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Q13564

- ULA1_HUMAN

UniProt

Q13564 - ULA1_HUMAN

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Protein

NEDD8-activating enzyme E1 regulatory subunit

Gene

NAE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation.3 Publications

Enzyme regulationi

Binding of TP53BP2 to the regulatory subunit NAE1 decreases neddylation activity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei211 – 2111Interaction with UBA3

GO - Molecular functioni

  1. catalytic activity Source: InterPro
  2. protein heterodimerization activity Source: UniProtKB
  3. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. mitotic DNA replication checkpoint Source: UniProtKB
  2. neuron apoptotic process Source: UniProtKB
  3. protein neddylation Source: UniProtKB
  4. regulation of apoptotic process Source: UniProtKB
  5. regulation of neuron apoptotic process Source: UniProtKB
  6. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00885.

Names & Taxonomyi

Protein namesi
Recommended name:
NEDD8-activating enzyme E1 regulatory subunit
Alternative name(s):
Amyloid beta precursor protein-binding protein 1, 59 kDa
Short name:
APP-BP1
Amyloid protein-binding protein 1
Proto-oncogene protein 1
Gene namesi
Name:NAE1
Synonyms:APPBP1
ORF Names:HPP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:621. NAE1.

Subcellular locationi

Cell membrane 1 Publication
Note: Colocalizes with APP in lipid rafts.

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: RefGenome
  3. nucleus Source: RefGenome
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi331 – 3311D → A: Impairs the formation of the NEDD8-UBA3 thioester. 1 Publication

Organism-specific databases

PharmGKBiPA162396730.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 534533NEDD8-activating enzyme E1 regulatory subunitPRO_0000194951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei6 – 61N6-acetyllysine1 Publication
Modified residuei341 – 3411N6-acetyllysineBy similarity

Post-translational modificationi

Ubiquitinated by TRIP12, leading to its degradation by the proteasome.1 Publication

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

MaxQBiQ13564.
PaxDbiQ13564.
PRIDEiQ13564.

PTM databases

PhosphoSiteiQ13564.

Expressioni

Tissue specificityi

Ubiquitous in fetal tissues. Expressed throughout the adult brain.1 Publication

Gene expression databases

BgeeiQ13564.
CleanExiHS_NAE1.
ExpressionAtlasiQ13564. baseline and differential.
GenevestigatoriQ13564.

Organism-specific databases

HPAiHPA041178.
HPA042041.

Interactioni

Subunit structurei

Heterodimer of UBA3 and NAE1. The complex binds NEDD8 and UBE2M. Binds APP and TP53BP2.3 Publications

Protein-protein interaction databases

BioGridi114402. 33 interactions.
IntActiQ13564. 6 interactions.
MINTiMINT-1429663.
STRINGi9606.ENSP00000290810.

Structurei

Secondary structure

1
534
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1210
Helixi14 – 3017
Beta strandi32 – 365
Helixi40 – 5011
Turni51 – 533
Beta strandi55 – 606
Helixi67 – 726
Helixi78 – 803
Helixi85 – 9410
Beta strandi104 – 1074
Helixi109 – 1146
Helixi117 – 1226
Beta strandi124 – 1307
Helixi133 – 14513
Beta strandi150 – 1567
Beta strandi159 – 1657
Beta strandi169 – 1724
Beta strandi185 – 1873
Helixi190 – 1978
Beta strandi201 – 2044
Helixi209 – 2113
Helixi214 – 22512
Turni226 – 2294
Helixi236 – 24914
Beta strandi257 – 2593
Helixi262 – 27514
Helixi283 – 2897
Helixi292 – 2954
Beta strandi299 – 3013
Helixi303 – 31614
Turni317 – 3215
Helixi336 – 36631
Turni367 – 3693
Beta strandi372 – 3754
Helixi377 – 3859
Helixi387 – 3893
Beta strandi391 – 3933
Helixi398 – 4025
Turni404 – 4063
Helixi409 – 4157
Helixi423 – 43917
Turni447 – 4493
Helixi450 – 46718
Helixi476 – 4849
Turni485 – 4873
Helixi491 – 51020
Beta strandi520 – 5234
Turni524 – 5274
Beta strandi528 – 5314

