wanglab/gogpt-training-data huggingface dataset:
Protein: Histone H2B variant L1 (Histone H2B subacrosomal variant) (Q9D9Z7)
Organism: Mus musculus (Mouse)
Function: May act as an acrosome-nuclear docking protein in sperm.
Subcellular location: Cytoplasm {ECO:0000250}. Note=Subacrosomal region. Does not localize in nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Histone H3.2
- Histone H3.3
- Histone H3.1
- Histone H4
- Plasminogen
- Histone H2AX
- Breast cancer type 1 susceptibility protein homolog
- Histone deacetylase 1
- Histone deacetylase 2
- Histone H2A.Z
Sequence:
MAKPTFKRQCYIKRHLRPLYRKHSRCSSINLGHGNYSLYINRVLKEVVPNRGISSYSVDIMNILINDIFERIATEACQQMFLRKRCTLTPGDIQQAVHLLLPKKLATLAVTFGSKAVHRFIHS
Protein: Peripherin (Neurofilament 4) (P41219)
Organism: Homo sapiens (Human)
Function: Class-III neuronal intermediate filament protein (By similarity). May form an independent structural network without the involvement of other neurofilaments or may cooperate with the neuronal intermediate filament proteins NEFL, NEFH, NEFM and INA to form a filamentous network. Assembly of the neuronal intermediate filaments may be regulated by RAB7A (By similarity). Plays a role in the development of unmyelinated sensory neurons (By similarity). May be involved in axon elongation and axon regeneration after injury (By similarity). Inhibits neurite extension in type II spiral ganglion neurons in the cochlea (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15322088, ECO:0000269|PubMed:15446584, ECO:0000269|PubMed:18408015}. Cell projection, axon {ECO:0000250|UniProtKB:P15331}. Perikaryon {ECO:0000250|UniProtKB:P15331}.
Interaction partners:
- Neurofilament medium polypeptide
- Neurofilament heavy polypeptide
- Neurofilament light polypeptide
Sequence:
MSHHPSGLRAGFSSTSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSASPSSSVRLGSFRSPRAGAGALLRLPSERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQYESIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESRRQIQSLTCEVDGLRGTNEALLRQLRELEEQFALEAGGYQAGAARLEEELRQLKEEMARHLREYQELLNVKMALDIEIATYRKLLEGEESRISVPVHSFASLNIKTTVPEVEPPQDSHSRKTVLIKTIETRNGEVVTESQKEQRSELDKSSAHSY
Protein: Cytosolic carboxypeptidase 1 (EC 3.4.17.-) (O76373)
Organism: Caenorhabditis elegans
Function: Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia. In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles. Also regulates microtubule dynamics in uterine muscle cells.
Subcellular location: Perikaryon {ECO:0000269|PubMed:21982591}. Cell projection, cilium {ECO:0000269|PubMed:21982591}. Cell projection, dendrite {ECO:0000269|PubMed:21982591}.
