wanglab/gogpt-training-data huggingface dataset:
Protein: Microtubule-associated protein 1 light chain 3 beta (Autophagy-related protein LC3 B) (Autophagy-related ubiquitin-like modifier LC3 B) (MAP1 light chain 3-like protein 2) (Microtubule-associated proteins 1A/1B light chain 3B) (MAP1A/MAP1B LC3 B) (MAP1A/MAP1B light chain 3 B) (Q9GZQ8)
Organism: Homo sapiens (Human)
Function: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. In response to cellular stress and upon mitochondria fission, binds C-18 ceramides and anchors autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria. While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. Upon nutrient stress, directly recruits cofactor JMY to the phagophore membrane surfaces and promotes JMY's actin nucleation activity and autophagosome biogenesis during autophagy.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:20529957, ECO:0000269|PubMed:22311637, ECO:0000269|PubMed:23459205, ECO:0000269|PubMed:31315929, ECO:0000269|PubMed:33499712}; Lipid-anchor {ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:29458288}. Endomembrane system {ECO:0000269|PubMed:12740394}; Lipid-anchor {ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:29458288}. Mitochondrion membrane {ECO:0000269|PubMed:25215947, ECO:0000269|PubMed:28017329}; Lipid-anchor {ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:29458288}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9CQV6}. Cytoplasmic vesicle {ECO:0000269|PubMed:30420355}. Note=LC3-II binds to the autophagic membranes. LC3-II localizes with the mitochondrial inner membrane during Parkin-mediated mitophagy (PubMed:28017329). Also localizes to discrete punctae along the ciliary axoneme. {ECO:0000269|PubMed:28017329}.
Interaction partners:
- Sequestosome-1
- Next to BRCA1 gene 1 protein
- FUN14 domain-containing protein 1
- Cysteine protease ATG4B
- Ubiquitin-like modifier-activating enzyme ATG7
- Ubiquitin-like-conjugating enzyme ATG3
- Optineurin
- FYVE and coiled-coil domain-containing protein 1
- Serine/threonine-protein kinase ULK1
- Autophagy protein 5
Sequence:
MPSEKTFKQRRTFEQRVEDVRLIREQHPTKIPVIIERYKGEKQLPVLDKTKFLVPDHVNMSELIKIIRRRLQLNANQAFFLLVNGHSMVSVSTPISEVYESEKDEDGFLYMVYASQETFGMKLSV
Protein: Adenylate kinase, putative (EC 2.7.4.3) (Q38BZ2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Adenylosuccinate lyase
- Adenosine kinase
- Adenosine kinase
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- Pyruvate kinase
- Phosphodiesterase
Sequence:
MKVIFLGPPGCGKGTQSPFVAKRYDICHLSTGDMLREAVEKKTEYGLKAKSVMDVGGLVSDDIVFGIVKESIKQPRCKNGYLLDGYPRTLRQAEMMEEAGEKVNKVIHFDAPDDVIISRVSGRWLHRASGRIYHEVFCPPKVRGLDDVTSEPLIQRPDDRKEVVEKRLVGYHRQTKPLIDYYRARGVLATLDATQSVNVVRESLRRVLDPVARLIGAKIHGN
Protein: PWWP domain-containing protein 2A (Q69Z61)
Organism: Mus musculus (Mouse)
Function: Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes. Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (By similarity). Plays a role in facilitating transcriptional elongation and repression of spurious transcription initiation through regulation of histone acetylation. Essential for proper mitosis progression (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96N64}.
