTKEYLDEYIALENQMLAARYGAIVTRRRRLVDSARFMEDNLDEGLAKKMCMDKNLPMDTNETVLIDQSLVDENSRSLTTAESTMGISQAENSTLKSSEVEATLSVSHIENSLSDSQEENPPLSSTLAINESSVLDSTRVDPIKDLTLDELLLIDSGISMEELSDIQMHTDLEDQRQLSPMLQMVSPSMEAKTLNIIEMDADLIMNVPREVSYPILLNVMGLPIKRLRRKCIFKLPPEFDLFRQARLPIKREGQQKSPTTPRTVLQIGREAPQNEREPGSPCSLEFDEDLNFLGFRQRRPTFDSGFDIEEPRVSSCVSTIGEVKTELEDEIEANTNNLTDASASDALNENVNDTKESGLGDSLAQELNASTEPNAENNTANSSQLEVTATESSGTLSGLETTVDLGMESALVSSVLDLSTEPSAMDSNIINVTQPDNSDLEISTVQDQDTLHDEADANDLSAETPNPIADSAVDDCSLIRDWHRRLAPALEAAHERQNFNIKDLGTEILDICKAGNRTATLADVMADKDPSIMCRYMLASLVLTNHGNVSLDFENRDKSKPIDMSQFRMHLKSMKRMEINPEDDVGNINAAQSKSTPRSKQLNDSAHKPRTSTTASAPTKRKSAENSLSEVFAKTVRLIQPIPKMWPTPSDADSGISSMGSSLASTARLK
Protein: MICOS complex subunit MIC25 (Coiled-coil-helix cristae morphology protein 1) (Coiled-coil-helix-coiled-coil-helix domain-containing protein 6) (Q9BRQ6)
Organism: Homo sapiens (Human)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:22228767}; Lipid-anchor {ECO:0000305|PubMed:22228767}. Mitochondrion {ECO:0000269|PubMed:25781180, ECO:0000269|PubMed:25997101}.
Interaction partners:
- MICOS complex subunit MIC60
- MICOS complex subunit MIC27
- MICOS complex subunit MIC19
- MICOS complex subunit MIC26
- MICOS complex subunit MIC13
- MICOS complex subunit MIC10
- Metaxin-2
- Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial
- Sorting and assembly machinery component 50 homolog
- Metaxin-1
Sequence:
MGSTESSEGRRVSFGVDEEERVRVLQGVRLSENVVNRMKEPSSPPPAPTSSTFGLQDGNLRAPHKESTLPRSGSSGGQQPSGMKEGVKRYEQEHAAIQDKLFQVAKREREAATKHSKASLPTGEGSISHEEQKSVRLARELESREAELRRRDTFYKEQLERIERKNAEMYKLSSEQFHEAASKMESTIKPRRVEPVCSGLQAQILHCYRDRPHEVLLCSDLVKAYQRCVSAAHKG
Protein: Uncharacterized protein (Q582V1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEKNAHGLLADADSPKAHRHIRNTLKVNKLSSALMFMAVVTPVMVLVSFYSAKLEAVREKWVDPYELPPGFNPKTGRFMSDSKPQGVTEPPAPLLLRGAVPGATRQ
Protein: XRCC1 N-terminal domain containing 1, N-terminal like (E9PJ82)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPVKISHVVSFSSQDPKYPVENLLNPDSPRRPWLGCPQDKSGQLKVELQLERAVPTGYIDVGNCGCAFLQIDVGHSSWPLDRPFITL
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Cyclophilin) (Cyp) (Cyclosporin A-binding protein) (Rotamase) (allergen Cat r 1) (Q39613)
Organism: Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Function: PPIases accelerate the folding of proteins (By similarity). It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24939849}.
Interaction partners:
Sequence:
MPNPRVFFDMSVGGQPAGRIVMELFADTTPRTAENFRALCTGEKGTGRSGKPLHYKDSSFHRVIPGFMCQGGDFTAGNGTGGESIYGAKFADENFIKKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGQVVEGMDVVKAIEKVGSSSGRTAKKVVVEDCGQLS
Protein: Copper-containing nitrite reductase (EC 1.7.2.1) (Q9JYE1)
Organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)
Function: Catalyzes the reduction of nitrite to nitric oxide (NO). It could be essential for growth and survival in oxygen-depleted environments.
