wanglab/gogpt-training-data huggingface dataset:
Protein: Bestrophin-1 (TU15B) (Vitelliform macular dystrophy protein 2) (O76090)
Organism: Homo sapiens (Human)
Function: Forms calcium-sensitive chloride channels. Highly permeable to bicarbonate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26200502}; Multi-pass membrane protein {ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:35789156}. Basolateral cell membrane {ECO:0000269|PubMed:19853238, ECO:0000269|PubMed:21330666, ECO:0000269|PubMed:26200502}; Multi-pass membrane protein {ECO:0000269|PubMed:17110374, ECO:0000269|PubMed:35789156}. Note=Localized at the surface membrane of microdomains adjacent to glutamatergic synapses. {ECO:0000250|UniProtKB:O88870}.
Interaction partners:
- Retinoid isomerohydrolase
- Peripherin-2
- Myelin regulatory factor
- Retinal-specific phospholipid-transporting ATPase ABCA4
- Cone-rod homeobox protein
- Retinaldehyde-binding protein 1
- Interphotoreceptor matrix proteoglycan 2
- X-linked retinitis pigmentosa GTPase regulator
- Protein eyes shut homolog
- U4/U6 small nuclear ribonucleoprotein Prp31
Sequence:
MTITYTSQVANARLGSFSRLLLCWRGSIYKLLYGEFLIFLLCYYIIRFIYRLALTEEQQLMFEKLTLYCDSYIQLIPISFVLGFYVTLVVTRWWNQYENLPWPDRLMSLVSGFVEGKDEQGRLLRRTLIRYANLGNVLILRSVSTAVYKRFPSAQHLVQAGFMTPAEHKQLEKLSLPHNMFWVPWVWFANLSMKAWLGGRIRDPILLQSLLNEMNTLRTQCGHLYAYDWISIPLVYTQVVTVAVYSFFLTCLVGRQFLNPAKAYPGHELDLVVPVFTFLQFFFYVGWLKVAEQLINPFGEDDDDFETNWIVDRNLQVSLLAVDEMHQDLPRMEPDMYWNKPEPQPPYTAASAQFRRASFMGSTFNISLNKEEMEFQPNQEDEEDAHAGIIGRFLGLQSHDHHPPRANSRTKLLWPKRESLLHEGLPKNHKAAKQNVRGQEDNKAWKLKAVDAFKSAPLYQRPGYYSAPQTPLSPTPMFFPLEPSAPSKLHSVTGIDTKDKSLKTVSSGAKKSFELLSESDGALMEHPEVSQVRRKTVEFNLTDMPEIPENHLKEPLEQSPTNIHTTLKDHMDPYWALENRDEAHS
Protein: AT5g40270/MSN9_170 (HD domain-containing metal-dependent phosphohydrolase family protein) (Similarity to intracellular protein) (Q9FL05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DDB1- and CUL4-associated factor homolog 1
Sequence:
MGAYCDENLSSLPVFSSGAPANELRFSKHVYDNVHGNIYLDPLCLKFIDTEQFQRLRELKQLGVTNMVYPGAVHSRFEHSLGVYWLAGETAQRLKNFQGMELGIDNYDLQTVRLAGLLHDIGHGPFSHMFEREFLPKVISDCQWSHELMSVNMIDHMVDTHHIDIDAQMLKRVKDMILASTEFSQLKGNAEKRFLYDIVANGRNGIDVDKFDYLVRDSRACGLGSNFQFQRLTETMRVLDNEICFRAKEYLSVHKLFATRADLYRTVYTHSKVKAIELMIVDAMVKANNHLEISSMINDPSEYWKLDDTILKTIEIAPDPELAEAKELILRVRRRQLYQFCNEYAVPKDKIDHFKAVTPQDIICSQKHTSLTLKEEDIAVTNVKIDLARGRENPLECINFYKDYDSAEKFVIPEDRVSHLLPTTYQDMIVRVYAKKPELVEAVSEAFENFQMRTYGIKAQVHATPEKKKRRVM