Interaction partners:
Sequence:
MAAVAAEAAATAASPGEGGAGEAEPELEPIPGSEAGTPLPVTATEAAVPDGEADGRQSAPQADEQPLPPPPPPPPPGELADSSEAEEAKPPEPAAVPVSPPEQPPAAPEQPEDAPRPPPAPALVPPAGGDSAVSHLIPGSEVRVTLDHIIEDALVVSFRLGEKLFSGVLMDLSKRFGPHGIPVTVFPKREYKDKPDAMQLQSTTFQEGIEVKQEVNGAVPDDLSPVPPPERLWASKPPPLFHEGAPYPPPLFIRDTYNQSIPQPPPRKIKRPKRKMYREEPTSIMNAIKLRPRQVLCDKCKNSVVAEKKEIRKGSSDSSRYEDKKRRNDSVATVNKKLKTDHKVDGKNQNESQRRNTVVRVSSIAHSRGRVVKVSAQANTSKAQLNTKKVLQSKNMDHAKAREVLKIAKEKAQKKQSETSTSKTAHAKVHFTRRYQSPSSGSLPPRVRLKPQRYRNEENDSSLKTGLEKIRSGKLAPKPQSRCTSTRSAGEAPSEKPSPSEGPEESAGEVQDTSRVRVPGEQEELRMLGKKGSKSSISVYLTLNQETSDSSSASVCSIDSMDDLKSSNSECSSSESFVFPPGCMHAPSASSTSTSFSSKEENSLRNSLKMKIFSKNVSKCITPDGRTICVGDIVWAKIYGFPWWPARILTITVSRKDNGLLARQEARISWFASPTTSSLALSQLSPFLENFQLRFNKKRKGLYRRAITEAAKAAKQLTPEVRALLTQFET
Protein: Transcription initiation factor TFIID subunit 11 (TFIID subunit p30-beta) (Transcription initiation factor TFIID 28 kDa subunit) (TAF(II)28) (TAFII-28) (TAFII28) (Q99JX1)
Organism: Mus musculus (Mouse)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF11, together with TAF13 and TBP, play key roles during promoter binding by the TFIID and TFIIA transcription factor complexes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 13
- TATA-box-binding protein
- TATA-box binding protein associated factor 4
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 8
Sequence:
MDNLGESPTDKGGEPGESEETRATPGALVAADTEGIPEETDRDGDADLKEAAAEESELKSQDVSDVTAAERENSSLLTPAAKKLKLDIKDKKEKKQKVDEDEIQKMQILVSSFSEEQLNRYEMYRRSAFPKAAIKRLIQSITGTSVSQNVVIAMSGISKVFVGEVVEEALDVCEKWGETPPLQPKHMREAVRRLKSKGQIPNSKHKKITFF
Protein: Heterogeneous nuclear ribonucleoprotein A0 (B5X3U2)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
- Serine/arginine-rich splicing factor 2
- Serine/arginine-rich splicing factor 2
- Serine/arginine-rich splicing factor 2
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein K
- Nuclear cap-binding protein subunit 2
- small monomeric GTPase
- small monomeric GTPase
Sequence:
MENQLCKLFIGGLNVHTTDGGLRKHFEQYGQLTDCVVVQNQQLQRSRCFGFVTYATADEADAAMSARPHALDGNNVELKRAVAREDAGKPEALAKVKKIFIGGLKEDIEDEHLSEYFSQFGTIEKAEVISDNQTGKKRGFGFVYFEDYDSADKAVVLKFHHINGHKVEVKKALTKQEMQAAGTRGGRGGRFQNGYGGGYGGGYGGSDGGYGVGYSGGYGGSYGDQMGGYGGNGYSDFGGGYSEQSSNYGPMKGNYSGRSSAPYTRGGGGYGRGGYDGAY
Protein: Probable protein phosphatase 2C 23 (AtPP2C23) (EC 3.1.3.16) (Protein POLTERGEIST-LIKE 4) (Protein phosphatase 2C PLL4) (PP2C PLL4) (Q9ZV25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in leaf development regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Putative high mobility group B protein 11
- F-box protein At5g18160
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 9
- Protein phosphatase 2C 70
- MA3 DOMAIN-CONTAINING TRANSLATION REGULATORY FACTOR 1
- Probable alkaline/neutral invertase F
- MA3 DOMAIN-CONTAINING TRANSLATION REGULATORY FACTOR 2
Sequence:
MGNGIGKLSKCLTGGAGRNKKPELSILEPDPLDEGLGHSFCYVRPDPTRVSSSKVHSEEETTTFRTISGASVSANTATPLSTSLYDPYGHIDRAAAFESTTSFSSIPLQPIPRSSGPIVPGSGPLERGFLSGPIERGFMSGPLDGSSGPIDGKTGSDQFQRSFSHGLANLRVGSRKGSLVRVLRRAISKTITRGQNSIVAPIKPVKEPDWVFGSDKTRIHQIENNLTVNSLNFSSEGSLLDDDVSLESQNLQWAQGKAGEDRVHVVVSEEHGWLFVGIYDGFNGPDAPDYLLSHLYPAVHRELKGLLWDDPKTDAKSSDEADVENRDSSSEKKSKNWEESQRRWRCEWDRDLDRLLKDRSNGLDLDPDPNSSDVLKALSQALRKTEEAYLENADMMLDENPELALMGSCVLVMLMKGEDVYLMNVGDSRAVLGQKAESDYWIGKIKQDLERINEETMNDFDGCGDGEGASLVPTLSAFQLTVDHSTNVEEEVNRIRKEHPDDASAVSNERVKGSLKVTRAFGAGFLKQPKWNNALLEMFQIDYKGTSPYINCLPSLYHHRLGSKDQFLILSSDGLYQYFTNEEAVSEVELFITLQPEGDPAQHLVQELLFRAAKKAGMDFHELLEIPQGERRRYHDDVSIVVISLEGRMWKSCV
Protein: Nuclear envelope pore membrane protein POM 121C (Nuclear pore membrane protein 121-2) (POM121-2) (Pore membrane protein of 121 kDa C) (A8CG34)
Organism: Homo sapiens (Human)
Function: Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL).
