wanglab/gogpt-training-data huggingface dataset:
Protein: General transcription and DNA repair factor IIH helicase/translocase subunit XPB (TFIIH subunit XPB) (EC 5.6.2.4) (ATP-dependent DNA helicase hay) (DNA 3'-5' helicase/translocase XPB) (DNA excision repair protein haywire) (ERCC-3 homolog protein) (ERCC3Dm) (Q02870)
Organism: Drosophila melanogaster (Fruit fly)
Function: ATP-dependent 3'-5' 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 ATPase activity of haywire/XPB/ERCC3, but not its helicase activity, 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. The ATP-dependent helicase activity of haywire/XPB/ERCC3 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.
Subcellular location: Nucleus.
Interaction partners:
- General transcription and DNA repair factor IIH helicase subunit XPD
- CDK-activating kinase assembly factor MAT1
- General transcription factor IIH subunit 4
- General transcription factor IIH subunit 1
- General transcription factor IIH subunit
- General transcription factor IIH subunit 3
- Cyclin-H
- General transcription factor IIE subunit 1
- Transcription initiation factor IIE subunit beta
- General transcription and DNA repair factor IIH subunit TFB5
Sequence:
MGPPKKSRKDRSGGDKFGKKRRAEDEAFTQLVDDNDSLDATESEGIPGAASKNAETNDEQINTDEYGAKDYRSQMQLRPDHGNRPLWVAPNGHVFLESFSPVYKHAHDFLIAISEPVCRPEHIHEYKLTAYSLYAAVSVGLQTHDIVEYLKRLSKTSIPEGILEFIRLCTLSYGKVKLVLKHNKYFIESPHPEVLQKLLKDPVIQKCRLIRSEGEDFIQGTLDGKAITQFGTKLPPGATDKPTPDPAAAAGADGTTAVPEDITDFYEKIDKEEEDEDEANLKTVSFEVAQEKIEVIQKRCIEIEHPLLAEYDFRNDTNNPDINIDLKPAAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLVGVTACCTVRKRALVLCNSGVSVEQWKQQFKMWSTADDSMICRFTSEAKDKPMGCGILVTTYSMITHTQKRSWEAEQTMRWLQEQEWGIMVLDEVHTIPAKMFRRVLTIVQSHCKLGLTATLLREDDKIADLNFLIGPKLYEANWLELQKKGYIARVQCAEVWCPMSPEFYREYLTTKTSKKMLLYVMNPSKFRSCQFLIKYHEQRGDKTIVFSDNVFALKHYAIKMNKPFIYGPTSQNERIQILQNFKFNSKVNTIFVSKVADTSFDLPEANVLIQISSHGGSRRQEAQRLGRILRAKKGAIAEEYNAFFYTLVSQDTMEMSYSRKRQRFLVNQGYSYKVITHLKGMDTDSDLMYGTQEEQGQLLQLVLSASDLDCEDEKLPGEPGYRPSGSGGAVRRVGGLSSMSGGDDAIYYEHRKKNIGSVHPLFKKFRG
Protein: Protocadherin domain-containing protein (Q8CA35)
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:
AGDPSYEISKQRLSIVIGVVAGIMTVILIILIVMMARYCRSKNKNGYEAGKKDHEDFFTPQQHDKSKKPKKDKKNKKSKQPLYSSIVTVEASKPNGQRYDSVNEKLSDSPSMGRYRSVNGGPGSPDLARHYKSSSPLPTVQLHPQSPTAGKKHQAVQDLPPANTFVGAGDNISIGSDHCSEYSCQTSNKYSKQPFRRVTFSVVSQPQDPHQGSLQSCYDSGLEESETPSSKSSSGPRLGALPLPEDNYERTTPDGSVGEAEHMENDSRPLPDVALTGKCTRECDEYGHSDSCWMPVRTSPERKKSQPKLSTFMPVDERGSQEKLANGEAAIMGDRNRNLLNKKLTSSYETFSAASFSKNEEANPEDIPLTKTGEYKPSPVNTLTRREVYL