Subcellular location: Cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Nitric oxide reductase
- Cytochrome
- Uncharacterized protein
- Sulfatase-modifying factor enzyme-like domain-containing protein
Sequence:
MKRQALAAMIASLFALAACGGEPAAQAPAETPAAAAEAASSAAQTAAETPSGELPVIDAVTTHAPEVPPAIDRDYPAKVRVKMETVEKTMTMEDGVEYRYWTFDGDVPGRMIRVREGDTVEVEFSNNPSSTVPHNVDFHAATGQGGGAAATFTAPGRTSTFSFKALQPGLYIYHCAVAPVGMHIANGMYGLILVEPKEGLPKVDKEFYIVQGDFYTKGKKGAQGLQPFDMDKAVAEQPEYVVFNGHVGAIAGDNALKAKAGETVRMYVGNGGPNLVSSFHVIGEIFDKVYVEGGKLINENVQSTIVPAGGSAIVEFKVDIPGSYTLVDHSIFRAFNKGALGQLKVEGAENPEIMTQKLSDTAYAGNGAAPAASAPAASAPAASASEKSVY
Protein: Nebulin (A2AQB2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MTSSVEPICIKIKILKSLKEKYKYIICLFLCCFFFFNHNFSTNTKKVTESSWATTWVSAACKMTPSWYGLYMLLRSRVTENTRKPMRSRKNVYKSDLEWMKGIGWLTEGSVEVMRVKNAQNLLNERLYRIRPEAYKFTSIVDTPEVILAKTNALQISEPLYRDAWDKEKANVNVPADIPVMLQSKLNAIQISNKHYQKAWEDVKMTGYDIRADAIGIQHAKASRDIASDYLYKTAYEKQKGHYIGCPSAKEDPKLVWAANVLKMQNDRLYKKAYNDHKAKISIPVDMVSINAAKEGQALASNVDYRQYLHQWSCFPDQNDVIQARKAYDLQSDAIYKADLEWLRGIGWMPEGSPEVLRVKNAQEILCDSVYRTPVVKLKYTSIVDTPEVVLAKSNAENISIPKYREVWDKDKTSIHIMPDTPEINLARANALNVSNKLYREGWDEVKMSCDVRLDAIPIQAAKASREIASDYKYKLDHEKQKGHYVGTLTARDDNKIRWALIAGKIQNEREYRLQWAKWKTKFQSPVDMLSILHSKKCQTLVSDIDYRNYLHEWTCMPDQNDVIQAKKAYELQSDAVYKADLEWLRGIGWMPNDSVSVNHAKHAADIFSEKKYRTKIETLNFTPVDDRVDYVTAKQSSEIRDDIKYRKDWNAIKSKYTLTETPLLHTAQEAARILDQYLYKEGWEKQKATGYILPPDAVPFVHAHHSSDVQSELKYKAEHVKQRGHYVGVPTMRDDPKLVWFEHAGQIQNDRLYKESYHKSKAKINIPADMVSVVAAKEGQNLVSDIDYRQYLHQWTCHPDQNDVIQAKIAYDLQSDNVYKADLEWLRGIGWIPLDSVDHVRVTKNQEMVNQIKYKKDALANYPNFTSVEDPPEIVLAKINSVNQSDVKYKETFNKAKGKYIFSPDTPYISHSKDMGKLYSTILYKGAWEGTKAYGYTLDERYIPIVGAKHADLVNSELKYKETYEKQKGHYLAGKEISEFPGVVHCLDFQQMRSALNYRRDYEDTKANVHIPNDMMNHVLAKRCQYILSDLEYRHYFHQWTSLPEEPNVIRARNAQEILSDNVYKDDLNWLKGIGCYVWDTPQILHAKKSYDLQSQLQYTAASKENLQNYNLVTDTPVYVTALQSGINASEVKYKENYHQIKDKYTTVLETADYDRTKHLKSLYSSNIYKEAWDKVKATSYNLPTSTLSLTHAKNQKHLASHIKYREEYEKFKALYTLPKSVDDDPNTARCLRVGKLNIDRLYRSVYEKNKMKINIVPDMVEMVTAKDSQKKVSEIDYRLHLHEWICHPDLQVNSHVRKVTDQISDIVYKDDLTWLKGIGCYVWDTPEILHAKHAYDLRNDIKYKAHVQKTRNDYKLVTDTPVYVQAVKSGKQLSDAVYHYDYVHSVRGKVAPTTKTVDLDRALHAYKLQSENLYKKGLRFLPTGYRLPVDTPHFNHTKDTRYMSSYFKYKEAYEHIKANGYTLGPKDVPFVHVRRVNNVTSERLYRELYHKLKDKIHTTPDTPEIRQVKKTQEAVSELIYKSDFFKMQGHMISLPYTPQVLHCRYVGDITSDIKYKEDLQILKGLGCFLYDTPDMVRSRHLRKLWSNYLYTDNARKMRDKYKVVLDTPEYRKVQELKTHLSELVYRASGKKQKSIFTSVPDTPDLLRAKRGQKLQSQYLYVELATKERPHHHAGNQTTALQHAKDVKDMVSEKKYKIQYEKMKDKYTPVADTPILIRAKRAYWNASDLRYKETFQKTKGRYHTVKDALDIVYHRKVTDDISKVKYKENYMSQLGIWSSIPDRPEHFHHRAVTDAVSDVKYKEDLTWLKGIGCYAYDTPDLTLAEQNKTLYSKYKYKEVFERTKSNFKYVADCPINRHFKYATQLMNEKKYRADYEQRKDKYHLVVDEPRHLLAKTAGDQISQIKYRKKYEKSKDKFTSVVDTPEHLRTTKVNKQISDILYKLEYNKARPRGYTTIHDTPMLLHVRKVKDEVSDLKYKEVYQRNKSNCTIKPDAVHIKAAKDAYKVNTNLDYKKQYEANKAYWKWTPDRPDFIQAAKSSLQQSDFEYKLDREFLKGCKLSVTDDKDMVLALRNSLIESDLKYKEKHVKERGSCHAVPDTPQILLAKTVSNLVSENKYKDHVKKHLAQGSYTTLPETRDTVHVKAVTKHVSDTNYKKKFVKEKGKSNYSIMQEPPEVKHAMEVAKKQSDVAYKKDAKENLHYTTVADRPDIKKATQAAKQASEVEYRAKHRKEGSHGLSMLGRPDIEMAKKAAKLSSQVKYRENFDKEKGKTPKYNPKDSQLYKTMKDANNLASEVKYKADLKKLHKPVTDMKESLIMHHVLNTSQLASSYQYKKNYEKSKGHYHTIPDNLEQLHHREATELQSIVKYKEKYEKERGKPMLDFETPTYITAKESQQMQSGKEYRKDYEESIKGRNLTGLEVTPALLHVRHATKIASEKEYRKDLEESIRGRGLTEMEDTPDMLRAKNATQILNEKEYKRDLELEVKGRGLNAMANETPDFMRARNATDIASQIKYKQSAEMEKANFTSVVDTPEIIHAQQVKNLSSQKKYKEDAEKSMSYYETVLDTPEMQRVRENQKNFSLLQYQCDLKNSKGKITVVQDTPEILRVKENQKNFSSVLYKEDVSPGTAIGKTPEMLRVKQTQDHISSVKYKEAIGQGTPIPDLPEVKRVKETQKHISSVMYKENPGTGIPTTVTPEIERVKRNQENFSSVLYKESLGKGTPTAITPEMERVKRNQENFSSILYKENLSKGTPLPVTPEMERAKRNQENFSSVLYSDSFRKQIQGKAAYVLDTPEMRRVRETQRHISTVKYHEDFEKHKGCFTPVVTDPITERVKKNTQDFSDINYRGIQRKVVEMEQKRNDQDQDTITGLRVWRTNPGSVFDYDPAEDNIQSRSLHMINVQAQRRSRDQSRSASALSISGGEEKSEHSEAADQRLSTYSDGGAFFSATSTAYKHVKTTQLPQQRSSSVATQQTTLSSIPSHPSTAGKIFRAIYDYIAADADEVSFKDGDAIVNAQAIDEGWMYGTVQRTGRTGMLPANYVEAI