Protein: FCP1 homology domain-containing protein (Q57ZA0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNHDAMSFFQNISARLSTVRNCTKKPHCRREEEAQPQQPIALPKQSSTPPPLISSVAPPTQSVVNEKAASTPVVLPSRVQPTVSARWSGPEAEVPESAARPRRNRTPCPPVKHRGEKSEEELRQVSSIIMTQAQEPASKSVRTGAAASLVEAYRCVNSIRDTGEPPGERTDDVTNINGSGDNDDGGNTKQARAKLYENAVSEQVRRIQKMPKNTSPVNAKNHASLLPRQLPRFRDKITLILDLDETLVHSSLTSQSRHHDLVLDVRMENTSTTVYVAFRPFMREFLQAVAPLFEVIIFTASVSVYCNQLMDAIDTDNILGSLRLYREHCSILNGAYVKDLSLLGRDLDRVAIIDNSPVAYLFQQRNAIPIPSWFDDPGDNELQQLIPMLEILAAESEVYTVLDQYNAVLHLQQEQARQNSPHY
Protein: Programmed cell death 1 ligand 2 (PD-1 ligand 2) (PD-L2) (PDCD1 ligand 2) (Programmed death ligand 2) (Butyrophilin B7-DC) (B7-DC) (CD antigen CD273) (Q9BQ51)
Organism: Homo sapiens (Human)
Function: Involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production (By similarity).
Subcellular location: [Isoform 3]: Secreted {ECO:0000305|PubMed:15253154}.; SUBCELLULAR LOCATION: [Isoform 2]: Endomembrane system {ECO:0000269|PubMed:15253154}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:15253154}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9WUL5, ECO:0000305|PubMed:15340161}.
Interaction partners:
- Programmed cell death protein 1
- Cytotoxic T-lymphocyte protein 4
- Programmed cell death 1 ligand 1
- T-lymphocyte activation antigen CD80
- T-cell-specific surface glycoprotein CD28
- Repulsive guidance molecule B
- Inducible T-cell costimulator
- T-lymphocyte activation antigen CD86
- T-cell surface glycoprotein CD4
- V-set domain-containing T-cell activation inhibitor 1
Sequence:
MIFLLLMLSLELQLHQIAALFTVTVPKELYIIEHGSNVTLECNFDTGSHVNLGAITASLQKVENDTSPHRERATLLEEQLPLGKASFHIPQVQVRDEGQYQCIIIYGVAWDYKYLTLKVKASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQSQMEPRTHPTWLLHIFIPFCIIAFIFIATVIALRKQLCQKLYSSKDTTKRPVTTTKREVNSAI
Protein: Nuclear transcription factor Y subunit B-3 (AtNF-YB-3) (AtNF-YB3) (Transcriptional activator HAP3C) (O23310)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the NF-Y/HAP transcription factor complex (By similarity). The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters (By similarity). Promotes the expression of heat stress-inducible genes by contributing to the formation of a heat stress-specific transcriptional complex with NF-Y subunits (e.g. DPB3-1, NF-YA2 and NF-YB3) and DREB2A at the promoter of target genes, thus promoting heat tolerance.
Subcellular location: Nucleus {ECO:0000269|PubMed:25490919}. Cytoplasm, cytosol {ECO:0000269|PubMed:25490919}. Note=Present in both cytoplasm and nucleus under nonstress conditions but translocates in the nucleus upon heat stress. {ECO:0000269|PubMed:25490919}.