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:17900573}. Nucleus membrane {ECO:0000269|PubMed:17900573}; Single-pass membrane protein {ECO:0000269|PubMed:17900573}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Stably associated with the NPC throughout interphase and the endoplasmic reticulum during metaphase. {ECO:0000250}.
Interaction partners:
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup205
- Nuclear pore complex protein Nup107
- Nuclear envelope pore membrane protein POM 121
- Nuclear pore complex protein Nup93
- Importin subunit beta-1
- Nuclear pore complex protein Nup155
- POM121-like protein 2
- Nucleoporin SEH1
- Nuclear pore complex protein Nup214
Sequence:
MSPAAAAAGAGERRRPIASVRDGRGRGCGGPAGAALLGLSLVGLLLYLVPAAAALAWLAVGTTAAWWGLSREPRGSRPLSSFVQKARHRRTLFASPPAKSTANGNLLEPRTLLEGPDPAELLLMGSYLGKPGPPQPAPAPEGQDLRNRPGRRPPARPAPRSTPPSQPTHRVHHFYPSLPTPLLRPSGRPSPRDRGTLPDRFVITPRRRYPIHQTQYSCPGVLPTVCWNGYHKKAVLSPRNSRMVCSPVTVRIAPPDRRFSRSAIPEQIISSTLSSPSSNAPDPCAKETVLSALKEKKKKRTVEEEDQIFLDGQENKRRRHDSSGSGHSAFEPLVASGVPASFVPKPGSLKRGLNSQSSDDHLNKRSRSSSMSSLTGAYTSGIPSSSRNAITSSYSSTRGISQLWKRNGPSSSPFSSPASSRSQTPERPAKKIREEELCHHSSSSTPLAADKESQGEKAADTTPRKKQNSNSQSTPGSSGQRKRKVQLLPSRRGEQLTLPPPPQLGYSITAEDLDLEKKASLQWFNQALEDKSDAASNSVTETPPTTQPSFTFTLPAAATASPPTSLLAPSTNPLLESLKKMQTPPSLPPCPESAGAATTEALSPPKTPSLLPPLGLSQSGPPGLLPSPSFDSKPPTTLLGLIPAPSMVPATDTKAPPTLQAETATKPQATSAPSPAPKQSFLFGTQNTSPSSPAAPAASSASPMFKPIFTAPPKSEKEGLTPPGPSVSATAPSSSSLPTTTSTTAPTFQPVFSSMGPPASVPLPAPFFKQTTTPATAPTTTAPLFTGLASATSAVAPITSASPSTDSASKPAFGFGINSVSSSSVSTTTSTATAASQPFLFGAPQASAASFTPAMGSIFQFGKPPALPTTTTVTTFSQSLPTAVPTATSSSAADFSGFGSTLATSAPATSSQPTLTFSNTSTPTFNIPFGSSAKSPLPSYPGANPQPAFGAAEGQPPGAAKPALTPSFGSSFTFGNSAAPAPATAPTPAPASTIKIVPAHVPTPIQPTFGGATHSAFGLKATASAFGAPASSQPAFGGSTAVFSFGAATSSGFGATTQTASSGSSSSVFGSTTPSPFTFGGSAAPAGSGSFGINVATPGSSATTGAFSFGAGQSGSTATSTPFTGGLGQNALGTTGQSTPFAFNVGSTTESKPVFGGTATPTFGQNTPAPGVGTSGSSLSFGASSAPAQGFVGVGPFGSAAPSFSIGAGSKTPGARQRLQARRQHTRKK
Protein: GSK3B-interacting protein (GSKIP) (GSK3beta interaction protein) (Q9P0R6)
Organism: Homo sapiens (Human)
Function: A-kinase anchoring protein for GSK3B and PKA that regulates or facilitates their kinase activity towards their targets. The ternary complex enhances Wnt-induced signaling by facilitating the GSK3B- and PKA-induced phosphorylation of beta-catenin leading to beta-catenin degradation and stabilization respectively. Upon cAMP activation, the ternary complex contributes to neuroprotection against oxidative stress-induced apoptosis by facilitating the PKA-induced phosphorylation of DML1 and PKA-induced inactivation of GSK3B. During neurite outgrowth promotes neuron proliferation; while increases beta-catenin-induced transcriptional activity through GSK3B kinase activity inhibition, reduces N-cadherin level to promote cell cycle progression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16981698, ECO:0000269|PubMed:20007971}. Nucleus {ECO:0000269|PubMed:20007971}.