Protein: Uncharacterized protein, isoform D (A0A0B4LFF4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSRNRRRSFPSSQYEDKTAAAQPSGSSLRSQSLSRLDISVQNSSIYYNDTRNTRPQMVSVAVGTVSTDILNGRTSFLSLSQSHGSEVDLPSFYESFNPTFLPKLPIRRFPHMLVGASNEPEISKNQPAIPPSRPIEPISEVPFVEPAFEKKYSRTRGFSKELSTHRDNENEYIESTDEVSQMLSFTSYTDEYDRAEPLITKTQKFYKKRSPLIPKYDSEDSYVVPKETDQQESGLSFNVTTVQLADTASPESFSEYDGNRTRKQSFDMESKNSKESFDFSRGGRRLGSGMVFIYMVIPPDGGFGWVIMVLSFLAQLIIDGLIFTIGVLLPSIAQDLDVSISSVSFVASVQIGCYFTSGAFSAVLINRFGFRKVAIAGVLCSAVSILASSWSVSLTMLIFFYSVLACAGGITLSMIWASSQLIVGYYFERYRPMANGFSCSGGGAGIVLFTFLNSWLVPIIGWRNMLRTQAGLIMLILLMVVAYVEVAPTQVGMYHLPGSSDTSSDEYYGNFYVHDYLRQSAMTAKSRSILSTYEPRPKKKGCAKFCPSCSNCCWRRRKKSQNADEQNLLIRPAPLEREDLFYTGPAEYEKPHSKENVDGKEFLLMGSDKNTQQVNYGIKNIRVDDEPDRISRVHRERRWSNENQKKQNSCRNSRFMLTVLKLFDYRLLKQFEFKILVASAFLFPMGFNIPFVYSSARTTIPVEYARMIGPIIGISNLVMRNILGILAYKRRSWTLGLCGCGLIFGGVSVLISAFYGENLIWFQFLYGFSYAVAPAVYSTLRGLIYVKYLGLSKLTNAFGITSLAMGMGAFIGTTIAGKLIGITGNYSAAFCFAGLCLIVSGFLKLLLPLLIKCRNRMAQ
Protein: Phytohormone-binding protein CSBP (Cytokinin-specific binding protein) (VrCSBP) (Major pollen allergen Bet v 1-like protein) (Pathogenesis-related PR10-like protein) (allergen Vig r 6) (A0A1S3THR8)
Organism: Vigna radiata var. radiata (Mung bean) (Phaseolus aureus)
Function: Binds the cytokinin trans-zeatin in vitro. Binds gibberellin A3 (GA3) in vitro.
Interaction partners:
- Kirola
- Abscisic acid receptor PYL2
- Kirola
Sequence:
MVKEFNTQTELSVRLEALWAVLSKDFITVVPKVLPHIVKDVQLIEGDGGVGTILIFNFLPEVSPSYQREEITEFDESSHEIGLQVIEGGYLSQGLSYYKTTFKLSEIEEDKTLVNVKISYDHDSDIEEKVTPTKTSQSTLMYLRRLERYLSNGSA
Protein: Paired immunoglobulin-like type 2 receptor alpha (Cell surface receptor FDF03) (Inhibitory receptor PILR-alpha) (Q9UKJ1)
Organism: Homo sapiens (Human)
Function: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 11
- Paired immunoglobulin-like type 2 receptor beta
- CD99 antigen
- CD99 antigen-like protein 2
- Glycophorin-C
- PILR alpha-associated neural protein
- Leukocyte-associated immunoglobulin-like receptor 1
- Collectin-12
- Tumor necrosis factor receptor superfamily member 14
- Neural proliferation differentiation and control protein 1
Sequence:
MGRPLLLPLLPLLLPPAFLQPSGSTGSGPSYLYGVTQPKHLSASMGGSVEIPFSFYYPWELATAPDVRISWRRGHFHRQSFYSTRPPSIHKDYVNRLFLNWTEGQKSGFLRISNLQKQDQSVYFCRVELDTRSSGRQQWQSIEGTKLSITQAVTTTTQRPSSMTTTWRLSSTTTTTGLRVTQGKRRSDSWHISLETAVGVAVAVTVLGIMILGLICLLRWRRRKGQQRTKATTPAREPFQNTEEPYENIRNEGQNTDPKLNPKDDGIVYASLALSSSTSPRAPPSHRPLKSPQNETLYSVLKA
Protein: Homeobox protein Meis2 (Meis1-related protein 1) (O14770)
Organism: Homo sapiens (Human)
Function: Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3 is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3 and isoform 4 can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5 cannot activate DRD1 transcription.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P97367}.