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R4MX-ray3.00A/C/E/G1-534[»]
1R4NX-ray3.60A/C/E/G1-534[»]
1TT5X-ray2.60A/C1-534[»]
1YOVX-ray2.60A/C1-534[»]
2NVUX-ray2.80A1-534[»]
3DBHX-ray2.85A/C/E/G1-534[»]
3DBLX-ray2.90A/C/E/G1-534[»]
3DBRX-ray3.05A/C/E/G1-534[»]
3GZNX-ray3.00A/C1-534[»]
ProteinModelPortaliQ13564.
SMRiQ13564. Positions 6-534.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13564.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni331 – 34414Interaction with UBA3Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00550000074901.
HOGENOMiHOG000216537.
HOVERGENiHBG079761.
InParanoidiQ13564.
KOiK04532.
OMAiTNQYVPI.
PhylomeDBiQ13564.
TreeFamiTF313972.

Family and domain databases

Gene3Di3.40.50.720. 3 hits.
InterProiIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13564-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAQLGKLLKE QKYDRQLRLW GDHGQEALES AHVCLINATA TGTEILKNLV
60 70 80 90 100
LPGIGSFTII DGNQVSGEDA GNNFFLQRSS IGKNRAEAAM EFLQELNSDV
110 120 130 140 150
SGSFVEESPE NLLDNDPSFF CRFTVVVATQ LPESTSLRLA DVLWNSQIPL
160 170 180 190 200
LICRTYGLVG YMRIIIKEHP VIESHPDNAL EDLRLDKPFP ELREHFQSYD
210 220 230 240 250
LDHMEKKDHS HTPWIVIIAK YLAQWYSETN GRIPKTYKEK EDFRDLIRQG
260 270 280 290 300
ILKNENGAPE DEENFEEAIK NVNTALNTTQ IPSSIEDIFN DDRCINITKQ
310 320 330 340 350
TPSFWILARA LKEFVAKEGQ GNLPVRGTIP DMIADSGKYI KLQNVYREKA
360 370 380 390 400
KKDAAAVGNH VAKLLQSIGQ APESISEKEL KLLCSNSAFL RVVRCRSLAE
410 420 430 440 450
EYGLDTINKD EIISSMDNPD NEIVLYLMLR AVDRFHKQQG RYPGVSNYQV
460 470 480 490 500
EEDIGKLKSC LTGFLQEYGL SVMVKDDYVH EFCRYGAAEP HTIAAFLGGA
510 520 530
AAQEVIKIIT KQFVIFNNTY IYSGMSQTSA TFQL
Length:534
Mass (Da):60,246
Last modified:November 1, 1996 - v1
Checksum:i5EC8D3ACE6374F21
GO
Isoform 2 (identifier: Q13564-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MAQLGKLLKEQKYDRQL → MDAQQTKTNEA

Note: No experimental confirmation available.

Show »
Length:528
Mass (Da):59,420
Checksum:iF3732BF1F365C633
GO
Isoform 3 (identifier: Q13564-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.

Note: No experimental confirmation available.

Show »
Length:445
Mass (Da):50,624
Checksum:i0E6DF500733F61E6
GO
Isoform 4 (identifier: Q13564-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: G → GNVG

Show »
Length:537
Mass (Da):60,517
Checksum:i9F3D01503E29A668
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2681A → V in BAG53511. (PubMed:14702039)Curated
Sequence conflicti285 – 2851I → T in BAG53511. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011S → F.
Corresponds to variant rs363212 [ dbSNP | Ensembl ].
VAR_052435

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989Missing in isoform 3. CuratedVSP_054258Add
BLAST
Alternative sequencei1 – 1717MAQLG…YDRQL → MDAQQTKTNEA in isoform 2. 1 PublicationVSP_042895Add
BLAST
Alternative sequencei53 – 531G → GNVG in isoform 4. 1 PublicationVSP_054259