Interaction partners:
- Nuclear transcription factor Y subunit A-4
- Nuclear transcription factor Y subunit C-3
- Nuclear transcription factor Y subunit C-4
- Nuclear transcription factor Y subunit C-1
- Nuclear transcription factor Y subunit A-2
- Nuclear transcription factor Y subunit C-9
- Nuclear transcription factor Y subunit C-2
- DNA polymerase II subunit B3-1
- Nuclear transcription factor Y subunit A-3
- Nuclear transcription factor Y subunit A-1
Sequence:
MADSDNDSGGHKDGGNASTREQDRFLPIANVSRIMKKALPANAKISKDAKETVQECVSEFISFITGEASDKCQREKRKTINGDDLLWAMTTLGFEDYVEPLKVYLQKYREVEGEKTTTAGRQGDKEGGGGGGGAGSGSGGAPMYGGGMVTTMGHQFSHHFS
Protein: Mannose-binding protein C (MBP-C) (Mannan-binding protein) (RA-reactive factor P28A subunit) (RARF/P28A) (P41317)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Mannan-binding lectin serine protease 2
- Mannan-binding lectin serine protease 1
- Plasma protease C1 inhibitor
- Complement C4-B
- Anionic trypsin-2
- Ficolin-2
- Ficolin-1
- Mannose-binding protein A
- Calreticulin
- Complement C2
Sequence:
MSIFTSFLLLCVVTVVYAETLTEGVQNSCPVVTCSSPGLNGFPGKDGRDGAKGEKGEPGQGLRGLQGPPGKVGPTGPPGNPGLKGAVGPKGDRGDRAEFDTSEIDSEIAALRSELRALRNWVLFSLSEKVGKKYFVSSVKKMSLDRVKALCSEFQGSVATPRNAEENSAIQKVAKDIAYLGITDVRVEGSFEDLTGNRVRYTNWNDGEPNNTGDGEDCVVILGNGKWNDVPCSDSFLAICEFSD
Protein: Outer membrane porin N (Outer membrane protein N) (Porin OmpN) (P77747)
Organism: Escherichia coli (strain K12)
Function: Forms pores that allow passive diffusion of small molecules across the outer membrane (By similarity). Non-specific porin.
Subcellular location: Cell outer membrane; Multi-pass membrane protein.
Interaction partners:
- Outer membrane protein A
- Cell division protein ZapB
- Z-ring associated protein G
- Penicillin-binding protein activator LpoB
- Universal stress protein A
- Cell division protein FtsN
- DNA helicase IV
- Outer-membrane lipoprotein carrier protein
- Protein AsmA
- Murein DD-endopeptidase MepM
Sequence:
MKSKVLALLIPALLAAGAAHAAEVYNKDGNKLDLYGKVDGLHYFSDNSAKDGDQSYARLGFKGETQINDQLTGYGQWEYNIQANNTESSKNQSWTRLAFAGLKFADYGSFDYGRNYGVMYDIEGWTDMLPEFGGDSYTNADNFMTGRANGVATYRNTDFFGLVNGLNFAVQYQGNNEGASNGQEGTNNGRDVRHENGDGWGLSTTYDLGMGFSAGAAYTSSDRTNDQVNHTAAGGDKADAWTAGLKYDANNIYLATMYSETRNMTPFGDSDYAVANKTQNFEVTAQYQFDFGLRPAVSFLMSKGRDLHAAGGADNPAGVDDKDLVKYADIGATYYFNKNMSTYVDYKINLLDEDDSFYAANGISTDDIVALGLVYQF
Protein: Opsin, ultraviolet-sensitive (UV-sensitive opsin) (AmUVop) (BUVOPS) (O61303)
Organism: Apis mellifera (Honeybee)
Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to 11-cis-retinal.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Arrestin_C domain-containing protein.