Protein: Type 1 encapsulin shell protein (Culture filtrate protein 29) (CFP29) [Cleaved into: Type 1 encapsulin shell protein, N-terminally processed] (I6WZG6)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Shell component of a type 1 encapsulin nanocompartment in situ; its cargo protects against oxidative stress at low pH. In situ and in E.coli assembles into proteinaceous shells about 22 nm in diameter with 2.5 nm thick walls. Cargo proteins are targeted to the interior via their C-terminal extensions; empty intact shells can be isolated in E.coli in the absence of cargo protein. There are at least 4 possible cargo proteins, DyP (encoded in the same locus), FolB, BfrB and Rv1762c; DyP and Rv1762c have been identified in vivo. Probably involved in protection against oxidative damage from the host immune response (Probable). A T-cell antigen found in bacterial culture cell filtrates, stimulates mouse immune response. Does not have detectable bacteriocin activity.
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:24855650}. Secreted {ECO:0000269|PubMed:9596740}. Cell membrane {ECO:0000269|PubMed:9596740}; Peripheral membrane protein {ECO:0000269|PubMed:9596740}. Note=Encapsulin microcompartments of this protein encapsulating DyP are found in situ (PubMed:34751132). Detected at low levels in short-term culture filtrate, the nanocompartment is very stable and may survive cell lysis, explaining its apparent secretion (Probable) (PubMed:9596740). Detected in infected host (mouse J774 cell line) exosomes (PubMed:20662102). {ECO:0000269|PubMed:20662102, ECO:0000269|PubMed:34751132, ECO:0000269|PubMed:9596740, ECO:0000305|PubMed:34751132}.
Interaction partners:
- Dye-decolorizing peroxidase
- Probable M18 family aminopeptidase 2
Sequence:
MNNLYRDLAPVTEAAWAEIELEAARTFKRHIAGRRVVDVSDPGGPVTAAVSTGRLIDVKAPTNGVIAHLRASKPLVRLRVPFTLSRNEIDDVERGSKDSDWEPVKEAAKKLAFVEDRTIFEGYSAASIEGIRSASSNPALTLPEDPREIPDVISQALSELRLAGVDGPYSVLLSADVYTKVSETSDHGYPIREHLNRLVDGDIIWAPAIDGAFVLTTRGGDFDLQLGTDVAIGYASHDTDTVRLYLQETLTFLCYTAEASVALSH
Protein: RING finger family protein (RING/U-box superfamily protein) (Q84WW4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pentatricopeptide repeat-containing protein At5g25630
- Acyl-CoA-binding domain-containing protein 5