Interaction partners:
- Tubulin polyglutamylase ttll-4
- Tubulin polyglutamylase ttll-5
- Tubulin polyglutamylase ttll-11
- Probable tubulin polyglutamylase ttll-9
- Probable tubulin polyglutamylase ttll-15
- Kinesin-like protein
- Tubulin--tyrosine ligase-like protein 12
- Spastin homolog
- Kinesin-like protein
- Osmotic avoidance abnormal protein 3
Sequence:
MPSDSDDVAAVKQPWSQLIVDISNFLSEHPQSKTSQALLPSCNGVWSDEEKLELIEAFGHKKQSHLTKSGVKAVLAAFEGDRTQPDVIFLCRLLHLIFSHFSSENDRKKEKYIVKCDVIATLTRITRKRIIMTLDVTDESSIDHNLDEVLWKLLHKIGLKDPRVSLKVRMGGLISPMCKLFIQKDTLPELFLPFFIKISRSPRNGQAIGRYEGFMTRLLVKIKALDASDQTSQVLLLDKHLQLLFFTMKNKRTRTQLLRENICKYLLEVLRRHLASSSNSRPTRLLSSLFGTFDKSLSAAHTEVVIGTIAILRLLSNFKKARDELKNLQVLDICSRELKEFWSDEWKTGPKSRIVDSLSALCLRCMSPLPYPLETRRFPIDFPLPTATPSTPGGHGRIRNSSSINISFDNGRSSDEDGMDEEDEAFVRDDDDEGKDDRGSDDDDGKDDDEINGALPKTTRLNPQQLAKYAPFFVENEQGTLQPTFSMIYQTNQESWRSICEKTRHVMPIHHHLPIEMFNTPTRIREKTAKTSNNMKKMIIEELDKPERSATSNQVIYDLDTAAFDGLPSPELPFVTGGGKLDTSKDLQFDSRFESGNLRMVIQVAPTHYELFLSPDVNQLRDHYQWFFFQVSNMRKSVKYTFEIVNCLKSTSLYSQGMQPVMYSMMESANGWRRVGENVCYFRNLYINENEEKKNVEEQKKKKYYYSIRFNVTFQNTGDICYIAYHYPYTYSFLNSSLSMLKKRKQENVYCREDVIGHSLAGNPIKMLTITTPASAAEIAAREVIVLSARVHPGETNASWIMQGILENLLCRQSNEMYRLRESFIFKIVPMINPDGVTNGSHRCSLAGIDLNRMWDRPNEALHPEVFATKAIIQYLCEVANKKPFAYVDIHGHSKKWDYFVYGNNASESWRADDVLDVGAAQLEEELHLALPKALEATCPSRFNASECRFNITRAKESSARVNVWRQFGVSTAYTLESTFCGFHKGQNSGYQINTSDLKEIGRDLLHSFLEMTKT
Protein: 1,4-alpha-glucan branching enzyme TK1436 (EC 2.4.1.18) (1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase) (Alpha-(1->4)-glucan branching enzyme) (Branching enzyme) (BE) (Q5JDJ7)
Organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Function: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 5 to 30, with two local maxima at DP 6 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Does not display alpha-galactosidase or pullulanase activity, since melibiose and pullulan are not substrates. Is not able to catalyze the hydrolysis or transglycosylation of maltoheptaose, suggesting that the TK1436 protein contains neither alpha-amylase nor 4-alpha-glucanotransferase activity.
Interaction partners:
- glycogen phosphorylase
- Cyclomaltodextrinase
- Glycogen synthase
- 4-alpha-glucanotransferase
- Pullulanase type II, GH13 family
- Alpha-amylase, GH13 family
- Glycosyltransferase, family 4
- Glycosyltransferase, family 4
- Nitrogen regulatory protein P-II
Sequence:
MKGYLTFVLHTHIPYVRKHGKWPFGEEWVFEAISETYIPLLMEFERLRDSGVKFGIVINVTPVLAEQLTDEYMKKAFEEYMERKLKAMEEDLKSGKYDEKAVSYMLNYFRKVYDYWKAINGDIIGKLRELQDQGYVEVITSAATHGYLPLLGRDEAIRAQIANGVATYEKHFGMKPKGIWLPECAYRPAGEWELPGGRKVKRQGIEKFLEEFGLRYFFVESRLIDEGPASNVYGEVLIADTEKTTLRPYWIKGSNVAVFARNRETGHQVWSAHYGYPGDFWYREFHKKAPKSGGQYWRITSKEVGLGEKEFYDPDKAMERVEEHARHFVSLVERLLREHEEKFGEKGIIVAPYDTELFGHWWFEGVKWLGRVLELLYQRGVETPTLSRFLEEYSGEKHEIELPEGSWGANSDHSTWWNEETEWTWPHIYRAEDRMVAIVSRFRGRDELTNRVIEQLARELLILEASDWQFLITTGQAKEYAKRRVLIHSRDFHRLANELVRYVKIGEFDVKLLEELEERDNPFRPVVVGPYVSENPPELEEYVEPPEVPPEKEETEEKPKVLTEKATSLALAVKKVKPVKEETREVKKKAVEASKRGKRKSSKSKRLPRKVSKKAPSKGPSDLLSIKGIGPKTFQKLKRAGVETIEDLKNANIEDLARKTGISTKRLKKFIAQVE