Interaction partners:
- Glycogen synthase kinase-3 beta
- Glycogen synthase kinase-3 alpha
- Autophagy-related protein 2 homolog B
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
Sequence:
METDCNPMELSSMSGFEEGSELNGFEGTDMKDMRLEAEAVVNDVLFAVNNMFVSKSLRCADDVAYINVETKERNRYCLELTEAGLKVVGYAFDQVDDHLQTPYHETVYSLLDTLSPAYREAFGNALLQRLEALKRDGQS
Protein: Vesicle-associated membrane protein 7 (Synaptobrevin-like protein 1) (Q7JYX5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, phagosome membrane {ECO:0000256|ARBA:ARBA00037875}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00037875}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000256|ARBA:ARBA00037803}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00037803}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004163}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00037801}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00037801}. Late endosome membrane {ECO:0000256|ARBA:ARBA00037845}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00037845}. Lysosome membrane {ECO:0000256|ARBA:ARBA00037863}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00037863}.
Interaction partners:
- LD03592p
- Syntaxin 17, isoform B
- LD23667p
- LD27967p
- Syntaxin-4
- Syntaxin 8
- Syntaxin-1A
- BET1 homolog
- Syntaxin-5
- LD34211p
Sequence:
MPILYSVISRGTTVLAKFAECVGNFAEVTEHIIGRIGVHNHKMTYTHGDYLIHYTCENKLVYMCITDNEFERSRAFLFLADIKQKFIQTYGLQVATAIAYSMNTEFSKILAQQMVYFSQSREVDTISRVHGQIDELKDIMVKNIDSLRDRGEKLELLVNKTENLSNNSVAFRKASRNLARQMFWKNIRVYVVVGLVITFIVYVIVSMACGGLAWQSCV
Protein: Swollenin, putative (EC 3.-.-.-) (Q4WD28)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Extracellular cellulase CelA/allergen Asp F7-like, putative
Sequence:
MTLLFGIFLARLAVAAAQSSCVSAWGQCGGISYTGSTCCQSGNTCAEINSYYYQCIPATAVSTSTTTVTSPSSSGSSSANTSGYTTTTVLPSPTATQNPYPPANASSCGSWALVDNVCCPYYCLSDNESESCTSSCTGGCGSPDSSMCKSGTMWGEQHTVTSNEDWHYSRSTHFGLTSGGACGFGLYGLCTKNSVTASWTDPMLGSTCDAFCTAYPLLCKDPANVTLRGNFAAPNGDYYTQFWPSLAASGNPDNYLSCGECFEVIRTKPDGTDYAVGESGYTDPIVLEVVDSCPCNANSKWCCKRPPPPPFFSPPSNGQNLTRPGGSGADHCGEIDFKYGCPLPEGSHHMDLSDIAMGRLQGNGSLADGVIPIRYRRVPCPKPGNIYIWLHDGAGPYYFALSAVNTNGPGSVISIEVQAGGSGPWVALEHDPNYTSSRPQERYGSWVLPQGKGPITVPVSMRLTAPNGQQVVKEGAITSYTPPATAVEGFWYIDLGVQFT
Protein: Cytochrome b-c1 complex subunit 2, mitochondrial (J9VPD8)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07257}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07257}; Matrix side {ECO:0000250|UniProtKB:P07257}.