Sequence:
MSNDSIHWEARYLPAGPPRLLGWNVPAEELIHIPEHWLVYPEPNPSLHYLLALLYILFTFLALLGNGLVIWIFCAAKSLRTPSNMFVVNLAICDFFMMIKTPIFIYNSFNTGFALGNLGCQIFAVIGSLTGIGAAITNAAIAYDRYSTIARPLDGKLSRGQVILFIVLIWTYTIPWALMPVMGVWGRFVPEGFLTSCSFDYLTDTNEIRIFVATIFTFSYCIPMILIIYYYSQIVSHVVNHEKALREQAKKMNVDSLRSNANTSSQSAEIRIAKAAITICFLYVLSWTPYGVMSMIGAFGNKALLTPGVTMIPACTCKAVACLDPYVYAISHPKYRLELQKRLPWLELQEKPISDSTSTTTETVNTPPASS
Protein: Eukaryotic translation initiation factor 3 subunit C (eIF3c) (Eukaryotic translation initiation factor 3 93 kDa subunit homolog) (eIF3 p93) (Translation initiation factor eIF3, p93 subunit homolog) (O14164)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit E
- Probable eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit H
- Probable eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit I
Sequence:
MSRFFKGGSSDSDAESVDSSEENRLTSSRLKKQDDSSSEEESSEEESASSSESESSEEESESEESEVEVPKKKAVAASEDSESDSESSEEEEETESEEDSEVSDESESESESESESEEESESEEESDESERSGPSSFLKKPEKEEAKPAGLKFLRGESSEESSDEEEGRRVVKSAKDKRYEEFISCMETIKNAMSSNNWIVVSNEFDHLNKVSQKCKEAGRNPPPYIEFLSALDQKLESADKAFIKSLDAANGRAFNALKQRVRKNNRQFQSDIDRYRKDPEGFMKPAELNEIPKPAGKAGQDEVIVDGVATRGIVAPTEGLGKPEEITPADIFKYLRAIFEARGKKSTDRSEQIRLLEKLSTIAVTDYQRLRVKVALLAVRFDINTGSGQYMPIDQWNAALTELHSILDIFDANPKIVIVEQVEDENEEEEEAIAAAENNNGVIQVQGSVVSFLERLDDEFTRSLQMIDPHTPEYIDRLKDETSLYTLLVRSQGYLERIGVVENTARLIMRRLDRVYYKPEQVIRANEEVAWRSFPPTFDLTITPRATTTTPDILIHSLCVYLYNNGVSLLRTRAMLCHIYHEALQNRFYKARDMLLMSHLQDSVHAADIATQILHNRTMVQIGLCAFRNGMVQETQYALQDISTTGRVKELLGQGIQAPKFGQFTPDQDRLDKQLVLPFHMHINLELLECVYLTCSMLMEIPAMAAASSTASDSRKRVISRPFRRMLEYIDRQLFVGPPENTREYIMQASKALADGEWRRCEEFIHAIKIWSLMPDADKIKQMLSEKIREEGLRTYLLAYAAFYDSVSLEFLATTFDLPVQRVTVIVSRLLSKREIHAALDQVHGAIIFERVEINKLESLTVSLSEKTAQLNEANEKLYEQKTQHTNPQENRRRDKGGSVKRRNERTENRNRSDMN
Protein: DDK kinase regulatory subunit DBF4 (Dumbbell forming protein 4) (P32325)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory subunit of the CDC7-DBF4 kinase, also called DBF4-dependent kinase (DDK), which is involved in cell cycle regulation of premitotic and premeiotic chromosome replication and in chromosome segregation. DDK plays an essential role in initiating DNA replication at replication origins by phosphorylating the MCM2 and MCM4 subunits of the MCM2-7 helicase complex. DBF4 recruits the catalytic subunit CDC7 to MCM2 and to origins of replication. DDK has also postreplicative functions in meiosis. DDK phosphorylates the meiosis-specific double-strand break protein MER2 for initiation of meiotic recombination. Interacts with CDC5 during meiosis to promote double-strand breaks and monopolar spindle orientation. Inhibits CDC5 activity during mitosis through direct binding to its PBD.