- Acyl-CoA-binding domain-containing protein 4
- Acyl-CoA-binding domain-containing protein 1
Sequence:
MGLGNKGNKFNFGDNDLADEASGADGDEGDGFGSVACSICLETVVKNGDRAWANLQCDHQFHLDCIGSAFNAKGVMQCPNCRKVEKGQWLYANGCRSYPEFNVEDWVHEEDIYDIGAYSEMSFGVHWCPFGSSARLPSFEDGEFSPSSYHDLLGQQGYYTEPAAPTAGHPCPYVTYFGPVHSPSSSSGGAAGVSDSSSFSSHWNTGSSVSGEVPTPYGFPVDPHYHGWDYHPPPPPPPQHFSASGAHVGSPTQPTPPPAAARTSRANGSDMIRPRPPHFTRPFHGHSSSGRAGSSVASVPRTPPFPGSNARTRDRMQALQAYYQQSSAQSHQPDSPIVSRGPVFPSGRRPARGIASGMGSTSSSSDQAGGSGFIRFNIWERDPYMQSQQAYSVNQMDREPNIWTSSFNEGSGSFHQRHGGGGGSS
Protein: Anion exchange protein (Q8MQK6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
Sequence:
FCGDKVMAEKNEYIELPWTMNSSSGDDEAPKDPRTGGEDFTQQFTENDFEVTPPAQRVQFILGEDVDDGTHVSHPLFSEMGMLVKEGDEIEWKETARWIKFEEDVEEGGNRWSKPHVATLSLHSLFELRRLLVNGSVMLDMEAQNLEVMADLVCDHMVSAGTLPPGVKDKVKDALLRRHRHQHEYAKKTRLPIIRSLADMRNHSSSKKKKSNSKHSRPAQNLSSITEDMVKSPSNQSMARPGSGTELSEQQHKGNTHFMRKIPPGAEASNILVGEVDFLERTLSCFIRLSQAVVLGDLTEVPVPTRFVFILLGPPGSQSNFHEIGRAMATLMSDEIFHEVAYRARKRDHLLSGVDEFLDAVTVLPPGEWDPTIRIEPPAAIPSQEVRKRPPELPKEEVDEEEEEARLREENGLSRTGRLFGGLINDIKRKAPWYISDYKDALSMQCVASWIFLYFACLSPIITFGGLLAEATGKHMAAMESLVSGFVCGMGYGFFSGQPLTILGSTGPVLVFESIIYEFCLKMGWDYMTFRFWIGMWVAGICIVLTAIDASALVCYITRFTEENFATLIAFIFIYKAIENVMVIGKNFPVNQGIYDCVCTPPIGSNASVIDYAKYNWDSCESYNGTLVGGDCGTPPTENVFLMSVVLCAGTFLISTVLKEFKNALFFPSIVRQYISDFSVLIAIFAMSFFDYSLGVPTQKLEVPNELKPTLSTRGWLIPPFVEKNPWWSAIIAVFPALLGTILIFMDQQITAVIVNRKENKLKKGCGYHLDLFILSILIAICSMMGLPWFVAATVLSINHVNSLKLESECSAPGEKPQFLGVREQRVTHILIFLTIGVSVLLTPLLGNIPMPVLFGVFLYMGVASLKGLQFFDRILIMFMPAKYQPDYMFLRQVPIKRVHLFTMIQLACLIILWLIKSFSQTSILFPLMLVVMIGIRKALDLVFTRRELKILDDIMPEMTKRAAADDLHKLDAEVGLLARIFPWGKGSRSRVVTKPPGLDDGIVGSGGAVGAGLITCTTSNANEKEFEAQSSLLKK
Protein: Peptidase T (EC 3.4.11.4) (Aminotripeptidase) (Tripeptidase) (L6PepTR) (Tripeptide aminopeptidase) (Q76HM7)
Organism: Lactococcus lactis subsp. cremoris (Streptococcus cremoris)
Function: Cleaves the N-terminal amino acid of tripeptides.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00550}.