Interaction partners:
Sequence:
MYSLNRLPRSAAFKSSANLLRRNASTTSAGGVNVVGFENKGPAATSSLTVAIKAGSRYETTPGVAHVLKSFAYKATASASALRTAREAELYGGVLSAALTREHLLLSAEFLRGDEEHFLNVLASVLSSSQFYRHELSELVLPVVEAETISSQAIPSTIALDLAHSLAFRRGLGNSLYANKNYPVSIDDVKSFGEAAFAKSNIAVIGTGVSTEALAKAVSNAFGAGTSSGSKLSTPKANYYGGETRVPLDIHAPATATPTMVIAFGTSSPASADLKVLKHLLGGETSVKWTPGASPLAQAADKIPGASAKAFLLPYSDAALFGVVLSAPTSAETKTLAQEVASIVKNAGEFKEEEVKRAVAKATFEDAASTETLSGFVAAAGPAALVGSVPEAQSFSGVSASSISKAAGELLKGKPTVVSIGNISVLPYADELGL
Protein: Centromere protein P (CENP-P) (Q6IPU0)
Organism: Homo sapiens (Human)
Function: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:16622420}. Chromosome, centromere {ECO:0000269|PubMed:16622420}. Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex.
Interaction partners:
- Centromere protein U
- Centromere protein Q
- Centromere protein R
- Centromere protein H
- Centromere protein O
- Centromere protein N
- Centromere protein I
- Centromere protein K
- Centromere protein M
- Centromere protein L
Sequence:
MDAELAEVRALQAEIAALRRACEDPPAPWEEKSRVQKSFQAIHQFNLEGWKSSKDLKNQLGHLESELSFLSTLTGINIRNHSKQTEDLTSTEMTEKSIRKVLQRHRLSGNCHMVTFQLEFQILEIQNKERLSSAVTDLNIIMEPTECSELSEFVSRAEERKDLFMFFRSLHFFVEWFEYRKRTFKHLKEKYPDAVYLSEGPSSCSMGIRSASRPGFELVIVWRIQIDEDGKVFPKLDLLTKVPQRALELDKNRAIETAPLSFRTLVGLLGIEAALESLIKSLCAEENN
Protein: Ubiquitin-like protein ATG12 (Autophagy-related protein 12) (APG12-like) (O94817)
Organism: Homo sapiens (Human)
Function: Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes.
Subcellular location: Cytoplasm {ECO:0000250}. Preautophagosomal structure membrane {ECO:0000269|PubMed:22342342}; Peripheral membrane protein {ECO:0000269|PubMed:22342342}. Note=TECPR1 recruits the ATG12-ATG5 conjugate to the autolysosomal membrane.
Interaction partners:
- GABA type A receptor associated protein like 1
- Ubiquitin-like-conjugating enzyme ATG3
- Antiviral innate immune response receptor RIG-I
- Ubiquitin-like-conjugating enzyme ATG10
- Mitochondrial antiviral-signaling protein
- Autophagy protein 5
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy-related protein 16-1
- WD repeat domain phosphoinositide-interacting protein 2
Sequence:
MAEEPQSVLQLPTSIAAGGEGLTDVSPETTTPEPPSSAAVSPGTEEPAGDTKKKIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHYCKSQAWG
Protein: tRNA-dihydrouridine synthase B (EC 1.3.1.-) (P0ABT5)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
Interaction partners:
- DNA-binding protein Fis
- Ribosomal protein L11 methyltransferase
- Biotin carboxylase
- Uncharacterized membrane protein YhdT
- Sodium/pantothenate symporter
- Ribonuclease P protein component
- Small ribosomal subunit protein bS20
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein bS21
- Ribosome maturation factor RimM
Sequence:
MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSDPKEMADAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDVVKSILTEVVNAVDVPVTLKIRTGWAPEHRNCEEIAQLAEDCGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENFA
Protein: Testis-specific serine/threonine-protein kinase 1 (TSK-1) (TSK1) (TSSK-1) (Testis-specific kinase 1) (EC 2.7.11.1) (Serine/threonine-protein kinase 22A) (Q61241)
Organism: Mus musculus (Mouse)
Function: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-281' of TSKS. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.