Interaction partners:
- Homeobox protein Meis1
- Pre-B-cell leukemia transcription factor 1
- Pre-B-cell leukemia transcription factor 2
- Pre-B-cell leukemia transcription factor 3
- Homeobox protein Hox-B13
- Homeobox protein DLX-3
- Putative nucleotidyltransferase MAB21L1
- LIM homeobox transcription factor 1-beta
- Pre-B-cell leukemia transcription factor 4
- Protein mab-21-like 2
Sequence:
MAQRYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNHGPPLHATQHYGAHAPHPNVMPASMGSAVNDALKRDKDAIYGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPSSWRDHDDATSTHSAGTPGPSSGGHASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAGFLLDPSVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGLQSMPGDYVSQGGPMGMSMAQPSYTPPQMTPHPTQLRHGPPMHSYLPSHPHHPAMMMHGGPPTHPGMTMSAQSPTMLNSVDPNVGGQVMDIHAQ
Protein: Isochorismatase domain-containing protein 2A (P85094)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to the nucleus in the presence of CDKN2A. {ECO:0000250}.
Interaction partners:
- Izumo sperm-egg fusion protein 2
Sequence:
MAAARASLGRILPESSILFLCDLQEKFRPSIAYFPQIVSVAARMLKVARLLDVPILLTEQYPEGLGPTVPELGAQGIRPVSKTCFSMVPALQKELDGRSQLQSVLLCGIETQACILNTALDLLHRGLQVHVVVDACSSRSQVDRLVALARMRQSGAFLATSESLILQLVRDASHPQFKEIQKIIKEPVPDSGLLSLFQGQSPLTSC
Protein: At1g01225 (NC domain-containing protein-like protein) (Q29PY0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Heat shock 70 kDa protein 17
- Iron-sulfur cluster co-chaperone protein HscB homolog
- Ankyrin repeat family protein
- SH3 domain-containing protein
- Heat shock protein 90-1
- Heat shock protein 90-4
- Heat shock protein 90-5, chloroplastic
- Heat shock protein 90-3
- Heat shock protein 90-2
- Heat shock protein 90-6, mitochondrial
Sequence:
MGLLTNKIEREELKPGDHIYTYRAIFAYSHHGIFVGGSKVVHFRPEHNPMDSSTSSISSSSSEDICSIFPDCGFRQPDSGVVLSCLDCFLKNGSLYCFEYGVSPSVFLTKVRGGTCTTAQSDTTDSVIHRAMYLLQNGFGNYDIFKNNCEDFALYCKTGLLIMDKLGVGRSGQASSIVGAPLAALLSSPFKLLIPSPIGVATVTAGMYCMSRYATDIGVRSDVIKVSVEDLALNLDVKTIEQGEEEEEDEEEDSDTDYVR
Protein: MADS-box protein, GAGA2 (Q9ZS29)
Organism: Gerbera hybrida (Daisy)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSFPNDSGEMSPQRKLGRGKIEIKRIENTTNRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSSRGRLYEYANNSVKGTIDRYKKACLDPPSSGSVAEANAQFYQQEAAKLRQQIANLQNQNRQFYRNIMGESLGNMPAKDLKNLESKLEKGIGKIRSKKNEILFAEIEYMQKRENELHNSNQFLRSKIAENERAQQHMSLMPGSSDYELVAPHQPFDGRNYLQVNDLQPNNNYSCQDQTPLQLV
Protein: U3 small nucleolar RNA-associated protein 12 (U3 snoRNA-associated protein 12) (DOM34-interacting protein 2) (U three protein 12) (Q12220)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12068309}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 15
- rRNA biogenesis protein RRP5
- Ribosome biogenesis protein BMS1
- Nucleolar protein 56
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar RNA-associated protein 11
- Nucleolar complex protein 4
- U3 small nucleolar RNA-associated protein 22