Interaction partners:
- DNA replication licensing factor MCM6
- Cell division control protein 7
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM2
- Minichromosome maintenance protein 5
- DNA replication licensing factor MCM3
- Origin recognition complex subunit 2
- DNA replication licensing factor MCM7
- Cell division control protein 45
- Serine/threonine-protein kinase RAD53
Sequence:
MVSPTKMIIRSPLKETDTNLKHNNGIAASTTAAGHLNVFSNDNNCNNNNTTESFPKKRSLERLELQQQQHLHEKKRARIERARSIEGAVQVSKGTGLKNVEPRVTPKELLEWQTNWKKIMKRDSRIYFDITDDVEMNTYNKSKMDKRRDLLKRGFLTLGAQITQFFDTTVTIVITRRSVENIYLLKDTDILSRAKKNYMKVWSYEKAARFLKNLDVDLDHLSKTKSASLAAPTLSNLLHNEKLYGPTDRDPRTKRDDIHYFKYPHVYLYDLWQTWAPIITLEWKPQELTNLDELPYPILKIGSFGRCPFIGDRNYDESSYKRVVKRYSRDKANKKYALQLRALFQYHADTLLNTSSVNDQTKNLIFIPHTCNDSTKSFKKWMQEKAKNFEKTELKKTDDSAVQDVRNEHADQTDEKNSILLNETETKEPPLKEEKENKQSIAEESNKYPQRKELAATPKLNHPVLATFARQETEEVPDDLCTLKTKSRQAFEIKASGAHQSNDVATSFGNGLGPTRASVMSKNMKSLSRLMVDRKLGVKQTNGNNKNYTATIATTAETSKENRHRLDFNALKKDEAPSKETGKDSAVHLETNRKPQNFPKVATKSVSADSKVHNDIKITTTESPTASKKSTSTNVTLHFNAQTAQTAQPVKKETVKNSGYCENCRVKYESLEQHIVSEKHLSFAENDLNFEAIDSLIENLRFQI
Protein: Voltage-gated delayed rectifier potassium channel KCNH5 (Ether-a-go-go potassium channel 2) (rEAG2) (Potassium voltage-gated channel subfamily H member 5) (Voltage-gated potassium channel subunit Kv10.2) (Q9EPI9)
Organism: Rattus norvegicus (Rat)
Function: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits a non-inactivating outward rectifying current. Channel properties may be modulated by cAMP and subunit assembly.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MPGGKRGLVAPQNTFLENIVRRSSESSFLLGNAQIVDWPVVYSNDGFCKLSGYHRADVMQKSSTCSFMYGELTDKKTIEKVRQTFDNYESNCFEVLLYKKNRTPVWFYMQIAPIRNEHEKVVLFLCTFKDITLFKQPIEDDSTKGWTKFARLTRALTNSRSVLQQLTPMNKTETVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCAFKTTWDWVILILTFYTAIMVPYNVSFKTKQNNIAWLVLDSVVDVIFLVDIVLNFHTTFVGPGGEVISDPKLIRMNYLKTWFVIDLLSCLPYDIINAFENVDEGISSLFSSLKVVRLLRLGRVARKLDHYLEYGAAVLVLLVCVFGLVAHWLACIWYSIGDYEVIDEVTNTIQIDSWLYQLALSIGTPYRYNTSAGIWEGGPSKDSLYVSSLYFTMTSLTTIGFGNIAPTTDVEKMFSVAMMMVGSLLYATIFGNVTTIFQQMYANTNRYHEMLNNVRDFLKLYQVPKGLSERVMDYIVSTWSMSKGIDTEKVLSICPKDMRADICVHLNRKVFNEHPAFRLASDGCLRALAVEFQTIHCAPGDLIYHAGESVDALCFVVSGSLEVIQDEEVVAILGKGDVFGDIFWKETTLAHACANVRALTYCDLHIIKREALLKVLDFYTAFANSFSRNLTLTCNLRKRIIFRKISDVKKEEEERLRQKNEVTLSIPVDHPVRKLFQKFKQQKELRNQGSAQSDPERSQLQVESRPLQNGASITGTSVVTVSQITPIQTSLAYVKTSETLKQNNRDAMELKPNGGAEPKCLKVNSPIRMKNGNGKGWLRLKNNMGAHEEKKEEWNNVTKAESMGLLSEDPKGSDSENSVTKNPLRKTDSCDSGITKSDLRLDKAGEARSPLEHSPSQADAKHPFYPIPEQALQTTLQEVKHELKEDIQLLSCRMTALEKQVAEILKLLSEKSVPQTSSPKPQIPLQVPPQIPCQDIFSVSRPESPESDKDEINF