Protein: GH13023p (Q95U23)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPQSIARIANVGKEHRTVSSHPNYLQFEEPKFDLKDVTVEELAAAANVTVDTIKHAIYVREQQLKAEHRAQLAAKLREEFMRTSTVRTTTTTTTTTTTTPRPQKSLAEHKVSKVMNAPKEYYPVGYDKNFDDNFKSKVDLPPTSFSCAKQKHFPGLYADTDLGCMVFHVCALTDDGMVRKSFLCPENTLFDQTILKCNWWFYVDCSSSTSVYDSNIPISKSYQLMKSLTYFSKYAGGQRHEQGGDKDENALDIDSLRESMEGVARRQEQAKKAELRVEEQRSMPKEDHEHVVPAEAEQQLSN
Protein: E3 ubiquitin-protein ligase RSP5 (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase RSP5) (Q5BDP1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. Ubiquitinates 'Lys-528' of the uric acid/xanthine transporter uapA at the cell membrane, leading to its internalization, sorting into the endosomal pathway to the vacuolar lumen where it is eventually degraded.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P39940}.
Interaction partners:
- HECT-type ubiquitin ligase-interacting protein creD
- RNA polymerase I specific transcription initiation factor Rrn7, putative
- 26S proteasome regulatory subunit S5A
- Catabolite repression protein creC
- Pheromone receptor PREB
- Ubiquitin-like domain-containing protein
- B-zip transcription factor
- Uncharacterized protein
- Ubiquitin carboxyl-terminal hydrolase creB
- DNA-directed RNA polymerase subunit
Sequence:
MGSNLPAQPNLRVTIIAADGLYKRDVFRLPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNPNQANGLHRTQLGASTSSGLVPQVAPTPSVPQAGPSSVDQSAAASSASLNPQRVPSATRPTSQIAPPNGAPPIANGQGVPRPNLSSFEDNQGRLPAGWERREDNLGRTYYVDHNTRTTTWNRPSANYNEQTQRTQREANMQLERRAHQNRMLPEDRTGASSPNLSETQPQAQTPPAGGSGASNSNVVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGQNASGGNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLTWTLENDIEGIIDLTFTVDDEKFGERRTIELKPGGEDIPVTNENKHEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQEQDEVIQNFWKIVRTWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPIALPKSHTCFNRLDLPPYKSHEVLEHKLSIAVEETLGFGQE
Protein: Aminomethyltransferase, mitochondrial (EC 2.1.2.10) (Glycine cleavage system T protein) (GCVT) (O65396)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The glycine decarboxylase (GDC) or glycine cleavage system catalyzes the degradation of glycine.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Glycine dehydrogenase
- Glycine dehydrogenase
- Glycine cleavage system H protein 1
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Glycine cleavage system H protein 3
- Glycine cleavage system H protein 2
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Serine hydroxymethyltransferase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 1, mitochondrial
Sequence:
MRGGSLWQLGQSITRRLAQSDKKVVSRRYFASEADLKKTALYDFHVAHGGKMVPFAGWSMPIQYKDSIMDSTVNCRENGSLFDVAHMCGLSLKGKDCVPFLETLVVADVAGLAPGTGSLTVFTNEKGGAIDDSVITKVTDEHIYLVVNAGCRDKDLAHIEEHMKAFKSKGGDVSWHIHDERSLLALQGPLAAPVLQHLTKEDLSKLYFGNFQILDINGSTCFLTRTGYTGEDGFEISVPDEHAVDLAKAILEKSEGKVRLTGLGARDSLRLEAGLCLYGNDMEQHISPVEAGLTWAIGKRRRAEGGFLGADVILQQLKDGPTIRRVGFFSSGPPARSHSEVHDESGNKIGEITSGGFSPNLKKNIAMGYVKSGQHKTGTKVKILVRGKPYEGSITKMPFVATKYYKPT
Protein: Lactam utilization protein lamB (P38096)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in the utilization of lactams. Required for the conversion of exogenous 2-pyrrolidinone (gamma-butyrolactam) to endogenous gamma-amino-n-butyrate (GABA).