- U3 small nucleolar RNA-associated protein 21
- Protein BFR2
Sequence:
MVKSYQRFEQAAAFGVIASNANCVWIPASSGNSNGSGPGQLITSALEDVNIWDIKTGDLVSKLSDGLPPGASDARGAKPAECTYLEAHKDTDLLAVGYADGVIKVWDLMSKTVLLNFNGHKAAITLLQFDGTGTRLISGSKDSNIIVWDLVGEVGLYKLRSHKDSITGFWCQGEDWLISTSKDGMIKLWDLKTHQCIETHIAHTGECWGLAVKDDLLITTGTDSQVKIWKLDIENDKMGGKLTEMGIFEKQSKQRGLKIEFITNSSDKTSFFYIQNADKTIETFRIRKEEEIARGLKKREKRLKEKGLTEEEIAKSIKESYSSFILHPFQTIRSLYKIKSASWTTVSSSKLELVLTTSSNTIEYYSIPYEKRDPTSPAPLKTHTIELQGQRTDVRSIDISDDNKLLATASNGSLKIWNIKTHKCIRTFECGYALTCKFLPGGLLVILGTRNGELQLFDLASSSLLDTIEDAHDAAIWSLDLTSDGKRLVTGSADKTVKFWDFKVENSLVPGTKNKFLPVLKLHHDTTLELTDDILCVRVSPDDRYLAISLLDNTVKVFFLDSMKFYLSLYGHKLPVLSIDISFDSKMIITSSADKNIKIWGLDFGDCHKSLFAHQDSIMNVKFLPQSHNFFSCSKDAVVKYWDGEKFECIQKLYAHQSEVWALAVATDGGFVVSSSHDHSIRIWEETEDQVFLEEEKEKELEEQYEDTLLTSLEEGNGDDAFKADASGEGVEDEASGVHKQTLESLKAGERLMEALDLGIAEIEGLEAYNRDMKLWQRKKLGEAPIKPQGNAVLIAVNKTPEQYIMDTLLRIRMSQLEDALMVMPFSYVLKFLKFIDTVMQNKTLLHSHLPLICKNLFFIIKFNHKELVSQKNEELKLQINRVKTELRSALKSTEDDLGFNVQGLKFVKQQWNLRHNYEFVDEYDQQEKESNSARKRVFGTVI
Protein: Serine/threonine-protein kinase BRSK1 (EC 2.7.11.1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 1) (BR serine/threonine-protein kinase 1) (Serine/threonine-protein kinase SAD-B) (Q5RJI5)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-504' and 'Ser-554'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Synapse {ECO:0000250|UniProtKB:B2DD29}. Presynaptic active zone {ECO:0000250|UniProtKB:B2DD29}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:B2DD29}. Note=Nuclear in the absence of DNA damage. Translocated to the nucleus in response to UV- or MMS-induced DNA damage (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MSSGSKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAVKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGSGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGAGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSSGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGTPPRSLQPPPGRSDPDLSSSPRRGPPKDKKLLATNGTPLP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (O46308)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- CG5272 protein
- DNA replication inhibitor plutonium
- Mitosis initiation protein fs
- G2/mitotic-specific cyclin-B
- Protein asunder
- Tubulin gamma-2 chain
- ATP-dependent RNA helicase me31b
Sequence:
MELGDSKLRAVRVLGQGTFGRVFLCHQNEVRGQPERKVCVKRIIVRNPKTELGLIKEEVYIISQLRHPHIVEFLRSFSHAGTVNIVMEYVPNGTLRDVIQQLPSGTGGVNQERLMGYFRDMVVGLEYLHIRCVIHRDIKPENMLLDANDRVKIADFGIANVHAPSTQLQAGMGTPMYMAPEAMSSQGKVDFKSDVWSLGLVLYELCLGRSPFAAFLDKNATPALLHTVVQALVRPRLDCQLIRRLYDPVWAQVCELMVVYEQERRICLPDIFHLDAGMTVTLYKHYFSYSY
Protein: Glutaminase A (C8VAK7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- NADH-ubiquinone oxidoreductase
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH-ubiquinone oxidoreductase 299 kDa subunit, putative
- NADH dehydrogenase 1 alpha subcomplex subunit 1
