Q13564 (ULA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NAE1
Synonyms:	APPBP1
ORF Names:	HPP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	534 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.9 Ref.10 Ref.11
Enzyme regulation	Binding of TP53BP2 to the regulatory subunit NAE1 decreases neddylation activity.
Pathway	Protein modification; protein neddylation.
Subunit structure	Heterodimer of UBA3 and NAE1. The complex binds NEDD8 and UBE2M. Binds APP and TP53BP2.
Subcellular location	Cell membrane. Note: Colocalizes with APP in lipid rafts. Ref.12
Tissue specificity	Ubiquitous in fetal tissues. Expressed throughout the adult brain. Ref.1
Post-translational modification	Ubiquitinated by TRIP12, leading to its degradation by the proteasome. Ref.14
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.
Sequence similarities	Belongs to the ubiquitin-activating E1 family. ULA1 subfamily.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Ubl conjugation pathway
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitotic DNA replication checkpoint Inferred from direct assay Ref.10. Source: UniProtKB neuron apoptotic process Inferred from direct assay Ref.12. Source: UniProtKB protein neddylation Inferred from direct assay Ref.9Ref.11. Source: UniProtKB regulation of apoptotic process Inferred from direct assay Ref.12. Source: UniProtKB regulation of neuron apoptotic process Inferred from direct assay Ref.10. Source: UniProtKB signal transduction Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Traceable author statement Ref.1. Source: ProtInc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	catalytic activity Inferred from electronic annotation. Source: InterPro protein heterodimerization activity Inferred from physical interaction Ref.11. Source: UniProtKB ubiquitin protein ligase binding Inferred from physical interaction Ref.14. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13564-1)

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.

Isoform 2 (identifier: Q13564-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: Q13564-3)

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

Note: No experimental confirmation available.

Isoform 4 (identifier: Q13564-4)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.15

Chain

2 – 534

533

NEDD8-activating enzyme E1 regulatory subunit

PRO_0000194951

Regions

Region

331 – 344

14

Interaction with UBA3

Sites

Site

211

1

Interaction with UBA3

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.15 Ref.17

Modified residue

6

1

N6-acetyllysine Ref.15

Modified residue

341

1

N6-acetyllysine By similarity

Natural variations

Alternative sequence

1 – 89

89

Missing in isoform 3.

VSP_054258

Alternative sequence

1 – 17

17

MAQLG…YDRQL → MDAQQTKTNEA in isoform 2.

VSP_042895

Alternative sequence

53

1

G → GNVG in isoform 4.

VSP_054259

Natural variant

101

1

S → F.
Corresponds to variant rs363212 [ dbSNP | Ensembl ].

VAR_052435

Experimental info

Mutagenesis

331

1

D → A: Impairs the formation of the NEDD8-UBA3 thioester. Ref.19

Sequence conflict

268

1

A → V in BAG53511. Ref.3

Sequence conflict

285

1

I → T in BAG53511. Ref.3

Secondary structure

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534

Helix Strand Turn

Details...