Protein: Chordin (Q9H2X0)
Organism: Homo sapiens (Human)
Function: Dorsalizing factor. Key developmental protein that dorsalizes early vertebrate embryonic tissues by binding to ventralizing TGF-beta family bone morphogenetic proteins (BMPs) and sequestering them in latent complexes (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Bone morphogenetic protein 4
- Bone morphogenetic protein 2
- Bone morphogenetic protein 7
- Bone morphogenetic protein 1
- Bone morphogenetic protein 5
- Bone morphogenetic protein 6
- Growth/differentiation factor 5
- Growth/differentiation factor 7
- Twisted gastrulation protein homolog 1
- Growth/differentiation factor 6
Sequence:
MPSLPAPPAPLLLLGLLLLGSRPARGAGPEPPVLPIRSEKEPLPVRGAAGCTFGGKVYALDETWHPDLGEPFGVMRCVLCACEAPQWGRRTRGPGRVSCKNIKPECPTPACGQPRQLPGHCCQTCPQERSSSERQPSGLSFEYPRDPEHRSYSDRGEPGAEERARGDGHTDFVALLTGPRSQAVARARVSLLRSSLRFSISYRRLDRPTRIRFSDSNGSVLFEHPAAPTQDGLVCGVWRAVPRLSLRLLRAEQLHVALVTLTHPSGEVWGPLIRHRALAAETFSAILTLEGPPQQGVGGITLLTLSDTEDSLHFLLLFRGLLEPRSGGLTQVPLRLQILHQGQLLRELQANVSAQEPGFAEVLPNLTVQEMDWLVLGELQMALEWAGRPGLRISGHIAARKSCDVLQSVLCGADALIPVQTGAAGSASLTLLGNGSLIYQVQVVGTSSEVVAMTLETKPQRRDQRTVLCHMAGLQPGGHTAVGICPGLGARGAHMLLQNELFLNVGTKDFPDGELRGHVAALPYCGHSARHDTLPVPLAGALVLPPVKSQAAGHAWLSLDTHCHLHYEVLLAGLGGSEQGTVTAHLLGPPGTPGPRRLLKGFYGSEAQGVVKDLEPELLRHLAKGMASLMITTKGSPRGELRGQVHIANQCEVGGLRLEAAGAEGVRALGAPDTASAAPPVVPGLPALAPAKPGGPGRPRDPNTCFFEGQQRPHGARWAPNYDPLCSLCTCQRRTVICDPVVCPPPSCPHPVQAPDQCCPVCPEKQDVRDLPGLPRSRDPGEGCYFDGDRSWRAAGTRWHPVVPPFGLIKCAVCTCKGGTGEVHCEKVQCPRLACAQPVRVNPTDCCKQCPVGSGAHPQLGDPMQADGPRGCRFAGQWFPESQSWHPSVPPFGEMSCITCRCGAGVPHCERDDCSLPLSCGSGKESRCCSRCTAHRRPAPETRTDPELEKEAEGS
Protein: Uncharacterized protein (Q380Z5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHHIPISSNTFSPSRLVCSSAGVQRALAVNIVELMGNQESIKAQWERAAKRNNCRRDARDSIVVVFGKEPMETLATTGSKTDACGVVMQFLASSTTFMSSLRGTGLGARPCLRNGVRVEPKIEGQGDTREKDTVRADGIVAAWLLLDVVVLGAEFKHAMPVLYVQLAWDDLPKVDCVSAYRSALQVTRVALLFMPEPFQTRIHVDFTGVLSPEHNVPGLESVRMVWSGLVGSLLLTAAVAPKEAVVPPFHPAGDDDRRVQSTGENVVDQLKPGHNHCGVGETFCKEECVRQQGWACSDGDRNAVVSDWLSMLLKGNEETTAAFGRAVQRKNGTRSVPTVSLHPASLGAAATSDTHDNLGRGVGVNGFGGDCDDKPVVKREACFLPSNTAKEEIHEVQPLQLKTESDEEVIAEWVPNGTINRSSVGDPFPQVPVITDGAACLFLETPSNSHLFPISDDIALRQLCVSWTALSTERRDRQRLIVVVADGDHRFSEVLRSWVRTAWNENAFILPIFAVGDTSFCRRVDKELASISACVNSLTDTSRDIHHFVRILAFAVQYFRIDVKSSGCLSRTAAFSEAANHVGVHAAGDYNCVKEWVDKFNETVDSLTPSDRANFDVERERDRLFDELCGTSMLARDLRSQACRPEMLMKHVGTMRVGIARPTICDDVSLSSTYPPRFNPDARPKLFGSLSPAQRLRIYEFMSAFFTKNVFNASVDAVRSAAEGYFSDCHFQILGYGRFALACSVRRHLYVMVHMNLQPLLNEDVKIGAGDPHWSSVFQHLSCTCKPRAHERILKTETGQKRCRHLAQSVYWLLQDIADDPHYALRMPVGAVRGADCHSRGVAHCHFTFNSSLCSKNMREDIPKPLGPPRKRHHFERNGDISITQLSALTEESDQFDVTVLELATNSRLASWLGVGS
Protein: Clathrin heavy chain 1 (Q68FD5)
Organism: Mus musculus (Mouse)
Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension. Plays a role in early autophagosome formation.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Melanosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q00610}. Note=Cytoplasmic face of coated pits and vesicles. In complex with TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges in mitotic spindles. {ECO:0000250, ECO:0000250|UniProtKB:Q00610}.
Interaction partners:
- AP-2 complex subunit beta
- Clathrin light chain B
- Clathrin light chain A
- Cyclin-G-associated kinase
- Auxilin
- AP-2 complex subunit alpha-1
- AP-2 complex subunit mu
- Epidermal growth factor receptor substrate 15
- AP-1 complex subunit gamma-1
- Epsin-1
Sequence:
MAQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSNPIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTVALVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVGAMQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGNQPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISGETIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRNNLAGAEELFARKFNALFAQGNYSEAAKVAANAPKGILRTPDTIRRFQSVPAQPGQTSPLLQYFGILLDQGQLNKYESLELCRPVLQQGRKQLLEKWLKEDKLECSEELGDLVKSVDPTLALSVYLRANVPNKVIQCFAETGQVQKIVLYAKKVGYTPDWIFLLRNVMRISPDQGQQFAQMLVQDEEPLADITQIVDVFMEYNLIQQCTAFLLDALKNNRPSEGPLQTRLLEMNLMHAPQVADAILGNQMFTHYDRAHIAQLCEKAGLLQRALEHFTDLYDIKRAVVHTHLLNPEWLVNYFGSLSVEDSLECLRAMLSANIRQNLQICVQVASKYHEQLSTQSLIELFESFKSFEGLFYFLGSIVNFSQDPDVHFKYIQAACKTGQIKEVERICRESNCYDPERVKNFLKEAKLTDQLPLIIVCDRFDFVHDLVLYLYRNNLQKYIEIYVQKVNPSRLPVVIGGLLDVDCSEDVIKNLILVVRGQFSTDELVAEVEKRNRLKLLLPWLEARIHEGCEEPATHNALAKIYIDSNNNPERFLRENPYYDSRVVGKYCEKRDPHLACVAYERGQCDLELINVCNENSLFKSLSRYLVRRKDPELWGSVLLESNPYRRPLIDQVVQTALSETQDPEEVSVTVKAFMTADLPNELIELLEKIVLDNSVFSEHRNLQNLLILTAIKADRTRVMEYINRLDNYDAPDIANIAISNELFEEAFAIFRKFDVNTSAVQVLIEHIGNLDRAYEFAERCNEPAVWSQLAKAQLQKGMVKEAIDSYIKADDPSSYMEVVQAANASGNWEELVKYLQMARKKARESYVETELIFALAKTNRLAELEEFINGPNNAHIQQVGDRCYDEKMYDAAKLLYNNVSNFGRLASTLVHLGEYQAAVDGARKANSTRTWKEVCFACVDGKEFRLAQMCGLHIVVHADELEELINYYQDRGYFEELITMLEAALGLERAHMGMFTELAILYSKFKPQKMREHLELFWSRVNIPKVLRAAEQAHLWAELVFLYDKYEEYDNAIITMMNHPTDAWKEGQFKDIITKVANVELYYKAIQFYLEFKPLLLNDLLMVLSPRLDHTRAVNYFSKVKQLPLVKPYLRSVQNHNNKSVNESLNNLFITEEDYQALRTSIDAYDNFDNISLAQRLEKHELIEFRRIAAYLFKGNNRWKQSVELCKKDSLYKDAMQYASESKDTELAEELLQWFLQEEKRECFGACLFTCYDLLRPDVVLETAWRHNIMDFAMPYFIQVMKEYLTKVDKLDASESLRKEEEQATETQPIVYGQPQLMLTAGPSVAVPPQAPFGYGYTAPPYGQPQPGFGYSM
Protein: NifU-like protein C1709.19c (Q9UUB8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Iron-sulfur assembly protein 2
- Iron-sulfur assembly protein 1
- Probable cysteine desulfurase, mitochondrial
- Iron-sulfur cluster assembly factor IBA57
- Iron sulfur cluster assembly protein 1, mitochondrial
- Lipoyl synthase, mitochondrial
- GrpE protein homolog
- Frataxin homolog, mitochondrial
- Monothiol glutaredoxin-5
- Protein isd11
Sequence:
MLFPRVVPFQSLRTAFQKKTFLPVSSAGNVFTPRFQLQAIRSIWIRSEETPNENALKFLPGLDILPPTIGSCEFMRGQGTVNSPLAQKLFDIDGVDSIFFGKDFITVSKGAGTEWAQMKPEVFSVIMEHLSNGSPVLSEEPLKGASDTQILESDSQIVAMIKELIETSIRPSIQEDGGDVEFRGFDEKTGTVSLKLRGACRTCSSSAVTLKNGIQQMLKHYIPEVENVVQVLDPEEEVAIAEFEKFEQRINGNKQKADNK
Protein: Matrix metalloproteinase-25 (MMP-25) (EC 3.4.24.-) (Leukolysin) (Membrane-type matrix metalloproteinase 6) (MT-MMP 6) (MTMMP6) (Membrane-type-6 matrix metalloproteinase) (MT6-MMP) (MT6MMP) (Q9NPA2)
Organism: Homo sapiens (Human)
Function: May activate progelatinase A.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Metalloproteinase inhibitor 2
- Kallikrein-4
- Furin
- Hemopexin
- Enamelin
- Metalloproteinase inhibitor 1
Sequence:
MRLRLRLLALLLLLLAPPARAPKPSAQDVSLGVDWLTRYGYLPPPHPAQAQLQSPEKLRDAIKVMQRFAGLPETGRMDPGTVATMRKPRCSLPDVLGVAGLVRRRRRYALSGSVWKKRTLTWRVRSFPQSSQLSQETVRVLMSYALMAWGMESGLTFHEVDSPQGQEPDILIDFARAFHQDSYPFDGLGGTLAHAFFPGEHPISGDTHFDDEETWTFGSKDGEGTDLFAVAVHEFGHALGLGHSSAPNSIMRPFYQGPVGDPDKYRLSQDDRDGLQQLYGKAPQTPYDKPTRKPLAPPPQPPASPTHSPSFPIPDRCEGNFDAIANIRGETFFFKGPWFWRLQPSGQLVSPRPARLHRFWEGLPAQVRVVQAAYARHRDGRILLFSGPQFWVFQDRQLEGGARPLTELGLPPGEEVDAVFSWPQNGKTYLVRGRQYWRYDEAAARPDPGYPRDLSLWEGAPPSPDDVTVSNAGDTYFFKGAHYWRFPKNSIKTEPDAPQPMGPNWLDCPAPSSGPRAPRPPKATPVSETCDCQCELNQAAGRWPAPIPLLLLPLLVGGVASR