Interaction partners:
- Nucleoporin NSP1
- Acetamidase regulatory protein
- GTP-binding nuclear protein
- Nuclear pore complex protein
Sequence:
MAPIKKKALINCDMGEAYGNWTCGPDLELLPLIDIANIACGFHAGDPLIMMETVRNCKAHNILVGAHPGLPDIQGFGRREMKLSPEELTAITIYQVGALQGFLDREGVRLNHVKPHGVLYGMMCRDYEVAKAVMLGIPKGIPVFGLPGTNMEKAANDLGIEFRAEFYGDVKYDSNGMLVIDRKKKPWDPADVEKHVRQQLEDQSVTSVDGVVVPLPIKDYDVSICCHSDSPGCLEIIKTTKKVVDEFNKKYGF
Protein: LIN-65L (Q95XN0)
Organism: Caenorhabditis elegans
Interaction partners:
- Lysine-specific demethylase 7 homolog
- Lysine-specific demethylase jmjd-3.1
- Homeobox protein dve-1
- ARF7 effector protein C-terminal domain-containing protein
- Stress activated transcription factor atfs-1
- Transcription factor atf-4 homolog
- ATP-dependent Clp protease proteolytic subunit 1, mitochondrial
Sequence:
MSEVIDESILNTEASDDPIPPLNDDQIAELLGEDGEIMEITEQKDESDDVVMLDDDDDDTPEPILVIDMDEDEDVTTDGPESQEELAADAPAPGAPEASAPAQEASEASAPDQEAPEVQDVPDSSGAPDASAQASEASDASAPEVPGSTEAQDAQDVPDSLGASDASAQEIPEAPEAPEAPEIAAEIDEEVLLAEQNGVLDEGFDETDDIIIEEEAVEEAEAVEPPINTENQENALEMLEERLKKNEEKEIVEKSDVKPEDEDIIHMETDSVETSSRKRTGGATSPRSPAQKRPKRRVQTLLKMRQNAIELLTRLYGSWDAQLSLSNLETIRLLGVNNNRKLIEIFEENEQVLKQKVSALTEELKKEKLAHAGTRSALKELTNEITGMRVQMNKLRSMVTQPTTSKIIDSFVQRHQAFEQQQQFQHQHHQHRPIMLAPRHHPPPPPHFTPNQRAAAPYHPNMVQPNRLAAMPHRRPIIGMQQQNSAPPQFNGHQALVPSPQSSSAFSRPPPTQLATQRRAPPLASTGLPATVRWEAIPPPKNPNVGHNEPPLNNGGRAQPLIDNTRVHDNTIMLCVPLVSTANTISSGDSTRLPKVPRIYENLTANPDLSVTIHSSAQDFRENYQIGGKINYEYLGGFDQYNIQVFVQVSSLKFTGMNGYPDPEDRISIDWGCSKLWPCKPKSHHKFRVRFHQAQLLPKNDRITIVAVAKDKTSGIIHISQPTFITLE
Protein: Tubulin alpha chain (O18688)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MREVISIHVGQAGVQIGNACWELYCLEHGIQPDGTMPSDQQADGESFTTFFSDTGNGRYVPRSIFVDLEPTVVDEIRTGTYKKLFHPEQMITGKEDAANNYARGHYTVGKELIDTVLDRIRRLADNCSGLQGFFVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLSVDRPSYTNLNRIISQVVSSITASLRFDGALNVDLNEFQTNLVPYPRIHFPLAAYTPLISADKAYHEALSVNDITNSCFEPANQMVKCDPRHGKYMAVCLLYRGDVVPKDVNTAIAAIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVPRAVCMLSNTTAIAEAWSRLDYKFDLMYAKRAFVHWYVGEGMEEGEFTEAREDLAALEKDYEEVGADSNEGGNEEEGEEY