Subcellular location: Cytoplasm. Cytoplasmic vesicle, secretory vesicle, acrosome. Cell projection, cilium, flagellum. Note=In spermatozoa, present in the sperm head and in the flagellum.
Interaction partners:
Sequence:
MDDAAVLKRRGYIMGINLGEGSYAKVKSAYSERLKFNVAVKIIDRKKAPSDFLEKFLPREIEILAMLNHRSIVKTYEIFETSDGKVYIVMELGVQGDLLEFIKTRGALQEDDARKKFHQLSSAIKYCHDLDVVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDDSGRLILSKTFCGSAAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYRMLQPDVNRRLHIDEILNHCWVQPKARGLSSGAINKEGESSRATEPSWIPEPGADKKSATKLEPREEARSEARSESKPQEDTLQVVRQSENVGLSSELNRDTEEGHPQQPSETHT
Protein: C-X-C motif chemokine 17 (6-Cys CXCL17) (13.6 kDa protein) (VEGF coregulated chemokine 1) [Cleaved into: 4-Cys CXCL17] (Q5UW37)
Organism: Mus musculus (Mouse)
Function: Chemokine that acts as chemoattractant for monocytes, macrophages and dendritic cells. Plays a role in angiogenesis and possibly in the development of tumors. Acts as an anti-inflammatory in the stomach. May play a role in the innate defense against infections. Activates the C-X-C chemokine receptor GPR35 to induce a rapid and transient rise in the level of intracellular calcium ions.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q6UXB2}.
Interaction partners:
- C-C motif chemokine 25
- C-X-C motif chemokine 14
- C-X-C motif chemokine 10
- C-C motif chemokine
- C-X-C motif chemokine 9
- C-C motif chemokine 28
- C-C motif chemokine 2
- C-C motif chemokine 5
- C-C motif chemokine ligand 26
- G-protein coupled receptor 35
Sequence:
MKLLASPFLLLLPVMLMSMVFSSPNPGVARSHGDQHLAPRRWLLEGGQECECKDWFLQAPKRKATAVLGPPRKQCPCDHVKGREKKNRHQKHHRKSQRPSRACQQFLKRCHLASFALPL
Protein: Arylamine N-acetyltransferase 2 (EC 2.3.1.5) (Arylamide acetylase 2) (N-acetyltransferase type 2) (NAT-2) (N-hydroxyarylamine O-acetyltransferase) (EC 2.3.1.118) (P50295)
Organism: Mus musculus (Mouse)
Function: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. 2-aminofluorene and p-aminobenzoic acid (PABA) are preferred substrates for NAT-2. Less activity with anisidine and barely detectable with SMZ.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2E1
- Xanthine dehydrogenase/oxidase
- Arylamine N-acetyltransferase 1
- Carboxylesterase 1C
- Carboxylesterase 1E
- Carboxylesterase 1F
- Carboxylesterase 1D
- Arylamine N-acetyltransferase 3
- Myeloperoxidase
Sequence:
MDIEAYFERIGYQSTRSKLDLKTLTEILQHQIRAIPFENLNIHCGESMELSLEAIFDQIVRKKRGGWCLQVNHLLYWALTKLGFETTMLGGYVFNTPANKYSSGMIHLLVQVTISGKDYIVDAGFGRSYQMWEPLELTSGKDQPQVPAIFRLTEENGTWYLDQIRREQYVPNQEFINSDLLEKNKYRKIYSFTLEPRTIEDFESMNTYLQTSPASVFTSKSFCSLQTPEGVHCLVGSTLTYRRFSYKDNVDLVEFKSLTEEEIEDVLRTIFGVSLERKLVPKHGDRFFTI