Interaction partners:
Sequence:
MKYEKLLPRFLEYVKVNTRSDENSTTTPSTQALVEFAHKMGEDMKALGLKDVHYLESNGYVIGTIPANTDKKVRKIGLLAHLDTADFNAEGVNPQILENYDGESVIQLGDTEFTLDPKDFPNLKNYKGQTLVHTDGTTLLGSDDKSGVAEIMTLADYLLNINPDFEHGEIRVGFGPDEEIGVGADKFDVADFDVDFAYTVDGGPLGELQYETFSAAGAVIEFQGKNVHPGTAKNMMVNALQLAIDYHNALPEFDRPEKTEGREGFFHLLKLDGTPEEARAQYIIRDHEEGKFNERKALMQEIADKMNAELGQNRVKPVIKDQYYNMAQIIEKDMSIIDIAKKAMENLDIAPIIEPIRGGTDGSKISFMGLPTPNLFAGGENMHGRFEFVSVQTMEKAVDTLLEIIRLNNEVAK
Protein: Uncharacterized protein C20orf141 (Q9NUB4)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTRLCLPRPEAREDPIPVPPRGLGAGEGSGSPVRPPVSTWGPSWAQLLDSVLWLGALGLTIQAVFSTTGPALLLLLVSFLTFDLLHRPAGHTLPQRKLLTRGQSQGAGEGPGQQEALLLQMGTVSGQLSLQDALLLLLMGLGPLLRACGMPLTLLGLAFCLHPWA
Protein: Dynein, axonemal, heavy chain 3, isoform E (IP15220p) (Q1LZ38)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQKKVAPERRPYCDPRLQDDKLRRKRTLHLPRVSQAQKKGEKRQLNDCPFYNLTYGFDQLPLDPVKEFLQEKISHMQTDKIVGHCNREFDFHRYDLDNVKDEYDECDDDSLQELQLEDIIMPEQFEMLRDAKDHLYNFDSTACNQFPWIDKWMTGVRPSEQEIYEMTSHLLEIYCNRRVRIFYPGCGTSSSLWTNQLRRQHGSPSELIGAYRTPSARHMRVNNMRGPPKKEKFTAGDHYAFRTPQECRNELMRVGKIIDELIEPVLKAAEHKIGHGLTKYPDPPSCKDNTNRILRSAGILVGKKKNCYVGKCRIHRKDFATNEEFLRCLKRMEATHFPYMQPLQPVDPDDQKIKMLAKYRVELARAEKLFTLKIQKRYQCLLKSVSYDER
Protein: Dro2 protein (Q2UYB4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVQIKFLFFFLAVMTIVVLAANMADADCLSGKYKGPCAVWDNEMCRRICKEEGHISGHCSPSLKCWCEGC
Protein: Malto-oligosyltrehalose trehalohydrolase (MTHase) (EC 3.2.1.141) (4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase) (Maltooligosyl trehalose trehalohydrolase) (P9WQ23)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Is involved in the biosynthesis of trehalose but not in that of capsular glucan and glycogen.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Putative maltooligosyl trehalose synthase
- Trehalose-phosphate phosphatase
- Uncharacterized glycosyl hydrolase Rv2006
- Glycogen operon protein GlgX homolog
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- Trehalose synthase/amylase TreS
- Alpha-maltose-1-phosphate synthase
- Glucose-1-phosphate adenylyltransferase
- Trehalase
- Maltokinase
Sequence:
MPEFRVWAPKPALVRLDVNGAVHAMTRSADGWWHTTVAAPADARYGYLLDDDPTVLPDPRSARQPDGVHARSQRWEPPGQFGAARTDTGWPGRSVEGAVIYELHIGTFTTAGTFDAAIEKLDYLVDLGIDFVELMPVNSFAGTRGWGYDGVLWYSVHEPYGGPDGLVRFIDACHARRLGVLIDAVFNHLGPSGNYLPRFGPYLSSASNPWGDGINIAGADSDEVRHYIIDCALRWMRDFHADGLRLDAVHALVDTTAVHVLEELANATRWLSGQLGRPLSLIAETDRNDPRLITRPSHGGYGITAQWNDDIHHAIHTAVSGERQGYYADFGSLATLAYTLRNGYFHAGTYSSFRRRRHGRALDTSAIPATRLLAYTCTHDQVGNRALGDRPSQYLTGGQLAIKAALTLGSPYTAMLFMGEEWGASSPFQFFCSHPEPELAHSTVAGRKEEFAEHGWAADDIPDPQDPQTFQRCKLNWAEAGSGEHARLHRFYRDLIALRHNEADLADPWLDHLMVDYDEQQRWVVMRRGQLMIACNLGAEPTCVPVSGELVLAWESPIIGDNSTELAAYSLAILRAAEPA