Protein: F14O10.3 protein (Pseudouridine synthase family protein) (Q9LN29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MENQEPDIEKLPRDDVPDREPDHKKLKISTTGQETDSSAVTTGGSNVAERRAPKYRRRKVAIVFAFCGVGYQGMQKNPGAKTIEGELEEALFHAGAVPDADRNKPRNYEWARSARTDKGVSAVGQVVSGRFYVDPPGFVERLNSKLPDQIRVFGYKRVAPSFSSKKFCDRRRYVYLIPVFALDPCVHGEAEMVRTDLGYEYVKCVECSEKGYKIPLGVMGKDTDCCDTKSLEIQSDISSSTCDAIGADVKCETLSSSVPSAENNLNSEVLDGADVSALSSKAEGMEESNTLAKVEMNNGEGEDMTKSESKFCYGEKEKERFNRILSYYVGSHNFHNFTTRTKAADPAANRYILSFNANTVINLDGKDFVKCEVVGQSFMLHQIRKMIGLAVAIMRNYAPESLIEASFKKDVRINVPMAPEVGLYLDECFFTSYNKRFKGSHEEVSMEEYKEVAEEFKWKYVYSHIGSAEEKDGAVAIWLHSLNQRNYPDLRSNEYQPDEVIVYKKIGEASEENIHEGNAELFVVDKVNDETSEGTTMEERTTLEEKATG
Protein: Varicose (A1XXK2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPVETIKMVGLRRDPSKPLGLTVELDEFKQLVVARILAGGVIDKQSMLHVGDVILEVNGTPVRTPDELQVEVSRAKENLTLKIGPNVDEEIKSGRYTVSGGQVKQNGIASLETGKKLTCYMRALFT
Protein: Zinc finger protein 707 (Q96C28)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDMAQEPVTFRDVAIYFSREEWACLEPSQRALYRDVMLDNFSSVAALGFCSPRPDLVSRLEQWEEPWVEDRERPEFQAVQRGPRPGARKSADPKRPCDHPAWAHKKTHVRRERAREGSSFRKGFRLDTDDGQLPRAAPERTDAKPTAFPCQVLTQRCGRRPGRRERRKQRAVELSFICGTCGKALSCHSRLLAHQTVHTGTKAFECPECGQTFRWASNLQRHQKNHTREKPFCCEACGQAFSLKDRLAQHRKVHTEHRPYSCGDCGKAFKQKSNLLRHQLVHTGERPFYCADCGKAFRTKENLSHHQRVHSGEKPYTCAECGKSFRWPKGFSIHRRLHLTKRFYECGHCGKGFRHLGFFTRHQRTHRHGEV
Protein: Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.24) (Peroxiredoxin 3) (Thioredoxinperoxidase 3) (Q9VEJ0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. May be involved in aging-associated changes in the responsiveness to oxidative stress. Involved in the maintenance of global thiol redox homeostasis. Functions in the central nervous system (CNS) and in motor neurons and is essential for normal motor function.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11677042, ECO:0000269|PubMed:20869434}.