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U50939 mRNA. Translation: AAC50477.1.
AY197612 mRNA. Translation: AAP35030.1.
AK097680 mRNA. Translation: BAG53511.1.
AK298159 mRNA. Translation: BAH12735.1.
AK312784 mRNA. Translation: BAG35647.1.
AC004638 Genomic DNA. Translation: AAC23784.1.
AC044802 Genomic DNA. No translation available.
AL136798 mRNA. Translation: CAB66732.1.
CH471092 Genomic DNA. Translation: EAW83042.1.
BC000480 mRNA. Translation: AAH00480.1.
BC013301 mRNA. Translation: AAH13301.1.
CCDSiCCDS10820.1. [Q13564-1]
CCDS42171.1. [Q13564-2]
CCDS42172.1. [Q13564-3]
CCDS67050.1. [Q13564-4]
RefSeqiNP_001018169.1. NM_001018159.1. [Q13564-2]
NP_001018170.1. NM_001018160.1. [Q13564-3]
NP_001273429.1. NM_001286500.1. [Q13564-4]
NP_003896.1. NM_003905.3. [Q13564-1]
XP_005256272.1. XM_005256215.1. [Q13564-3]
UniGeneiHs.460978.

Genome annotation databases

EnsembliENST00000290810; ENSP00000290810; ENSG00000159593. [Q13564-1]
ENST00000359087; ENSP00000351990; ENSG00000159593. [Q13564-4]
ENST00000379463; ENSP00000368776; ENSG00000159593. [Q13564-2]
ENST00000394074; ENSP00000377637; ENSG00000159593. [Q13564-3]
GeneIDi8883.
KEGGihsa:8883.
UCSCiuc002eqe.3. human. [Q13564-2]
uc002eqf.3. human. [Q13564-1]

Polymorphism databases

DMDMi50400302.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U50939 mRNA. Translation: AAC50477.1 .
AY197612 mRNA. Translation: AAP35030.1 .
AK097680 mRNA. Translation: BAG53511.1 .
AK298159 mRNA. Translation: BAH12735.1 .
AK312784 mRNA. Translation: BAG35647.1 .
AC004638 Genomic DNA. Translation: AAC23784.1 .
AC044802 Genomic DNA. No translation available.
AL136798 mRNA. Translation: CAB66732.1 .
CH471092 Genomic DNA. Translation: EAW83042.1 .
BC000480 mRNA. Translation: AAH00480.1 .
BC013301 mRNA. Translation: AAH13301.1 .
CCDSi CCDS10820.1. [Q13564-1 ]
CCDS42171.1. [Q13564-2 ]
CCDS42172.1. [Q13564-3 ]
CCDS67050.1. [Q13564-4 ]
RefSeqi NP_001018169.1. NM_001018159.1. [Q13564-2 ]
NP_001018170.1. NM_001018160.1. [Q13564-3 ]
NP_001273429.1. NM_001286500.1. [Q13564-4 ]
NP_003896.1. NM_003905.3. [Q13564-1 ]
XP_005256272.1. XM_005256215.1. [Q13564-3 ]
UniGenei Hs.460978.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1R4M X-ray 3.00 A/C/E/G 1-534 [» ]
1R4N X-ray 3.60 A/C/E/G 1-534 [» ]
1TT5 X-ray 2.60 A/C 1-534 [» ]
1YOV X-ray 2.60 A/C 1-534 [» ]
2NVU X-ray 2.80 A 1-534 [» ]
3DBH X-ray 2.85 A/C/E/G 1-534 [» ]
3DBL X-ray 2.90 A/C/E/G 1-534 [» ]
3DBR X-ray 3.05 A/C/E/G 1-534 [» ]
3GZN X-ray 3.00 A/C 1-534 [» ]
ProteinModelPortali Q13564.
SMRi Q13564. Positions 6-534.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114402. 33 interactions.
IntActi Q13564. 6 interactions.
MINTi MINT-1429663.
STRINGi 9606.ENSP00000290810.

Chemistry

ChEMBLi CHEMBL2016431.
DrugBanki DB00171. Adenosine triphosphate.

PTM databases

PhosphoSitei Q13564.

Polymorphism databases

DMDMi 50400302.

Proteomic databases

MaxQBi Q13564.
PaxDbi Q13564.
PRIDEi Q13564.