Protein: Pfmc-2TM Maurer's cleft two transmembrane protein (B9ZSH7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MFHYIYKIYIFTIILCASNLFNNNGVENGTYKLSYHNGGIQFRMLAQKNTNKKSNGNALKNILLKDKSKKGSKKKNPDAEISDLVNLVDNMNITQEKKDKIKNLSLKYINSRDVKEKNESINELQKYSNNEECKEYMDSYLMHLRMQNDIKCLKRKNLWNNIWIVSTTLLLIIIMIACVYWLASTPPPGLFCLPFIVLIFIIYIVARYFPDMKIGFKKLKTKLNTFFQNKKQITK
Protein: DNA damage checkpoint control protein rad1 (P22193)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Recombinational reparation of DNA damages induced by UV and gamma radiation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Checkpoint protein hus1
- Checkpoint protein rad17
- DNA repair protein rad9
- Replication factor C subunit 2
- DNA repair protein crb2
- Protein kinase rad3
- Replication factor C subunit 3
- Replication factor C subunit 4
- Serine/threonine-protein kinase cds1
- Serine/threonine-protein kinase chk1
Sequence:
MFQAETVCLKQIQSTLRCIDFSKECTIEITSRGLRFAVEESQSLQAHAFLDKSLFQTFNFQGDSDGDTYMFQTMISPLLQSLSIYTDGKERISTSAWDQPTVNIMHKRGVICKVQYNGPGCPFIWEVEEMAGYATACELLTMECEDDVDINRLASTLCTKIIMKSNWLYDALVELDNNMGENLIIHTSSQKSTFLLRCVGALSTTEIEYPNEKSVLESFETDSENTYSYRFSLIRHALKALQVGSKVNLRIDENGTLSIQIMLVGQEGLCTFVDFCIVPLDLVSEDEEEDEEEEPAESNQSDNNVLRNDPNYRGDAETEDEDS
Protein: Calsequestrin-2 (Calsequestrin, cardiac muscle isoform) (O09161)
Organism: Mus musculus (Mouse)
Function: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:19920148}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. {ECO:0000269|PubMed:16932808, ECO:0000269|PubMed:19920148}.
Interaction partners:
- Triadin
- Aspartyl/asparaginyl beta-hydroxylase
- Ryanodine receptor 2
- Ryanodine receptor 1
- Ryanodine receptor 3
- Junctophilin-1
- Junctophilin-3
- Calsequestrin-1
- Junctophilin-2
- Voltage-dependent L-type calcium channel subunit alpha-1C
Sequence:
MKRIYLLMVGVYLLSLSGAEEGLNFPTYDGKDRVVSLSEKNLKQMLKRYDLLCLYYHEPVSSDKVSQKQFQLKEIVLELVAQVLEHKNIGFVMVDSRKEAKLAKRLGFSEEGSLYVLKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIVNNKLEVQAFERIEDQTKLLGFFKNEDSEYYKAFQEAAEHFQPYIKFFATFDKAVAKKLSLKMNEVGFYEPFMDEPNVIPNKPYTEEELVEFVKEHQRPTLRRLRPEDMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFKPQIGVVNVTDADSIWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDNEDEDDDGDDNDDDDDDDDDNDNSDEDNEDSDDDDDDDE
Protein: Squalene synthase 8 (PgSS8) (SQS 8) (EC 2.5.1.21) (FPP:FPP farnesyltransferase SS8) (Farnesyl-diphosphate farnesyltransferase SS8) (A0A1P7Y0C9)
Organism: Panax ginseng (Korean ginseng)
Function: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways. Catalyzes the biosynthesis of squalene (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P53799}.
Interaction partners:
Sequence:
MGSLGAILKHPDDFYPLLKLKIAARHAEKQIPSEPHWAFCYSMLHKVSRSFGLVIQQLGPQLRDAVCIFYLVLRALDTVEDDTSISTEVKVPIVMAFHCHIYDNDWHFSCGTKEYKVLMDEFHHVSNAFLDLGSSYKEAIEDITMRMGAGMAKFICKEVETIDDYDEYCHYVAGLVGLGLSKLFHASGAEDLATDSLSNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRQIWSKYVDKLEDLKYEENSAKAVQCLNDMVTDALVHAEDCLKYMSDLRGPAIFRFCAIPQIMAIGTLALCFNNTQVFRGVVKMRRGLTAKVIDQTKTMSDVYGAFFDFSCLLKSKVDNNDPNATKTLSRLEAIQKTCKESGTLSKRFCVFDFPLETIFYRV