Helix

3 – 12

10

Helix

14 – 30

17

Beta strand

32 – 36

5

Helix

40 – 50

11

Turn

51 – 53

3

Beta strand

55 – 60

6

Helix

67 – 72

6

Helix

78 – 80

3

Helix

85 – 94

10

Beta strand

104 – 107

4

Helix

109 – 114

6

Helix

117 – 122

6

Beta strand

124 – 130

7

Helix

133 – 145

13

Beta strand

150 – 156

7

Beta strand

159 – 165

7

Beta strand

169 – 172

4

Beta strand

185 – 187

3

Helix

190 – 197

8

Beta strand

201 – 204

4

Helix

209 – 211

3

Helix

214 – 225

12

Turn

226 – 229

4

Helix

236 – 249

14

Beta strand

257 – 259

3

Helix

262 – 275

14

Helix

283 – 289

7

Helix

292 – 295

4

Beta strand

299 – 301

3

Helix

303 – 316

14

Turn

317 – 321

5

Helix

336 – 366

31

Turn

367 – 369

3

Beta strand

372 – 375

4

Helix

377 – 385

9

Helix

387 – 389

3

Beta strand

391 – 393

3

Helix

398 – 402

5

Turn

404 – 406

3

Helix

409 – 415

7

Helix

423 – 439

17

Turn

447 – 449

3

Helix

450 – 467

18

Helix

476 – 484

9

Turn

485 – 487

3

Helix

491 – 510

20

Beta strand

520 – 523

4

Turn

524 – 527

4

Beta strand

528 – 531

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5EC8D3ACE6374F21	FASTA	534	60,246
	10 20 30 40 50 60 MAQLGKLLKE QKYDRQLRLW GDHGQEALES AHVCLINATA TGTEILKNLV LPGIGSFTII 70 80 90 100 110 120 DGNQVSGEDA GNNFFLQRSS IGKNRAEAAM EFLQELNSDV SGSFVEESPE NLLDNDPSFF 130 140 150 160 170 180 CRFTVVVATQ LPESTSLRLA DVLWNSQIPL LICRTYGLVG YMRIIIKEHP VIESHPDNAL 190 200 210 220 230 240 EDLRLDKPFP ELREHFQSYD LDHMEKKDHS HTPWIVIIAK YLAQWYSETN GRIPKTYKEK 250 260 270 280 290 300 EDFRDLIRQG ILKNENGAPE DEENFEEAIK NVNTALNTTQ IPSSIEDIFN DDRCINITKQ 310 320 330 340 350 360 TPSFWILARA LKEFVAKEGQ GNLPVRGTIP DMIADSGKYI KLQNVYREKA KKDAAAVGNH 370 380 390 400 410 420 VAKLLQSIGQ APESISEKEL KLLCSNSAFL RVVRCRSLAE EYGLDTINKD EIISSMDNPD 430 440 450 460 470 480 NEIVLYLMLR AVDRFHKQQG RYPGVSNYQV EEDIGKLKSC LTGFLQEYGL SVMVKDDYVH 490 500 510 520 530 EFCRYGAAEP HTIAAFLGGA AAQEVIKIIT KQFVIFNNTY IYSGMSQTSA TFQL
	Isoform 2 [UniParc]. Checksum: F3732BF1F365C633	FASTA	528	59,420
	10 20 30 40 50 60 MDAQQTKTNE ARLWGDHGQE ALESAHVCLI NATATGTEIL KNLVLPGIGS FTIIDGNQVS 70 80 90 100 110 120 GEDAGNNFFL QRSSIGKNRA EAAMEFLQEL NSDVSGSFVE ESPENLLDND PSFFCRFTVV 130 140 150 160 170 180 VATQLPESTS LRLADVLWNS QIPLLICRTY GLVGYMRIII KEHPVIESHP DNALEDLRLD 190 200 210 220 230 240 KPFPELREHF QSYDLDHMEK KDHSHTPWIV IIAKYLAQWY SETNGRIPKT YKEKEDFRDL 250 260 270 280 290 300 IRQGILKNEN GAPEDEENFE EAIKNVNTAL NTTQIPSSIE DIFNDDRCIN ITKQTPSFWI 310 320 330 340 350 360 LARALKEFVA KEGQGNLPVR GTIPDMIADS GKYIKLQNVY REKAKKDAAA VGNHVAKLLQ 370 380 390 400 410 420 SIGQAPESIS EKELKLLCSN SAFLRVVRCR SLAEEYGLDT INKDEIISSM DNPDNEIVLY 430 440 450 460 470 480 LMLRAVDRFH KQQGRYPGVS NYQVEEDIGK LKSCLTGFLQ EYGLSVMVKD DYVHEFCRYG 490 500 510 520 AAEPHTIAAF LGGAAAQEVI KIITKQFVIF NNTYIYSGMS QTSATFQL
	Isoform 3 [UniParc]. Checksum: 0E6DF500733F61E6	FASTA	445	50,624
	10 20 30 40 50 60 MEFLQELNSD VSGSFVEESP ENLLDNDPSF FCRFTVVVAT QLPESTSLRL ADVLWNSQIP 70 80 90 100 110 120 LLICRTYGLV GYMRIIIKEH PVIESHPDNA LEDLRLDKPF PELREHFQSY DLDHMEKKDH 130 140 150 160 170 180 SHTPWIVIIA KYLAQWYSET NGRIPKTYKE KEDFRDLIRQ GILKNENGAP EDEENFEEAI 190 200 210 220 230 240 KNVNTALNTT QIPSSIEDIF NDDRCINITK QTPSFWILAR ALKEFVAKEG QGNLPVRGTI 250 260 270 280 290 300 PDMIADSGKY IKLQNVYREK AKKDAAAVGN HVAKLLQSIG QAPESISEKE LKLLCSNSAF 310 320 330 340 350 360 LRVVRCRSLA EEYGLDTINK DEIISSMDNP DNEIVLYLML RAVDRFHKQQ GRYPGVSNYQ 370 380 390 400 410 420 VEEDIGKLKS CLTGFLQEYG LSVMVKDDYV HEFCRYGAAE PHTIAAFLGG AAAQEVIKII 430 440 TKQFVIFNNT YIYSGMSQTS ATFQL
	Isoform 4 [UniParc]. Checksum: 9F3D01503E29A668	FASTA	537	60,517
	10 20 30 40 50 60 MAQLGKLLKE QKYDRQLRLW GDHGQEALES AHVCLINATA TGTEILKNLV LPGNVGIGSF 70 80 90 100 110 120 TIIDGNQVSG EDAGNNFFLQ RSSIGKNRAE AAMEFLQELN SDVSGSFVEE SPENLLDNDP 130 140 150 160 170 180 SFFCRFTVVV ATQLPESTSL RLADVLWNSQ IPLLICRTYG LVGYMRIIIK EHPVIESHPD 190 200 210 220 230 240 NALEDLRLDK PFPELREHFQ SYDLDHMEKK DHSHTPWIVI IAKYLAQWYS ETNGRIPKTY 250 260 270 280 290 300 KEKEDFRDLI RQGILKNENG APEDEENFEE AIKNVNTALN TTQIPSSIED IFNDDRCINI 310 320 330 340 350 360 TKQTPSFWIL ARALKEFVAK EGQGNLPVRG TIPDMIADSG KYIKLQNVYR EKAKKDAAAV 370 380 390 400 410 420 GNHVAKLLQS IGQAPESISE KELKLLCSNS AFLRVVRCRS LAEEYGLDTI NKDEIISSMD 430 440 450 460 470 480 NPDNEIVLYL MLRAVDRFHK QQGRYPGVSN YQVEEDIGKL KSCLTGFLQE YGLSVMVKDD 490 500 510 520 530 YVHEFCRYGA AEPHTIAAFL GGAAAQEVIK IITKQFVIFN NTYIYSGMSQ TSATFQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q." Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D. Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