Interaction partners:
- Peroxiredoxin-5
- Thioredoxin-2
- Superoxide dismutase, mitochondrial
- GEO01508p1
- Thioredoxin reductase 2, mitochondrial
- Sulfiredoxin
- Thioredoxin-1
- Thioredoxin-1
- Glutaredoxin-2
- Vacuolar protein sorting-associated protein 29
Sequence:
MSFVARSLIRNVPLMGKAILSQQKQIAARLLHQTAPLAAVRVQQPAPDFKGLAVVDNSFQEVKLEDYRGKYLVLFFYPLDFTFVCPTEIVAFSERIKEFHDINTEVLGVSVDSHFSHLTWCNVDRKNGGVGQLKYPLLSDLTKKISADYDVLLDKEGISLRGTFIIDPNGILRQYSINDLPVGRSVDEVLRLIKAFQFVEQHGEVCPANWNPNSNPATIKPDVEESKKYFSKHG
Protein: General transcription factor IIH subunit 1 (Basic transcription factor 2 62 kDa subunit) (BTF2 p62) (General transcription factor IIH polypeptide 1) (TFIIH basal transcription factor complex p62 subunit) (P32780)
Organism: Homo sapiens (Human)
Function: 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. 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.
Subcellular location: Nucleus.
Interaction partners:
- General transcription factor IIH subunit 2
- General transcription and DNA repair factor IIH helicase subunit XPD
- CDK-activating kinase assembly factor MAT1
- DNA excision repair protein ERCC-5
- Cyclin-H
- General transcription factor IIE subunit 1
- General transcription factor IIH subunit 2-like protein
- Cyclin-dependent kinase 7
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription factor IIH subunit 5
Sequence:
MATSSEEVLLIVKKVRQKKQDGALYLMAERIAWAPEGKDRFTISHMYADIKCQKISPEGKAKIQLQLVLHAGDTTNFHFSNESTAVKERDAVKDLLQQLLPKFKRKANKELEEKNRMLQEDPVLFQLYKDLVVSQVISAEEFWANRLNVNATDSSSTSNHKQDVGISAAFLADVRPQTDGCNGLRYNLTSDIIESIFRTYPAVKMKYAENVPHNMTEKEFWTRFFQSHYFHRDRLNTGSKDLFAECAKIDEKGLKTMVSLGVKNPLLDLTALEDKPLDEGYGISSVPSASNSKSIKENSNAAIIKRFNHHSAMVLAAGLRKQEAQNEQTSEPSNMDGNSGDADCFQPAVKRAKLQESIEYEDLGKNNSVKTIALNLKKSDRYYHGPTPIQSLQYATSQDIINSFQSIRQEMEAYTPKLTQVLSSSAASSTITALSPGGALMQGGTQQAINQMVPNDIQSELKHLYVAVGELLRHFWSCFPVNTPFLEEKVVKMKSNLERFQVTKLCPFQEKIRRQYLSTNLVSHIEEMLQTAYNKLHTWQSRRLMKKT
Protein: AP-3 complex subunit beta-2 (Adaptor protein complex AP-3 subunit beta-2) (Adaptor-related protein complex 3 subunit beta-2) (Beta-3B-adaptin) (Clathrin assembly protein complex 3 beta-2 large chain) (Neuron-specific vesicle coat protein beta-NAP) (Q13367)
Organism: Homo sapiens (Human)
Function: Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.