- NADH-quinone oxidoreductase subunit D domain-containing protein
- NADH-ubiquinone oxidoreductase B14 subunit, putative
- Lactobacillus shifted protein
- NADH dehydrogenase 1 alpha subcomplex subunit
- NADH dehydrogenase 1 alpha subcomplex subunit 13
Sequence:
MRTFLLGILCAPLAILTGAASTFSPARPPALPLAVKSPYLSTWLPAGKDGGNGGYLAGEWPAFWEGQITGWAGLIRVDGQVYTWMGLPGSATVNQTAYEYTSTKSIFTMHIGDMVEMKITFLSPITPNDLRRQSLVFSYLDVSVTSLDGQSHSVQVYADISAEFASGDRSAIAQWNYGVTSDGVAYHKIYRQTPLLFSEHRDQAEWGDWYWATDNVAGLTYQAGPDVDVREAFARNGKLTNNNDVNYRAISNNWPVFGFAHDLGSISSSTKVLFSIGLTQREAIQYSGNSSTLSPLPALWTSYFSTALDALDFFHHDYQKSNSLSSDLDRRIAQDSVAAAGHDYLTITSLSIRQAFAATQLCGPANDPYLFMKEISSNGNMNTVDVIFPAHPVFLYTNPALLKYLLRPHLEIQESGNYPNSYAMHDIGAHYPNATGHPDGNDEPMPLEECGNMVIMALAYAQKAGDTAYLESHYTILRRWTDYLIEDSLYPANQISTDDFAGPLANQTNLALKGIIGIEAMSVIASLTGDSDDKMNLTNYAHDYIEKWLILGIARNTTYPHTTLSYGSNESHGLLYNLYADRELGLNLVPQSVYDMQSNFYPTIKGQYGVPLDTRHQYTKGDWELFTAAVASVSTRDMFIKLLAQWINETPTNRPLTDLYDTVTGDYPPVVFIARPVMGAAFTLLLLD
Protein: Zn(2)-C6 fungal-type domain-containing protein (G5EAZ8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Glutamyl-tRNA
Sequence:
MAAVITLQSSSTAGLQQGSPSDRHLLRPLLQNNPQQPPLQQQPLQPQQSPSPAPIGTLPRLPALGRDGPSCDACLRRKSRCAMNEMVNKCYSCDFHRQDCTFTLSSSSTTTTTITTTATSANSANSASSASTAGTSRPSTADVQSKKRKLDDIINSDADSPKRLSTVSKADSARSPLSEHPRFNAVSYWHQTTQHIGLTTELEPALLAYLPVDQNDESIVAASRVRKLSDDGTFMRVVNTMSHADAPQSATLVSIESLVAPYGSTLVEKFFEHIHPTFPILMEDVFRQSYRTRNGISPLLLSAVYVLALKFVDIGPASQSARRPDATRLEATALRLLNESLPYASISTIQAGLLLMQKSTLATAALNAQLVTAGFELGLHQDCSDWRMETWEKGLRKRLAWALYMQDKWSAMVHGRPSHVVSSNWTVQDLVEEDFTDAFASTASQPEDAPVGHGPLFFCHLVALTTILSDILDRFYTLQSIQEFKAAGSNRTRLILERAKPAQIRLKEWFARLPASLKLDSTTDLFENITEENARNGALHLSYFATEITLHRCIVRSLSPDSTDAYLSHICRSAAKTRLISAMDFVNRLRPPHLRSFWPAASRTHFALIGSFGILLRVTAPTKEEAEFYRLRLCEYRWTLSVSKKDAEFLEFALESLDNATDLDHHVPAKPGIDELMTSSSKPYIASTSARSGTTQEEAILDLDPRSGTGGTSSVISGLASPATSVSEESMHDAAVAPM
Protein: Hexon-interlacing protein (Protein IX) (P03282)
Organism: Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Function: Structural component of the virion that forms triskelion structures consisting of three molecules that stabilize three hexon trimers at the center of each icosahedral facet and fixes the peripentonal hexons (By similarity). Dispensable for assembly. During virus entry, recruits the anterograde motor kinesin-1 to the capsid docked at the nuclear pore complex thereby subjecting the docked capsid to a pulling force. The resulting tension leads to capsid disruption, dispersion of capsid fragments toward cell periphery and eventually viral DNA entry into the host nucleus.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04050}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04050}. Note=Located in the canyons between the hexons on the outer surface of the capsid. Forms a sort of hairnet on the outer side of the virion. Present in 240 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04050}.