RefSeq

NP_001018169.1. NM_001018159.1.
NP_001018170.1. NM_001018160.1.
NP_001273429.1. NM_001286500.1.
NP_003896.1. NM_003905.3.

UniGene

Hs.460978.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q13564.

SMR

Q13564. Positions 6-534.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

114402. 32 interactions.

IntAct

Q13564. 6 interactions.

MINT

MINT-1429663.

STRING

9606.ENSP00000290810.

Chemistry

ChEMBL

CHEMBL2016431.

DrugBank

DB00171. Adenosine triphosphate.

PTM databases

PhosphoSite

Q13564.

Polymorphism databases

DMDM

50400302.

Proteomic databases

PaxDb

Q13564.

PRIDE

Q13564.

Protocols and materials databases

DNASU

8883.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000290810; ENSP00000290810; ENSG00000159593. [Q13564-1]
ENST00000359087; ENSP00000351990; ENSG00000159593.
ENST00000379463; ENSP00000368776; ENSG00000159593. [Q13564-2]
ENST00000394074; ENSP00000377637; ENSG00000159593.

GeneID

8883.

KEGG

hsa:8883.

UCSC

uc002eqe.3. human. [Q13564-2]
uc002eqf.3. human. [Q13564-1]

Organism-specific databases

CTD

8883.

GeneCards

GC16M066836.

HGNC

HGNC:621. NAE1.

HPA

HPA041178.
HPA042041.

MIM

603385. gene.

neXtProt

NX_Q13564.

PharmGKB

PA162396730.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0476.

HOGENOM

HOG000216537.

HOVERGEN

HBG079761.

KO

K04532.

OMA

TNQYVPI.

PhylomeDB

Q13564.

TreeFam

TF313972.

Enzyme and pathway databases

UniPathway

UPA00885.

Gene expression databases

ArrayExpress

Q13564.

Bgee

Q13564.

CleanEx

HS_NAE1.

Genevestigator

Q13564.

Family and domain databases

Gene3D

3.40.50.720. 3 hits.

InterPro

IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]

Pfam

PF00899. ThiF. 1 hit.
[Graphical view]

SUPFAM

SSF69572. SSF69572. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

NAE1. human.

EvolutionaryTrace

Q13564.

GeneWiki

APPBP1.

GenomeRNAi

8883.

NextBio

33357.

PRO

Q13564.

SOURCE

Search...

Entry information

Entry name

ULA1_HUMAN

Accession

Primary (citable) accession number: Q13564
Secondary accession number(s): A6NCK0 , A6NFN4, A8MU28, B2R700, B3KUP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	November 1, 1996
Last modified:	April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.