Interaction partners:
- AP-3 complex subunit mu-1
- AP-3 complex subunit mu-2
- AP-3 complex subunit sigma-1
- AP-3 complex subunit delta-1
- AP-3 complex subunit sigma-2
- AP-4 complex subunit epsilon-1
- AP-3 complex subunit beta-1
- AP-4 complex subunit sigma-1
- AP-4 complex subunit mu-1
- AP-2 complex subunit alpha-1
Sequence:
MSAAPAYSEDKGGSAGPGEPEYGHDPASGGIFSSDYKRHDDLKEMLDTNKDSLKLEAMKRIVAMIARGKNASDLFPAVVKNVACKNIEVKKLVYVYLVRYAEEQQDLALLSISTFQRGLKDPNQLIRASALRVLSSIRVPIIVPIMMLAIKEAASDMSPYVRKTAAHAIPKLYSLDSDQKDQLIEVIEKLLADKTTLVAGSVVMAFEEVCPERIDLIHKNYRKLCNLLIDVEEWGQVVIISMLTRYARTQFLSPTQNESLLEENAEKAFYGSEEDEAKGAGSEETAAAAAPSRKPYVMDPDHRLLLRNTKPLLQSRSAAVVMAVAQLYFHLAPKAEVGVIAKALVRLLRSHSEVQYVVLQNVATMSIKRRGMFEPYLKSFYIRSTDPTQIKILKLEVLTNLANETNIPTVLREFQTYIRSMDKDFVAATIQAIGRCATNIGRVRDTCLNGLVQLLSNRDELVVAESVVVIKKLLQMQPAQHGEIIKHLAKLTDNIQVPMARASILWLIGEYCEHVPRIAPDVLRKMAKSFTAEEDIVKLQVINLAAKLYLTNSKQTKLLTQYVLSLAKYDQNYDIRDRARFTRQLIVPSEQGGALSRHAKKLFLAPKPAPVLESSFKDRDHFQLGSLSHLLNAKATGYQELPDWPEEAPDPSVRNVEVPEWTKCSNREKRKEKEKPFYSDSEGESGPTESADSDPESESESDSKSSSESGSGESSSESDNEDQDEDEEKGRGSESEQSEEDGKRKTKKKVPERKGEASSSDEGSDSSSSSSESEMTSESEEEQLEPASWSRKTPPSSKSAPATKEISLLDLEDFTPPSVQPVSPPAIVSTSLAADLEGLTLTDSTLVPSLLSPVSGVGRQELLHRVAGEGLAVDYTFSRQPFSGDPHMVSVHIHFSNSSDTPIKGLHVGTPKLPAGISIQEFPEIESLAPGESATAVMGINFCDSTQAANFQLCTQTRQFYVSIQPPVGELMAPVFMSENEFKKEQGKLMGMNEITEKLMLPDTCRSDHIVVQKVTATANLGRVPCGTSDEYRFAGRTLTGGSLVLLTLDARPAGAAQLTVNSEKMVIGTMLVKDVIQALTQ
Protein: RIKEN cDNA 2310002L09 gene (Q14C20)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKCLVKIRTQRSLHLHMMNHCSSNVFVRLLKHGSKVIPRNAGAPLSKVDASEHMVASSPVKGAQSAGSPRKEEDKVKEDPLILSELAYNTSASLLPTQVDDDEVDMLFDCPSRFVLEREDTDTFEDVEADENVFLMAEEEKVKEAHQALSWSYSILTGRIWLNPLVKRCSRLLVVGLGLLLFVFPLVLLLLESVPVSMP
Protein: Anti-Muellerian hormone type-2 receptor (EC 2.7.11.30) (Anti-Muellerian hormone type II receptor) (AMH type II receptor) (C14) (MIS type II receptor) (MISRII) (MRII) (Q62893)
Organism: Rattus norvegicus (Rat)
Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Muellerian-inhibiting factor
- Bone morphogenetic protein receptor type-1A
- Activin receptor type-1
- Bone morphogenetic protein receptor type-2
- Growth/differentiation factor 6
- Growth/differentiation factor 5
- Bone morphogenetic protein 4
- Bone morphogenetic protein 6
- Bone morphogenetic protein 7
- Growth differentiation factor 7
Sequence:
MLGTLGLWTLLPAAAQVSPNRRTCVFFEAPGVRGSTKTLGEVVDAGPGPPKGIRCLYSHCCFGIWNLTHGRAQVEMQGCLDSDEPGCESLHCDPVPRAHPSPSSTLFTCSCGTDFCNANYSHLPPSGNRGAPGPQEPQATPGGPIWMAQLLLGVFLVLLLSIIILALLQRKACRVQGGSDPEPEPGSGGDCSEELPELAELRFSQVIQEGGHAVVWAGRLQGEMVAIKAFPPRAVAQFRAERAVYQLLGLQHNHIVRFITAGQGGPGPLPSGPLLVLELYPKGSLCHYLTQYTSDWGSSLRMALSLAEGLAFLHGERWQDGQYKPGIAHRDLSSQNVLIREDRSCAIGDLGLALVLPGLAQPPALAPTQPRGPAAILEAGTQRYMAPELLDKTLDLQDWGTALQRADVYSLALLLWEILSRCSDLRPDHRPPPFQLAYEAELGSNPSACELWALAVAERKRPNIPSSWSCSATDPRGLRELLEDCWDADPEARLTAECVQQRLAALAYPQVASSFPESCPQGCPENCPAAPASAAFPCRPQQSSCLLSVQQGSGSKS
Protein: Phospholipase A1-Igamma2, chloroplastic (EC 3.1.1.-) (DAD1-like lipase 3) (Q3EBR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acylhydrolase with broad specificity. Catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position. Possesses moderate activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:19527719, ECO:0000269|PubMed:31928671}.