Interaction partners:
Sequence:
MSANSFDGSIVSSYLTTRMPPWAGVRQNVMGSSIDGRPVLPANSTTLTYETVSGTPLETAASAAASAAAATARGIVTDFAFLSPLASSAASRSSARDDKLTALLAQLDSLTRELNVVSQQLLDLRQQVSALKASSPPNAV
Protein: Palmitoyltransferase (EC 2.3.1.225) (Q9I7L7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- IP07416p
Sequence:
MRFRSLKNIWPKEKLEQFLFLFILCGLPAIYYVLMEIILPELSDYWSPGYVFQLLLGLFLFSNVMSNYVMCILVDPSIDPKLMKNQLVRGQHSEDWHECDKCGILAPPRSRHCRKCGVCVLMRDHHCFFTGCCIGHENYRYFFYFLIYFFLSCMISLTSSSIFIYVLHGGRYQLFMLTHPAPNSAYFNSLIIRIIYFKLPDIYELVFTLVFVLLWIGVCVATYVAYDQWSRGYFCYDFELQNIPFDRKLRRNFKTFLGRRMKWTWISGFVPSQLDHDGFDLDPDNERVADWCSETTIKDG
Protein: Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic (EC 2.7.7.27) (ADP-glucose pyrophosphorylase) (ADP-glucose synthase) (AGPase S) (Alpha-D-glucose-1-phosphate adenyl transferase) (P55231)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Probable phosphoglucomutase, cytoplasmic 2
- Probable phosphoglucomutase, cytoplasmic 1
- Phosphoglucomutase, chloroplastic
- Probable starch synthase 4, chloroplastic/amyloplastic
- Sucrose synthase 3
- Sucrose synthase 1
- Sucrose synthase 5
- Sucrose synthase 2
- Sucrose synthase 4
Sequence:
MDSCCNFSLGTKTVLAKDSFKNVENKFLGEKIKGSVLKPFSSDLSSKKFRNRKLRPGVAYAIATSKNAKEALKNQPSMFERRRADPKNVAAIILGGGDGAKLFPLTKRAATPAVPVGGCYRMIDIPMSNCINSCINKIFVLTQFNSASLNRHLARTYFGNGINFGDGFVEVLAATQTPGEAGKKWFQGTADAVRKFLWVFEDAKNRNIENIIILSGDHLYRMNYMDFVQHHVDSKADITLSCAPVDESRASEYGLVNIDRSGRVVHFSEKPTGIDLKSMQTDTTMHGLSHQEAAKSPYIASMGVYCFKTEALLKLLTWRYPSSNDFGSEIIPAAIKDHNVQGYIYRDYWEDIGTIKSFYEANIALVEEHPKFEFYDQNTPFYTSPRFLPPTKTEKCRIVNSVISHGCFLGECSIQRSIIGERSRLDYGVELQDTLMLGADSYQTESEIASLLAEGNVPIGIGRDTKIRKCIIDKNAKIGKNVVIMNKDDVKEADRPEEGFYIRSGITVVVEKATIKDGTVI
Protein: Puratrophin-1 (Pleckstrin homology domain-containing family G member 4) (PH domain-containing family G member 4) (Purkinje cell atrophy-associated protein 1) (Q58EX7)
Organism: Homo sapiens (Human)
Function: Possible role in intracellular signaling and cytoskeleton dynamics at the Golgi.