Protocols and materials databases

DNASUi 8883.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290810 ; ENSP00000290810 ; ENSG00000159593 . [Q13564-1 ]
ENST00000359087 ; ENSP00000351990 ; ENSG00000159593 . [Q13564-4 ]
ENST00000379463 ; ENSP00000368776 ; ENSG00000159593 . [Q13564-2 ]
ENST00000394074 ; ENSP00000377637 ; ENSG00000159593 . [Q13564-3 ]
GeneIDi 8883.
KEGGi hsa:8883.
UCSCi uc002eqe.3. human. [Q13564-2 ]
uc002eqf.3. human. [Q13564-1 ]

Organism-specific databases

CTDi 8883.
GeneCardsi GC16M066836.
HGNCi HGNC:621. NAE1.
HPAi HPA041178.
HPA042041.
MIMi 603385. gene.
neXtProti NX_Q13564.
PharmGKBi PA162396730.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0476.
GeneTreei ENSGT00550000074901.
HOGENOMi HOG000216537.
HOVERGENi HBG079761.
InParanoidi Q13564.
KOi K04532.
OMAi TNQYVPI.
PhylomeDBi Q13564.
TreeFami TF313972.

Enzyme and pathway databases

UniPathwayi UPA00885 .

Miscellaneous databases

ChiTaRSi NAE1. human.
EvolutionaryTracei Q13564.
GeneWikii APPBP1.
GenomeRNAii 8883.
NextBioi 33357.
PROi Q13564.
SOURCEi Search...

Gene expression databases

Bgeei Q13564.
CleanExi HS_NAE1.
ExpressionAtlasi Q13564. baseline and differential.
Genevestigatori Q13564.

Family and domain databases

Gene3Di 3.40.50.720. 3 hits.
InterProi IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view ]
Pfami PF00899. ThiF. 1 hit.
[Graphical view ]
SUPFAMi SSF69572. SSF69572. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein."
    Chow N., Korenberg J.R., Chen X.-N., Neve R.L.
    J. Biol. Chem. 271:11339-11346(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH APP, TISSUE SPECIFICITY.
    Tissue: Fetal brain and Fetal skeletal muscle.
  2. "Identification of a new human protooncogene."
    Kim J.W.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  6. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle.
  9. "Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway."
    Gong L., Yeh E.T.H.
    J. Biol. Chem. 274:12036-12042(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The amyloid precursor protein-binding protein APP-BP1 drives the cell cycle through the S-M checkpoint and causes apoptosis in neurons."
    Chen Y., McPhie D.L., Hirschberg J., Neve R.L.
    J. Biol. Chem. 275:8929-8935(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBA3.
  11. "Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer."
    Bohnsack R.N., Haas A.L.
    J. Biol. Chem. 278:26823-26830(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBA3.
  12. "APP-BP1 mediates APP-induced apoptosis and DNA synthesis and is increased in Alzheimer's disease brain."
    Chen Y., Liu W., McPhie D.L., Hassinger L., Neve R.L.
    J. Cell Biol. 163:27-33(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APP, SUBCELLULAR LOCATION.
  13. "ASPP2 inhibits APP-BP1-mediated NEDD8 conjugation to cullin-1 and decreases APP-BP1-induced cell proliferation and neuronal apoptosis."
    Chen Y., Liu W., Naumovski L., Neve R.L.
    J. Neurochem. 85:801-809(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TP53BP2.
  14. "TRIP12 functions as an E3 ubiquitin ligase of APP-BP1."
    Park Y., Yoon S.K., Yoon J.B.
    Biochem. Biophys. Res. Commun. 374:294-298(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1."
    Walden H., Podgorski M.S., Huang D.T., Miller D.W., Howard R.J., Minor D.L. Jr., Holton J.M., Schulman B.A.
    Mol. Cell 12:1427-1437(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 5-534 IN COMPLEX WITH UBA3; NEDD8 AND ATP.
  19. "Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8."
    Walden H., Podgorski M.S., Schulman B.A.
    Nature 422:330-334(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 5-534 IN COMPLEX WITH UBA3, MUTAGENESIS OF ASP-331.
  20. "A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8."
    Huang D.T., Miller D.W., Mathew R., Cassell R., Holton J.M., Roussel M.F., Schulman B.A.
    Nat. Struct. Mol. Biol. 11:927-935(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH UBA3 AND UBE2M.

Entry informationi

Entry nameiULA1_HUMAN
AccessioniPrimary (citable) accession number: Q13564
Secondary accession number(s): A6NCK0
, A6NFN4, A8MU28, B2R700, B3KUP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

NAE1 and UBA3 correspond to the N-terminal and the C-terminal part of yeast UBA3. In yeast the two subunits form a single polypeptide chain.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3