Interaction partners:
- Glycosyltransferase
- Carbohydrate-binding X8 domain-containing protein
Sequence:
MAAIPSHNNLLTINHKNSITGSSSLNTNFSEINFPAKFRVATRALSRTDESSLSAVISRLERERRERQGLLIEEAEGAGELWMTAEDIRRRDKKTEEERRLRDTWRKIQGEDDWAGLMDPMDPILRSELIRYGEMAQACYDAFDFDPASKYCGTSRFTRLEFFDSLGMIDSGYEVARYLYATSNINLPNFFSKSRWSKVWSKNANWMGYVAVSDDETSRNRLGRRDIAIAWRGTVTKLEWIADLKDYLKPVTENKIRCPDPAVKVESGFLDLYTDKDTTCKFARFSAREQILTEVKRLVEEHGDDDDSDLSITVTGHSLGGALAILSAYDIAEMRLNRSKKGKVIPVTVLTYGGPRVGNVRFRERMEELGVKVMRVVNVHDVVPKSPGLFLNESRPHALMKIAEGLPWCYSHVGEELALDHQNSPFLKPSVDVSTAHNLEAMLHLLDGYHGKGERFVLSSGRDHALVNKASDFLKEHLQIPPFWRQDANKGMVRNSEGRWIQAERLRFEDHHSPDIHHHLSQLRLDHPC
Protein: Nematode cuticle collagen N-terminal domain-containing protein (Q9N527)
Organism: Caenorhabditis elegans
Interaction partners:
- Transcellular chaperone signaling
- Chitin-binding type-2 domain-containing protein
- C-type lectin domain-containing protein
- Zinc metalloproteinase nas-30
- FIP
- Sodium/potassium-transporting ATPase subunit beta-1-interacting protein
- Nematode cuticle collagen N-terminal domain-containing protein
Sequence:
MEDTREKAYKAVTYSAVTFSFLAILSVCISMPIIYNFVDSIHQQTKRDMTFCKSTARDIMSEISHKKPIAAAIAGNLTTIRNKRQAVGCAGCCKPGHPGRPGLPGRNGKPGVPGAPGRPGTPGRPPIVCEEQDVPPCNPCPPGPPGPQGPTGNSGQPGRPGNPGRPGSPGTPGPVGPNGASGDSGAPGNDGEKGEPGRPAQSTPSTPGEPGNPGDAGATGAPGDDGAPGRDGQPGQSGPPGPPGPPGNVGEAGPPGKPGQPGLPGPQGERGICPKYCALDGGVFFEDGTRR
Protein: At4g14455 (Q147J7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046280}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00046280}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004194}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004194}.
Interaction partners:
Sequence:
MNFRRENRASRTSLFDGLDGLEEGRLRASSSYAHDERDNDEALENLQDRVSFLKRVTGDIHEEVENHNRLLDKVGNKMDSARGIMSGTINRFKLVFEKKSNRKSCKLIAYFVLLFLIMYYLIRLLNYIKG