Interaction partners:
- Spectrin beta chain, non-erythrocytic 2
- Cell division control protein 42 homolog
- Protein BEAN1
- Ataxin-1
- Ataxin-7
Sequence:
MERPLENGDESPDSQGHATDWRFAVCSFRDAWEEEEPASQMHVKDPGPPRPPAGATQDEELQGSPLSRKFQLPPAADESGDAQRGTVESSSVLSEGPGPSGVESLLCPMSSHLSLAQGESDTPGVGLVGDPGPSRAMPSGLSPGALDSDPVGLGDPLSEISKLLEAAPSGSGLPKPADCLLAQDLCWELLASGMATLPGTRDVQGRAVLLLCAHSPAWLQSECSSQELIRLLLYLRSIPRPEVQALGLTVLVDARICAPSSSLFSGLSQLQEAAPGAVYQVLLVGSTLLKEVPSGLQLEQLPSQSLLTHIPTAGLPTSLGGGLPYCHQAWLDFRRRLEALLQNCQAACALLQGAIESVKAVPQPMEPGEVGQLLQQTEVLMQQVLDSPWLAWLQCQGGRELTWLKQEVPEVTLSPDYRTAMDKADELYDRVDGLLHQLTLQSNQRIQALELVQTLEARESGLHQIEVWLQQVGWPALEEAGEPSLDMLLQAQGSFQELYQVAQEQVRQGEKFLQPLTGWEAAELDPPGARFLALRAQLTEFSRALAQRCQRLADAERLFQLFREALTWAEEGQRVLAELEQERPGVVLQQLQLHWTRHPDLPPAHFRKMWALATGLGSEAIRQECRWAWARCQDTWLALDQKLEASLKLPPVGSTASLCVSQVPAAPAHPPLRKAYSFDRNLGQSLSEPACHCHHAATIAACRRPEAGGGALPQASPTVPPPGSSDPRSLNRLQLVLAEMVATEREYVRALEYTMENYFPELDRPDVPQGLRGQRAHLFGNLEKLRDFHCHFFLRELEACTRHPPRVAYAFLRHRVQFGMYALYSKNKPRSDALMSSYGHTFFKDKQQALGDHLDLASYLLKPIQRMGKYALLLQELARACGGPTQELSALREAQSLVHFQLRHGNDLLAMDAIQGCDVNLKEQGQLVRQDEFVVRTGRHKSVRRIFLFEELLLFSKPRHGPTGVDTFAYKRSFKMADLGLTECCGNSNLRFEIWFRRRKARDTFVLQASSLAIKQAWTADISHLLWRQAVHNKEVRMAEMVSMGVGNKAFRDIAPSEEAINDRTVNYVLKCREVRSRASIAVAPFDHDSLYLGASNSLPGDPASCSVLGSLNLHLYRDPALLGLRCPLYPSFPEEAALEAEAELGGQPSLTAEDSEISSQCPSASGSSGSDSSCVSGQALGRGLEDLPCV
Protein: Cell wall mannoprotein PIR1 (Covalently-linked cell wall protein 6) (Protein with internal repeats 1) (Q03178)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the outer cell wall layer. Required for stability of the cell wall and for optimal growth. Required for resistance against several antifungal and cell wall-perturbing agents and for tolerance to heat shock.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:15781460, ECO:0000269|PubMed:9192695, ECO:0000269|PubMed:9301021}. Note=Covalently attached to the cell wall.
Interaction partners:
- Cell wall mannoprotein HSP150
- Probable secreted beta-glucosidase SUN4
- Probable circularly permuted 1,3-beta-glucanase TOS1
- Cell wall protein CWP1
Sequence:
MQYKKSLVASALVATSLAAYAPKDPWSTLTPSATYKGGITDYSSTFGIAVEPIATTASSKAKRAAAISQIGDGQIQATTKTTAAAVSQIGDGQIQATTKTKAAAVSQIGDGQIQATTKTTSAKTTAAAVSQIGDGQIQATTKTKAAAVSQIGDGQIQATTKTTAAAVSQIGDGQIQATTKTTAAAVSQIGDGQIQATTNTTVAPVSQITDGQIQATTLTSATIIPSPAPAPITNGTDPVTAETCKSSGTLEMNLKGGILTDGKGRIGSIVANRQFQFDGPPPQAGAIYAAGWSITPEGNLAIGDQDTFYQCLSGNFYNLYDEHIGTQCNAVHLQAIDLLNC