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Q13564 (ULA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 534533NEDD8-activating enzyme E1 regulatory subunit
PRO_0000194951

Regions

Region331 – 34414Interaction with UBA3

Sites

Site2111Interaction with UBA3

Amino acid modifications

Modified residue21N-acetylalanine Ref.15 Ref.17
Modified residue61N6-acetyllysine Ref.15
Modified residue3411N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 8989Missing in isoform 3.
VSP_054258
Alternative sequence1 – 1717MAQLG…YDRQL → MDAQQTKTNEA in isoform 2.
VSP_042895
Alternative sequence531G → GNVG in isoform 4.
VSP_054259
Natural variant1011S → F.
Corresponds to variant rs363212 [ dbSNP | Ensembl ].
VAR_052435

Experimental info

Mutagenesis3311D → A: Impairs the formation of the NEDD8-UBA3 thioester. Ref.19
Sequence conflict2681A → V in BAG53511. Ref.3
Sequence conflict2851I → T in BAG53511. Ref.3

Secondary structure

........................................................................................... 534
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5EC8D3ACE6374F21

FASTA53460,246
        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 

« Hide

Isoform 2 [UniParc].

Checksum: F3732BF1F365C633
Show »

FASTA52859,420
Isoform 3 [UniParc].

Checksum: 0E6DF500733F61E6
Show »

FASTA44550,624
Isoform 4 [UniParc].

Checksum: 9F3D01503E29A668
Show »

FASTA53760,517

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_001018169.1. NM_001018159.1.
NP_001018170.1. NM_001018160.1.
NP_001273429.1. NM_001286500.1.
NP_003896.1. NM_003905.3.
UniGeneHs.460978.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ13564.
SMRQ13564. Positions 6-534.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114402. 32 interactions.
IntActQ13564. 6 interactions.
MINTMINT-1429663.
STRING9606.ENSP00000290810.

Chemistry

ChEMBLCHEMBL2016431.
DrugBankDB00171. Adenosine triphosphate.

PTM databases

PhosphoSiteQ13564.

Polymorphism databases

DMDM50400302.

Proteomic databases

PaxDbQ13564.
PRIDEQ13564.

Protocols and materials databases

DNASU8883.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290810; ENSP00000290810; ENSG00000159593. [Q13564-1]
ENST00000359087; ENSP00000351990; ENSG00000159593.
ENST00000379463; ENSP00000368776; ENSG00000159593. [Q13564-2]
ENST00000394074; ENSP00000377637; ENSG00000159593.
GeneID8883.
KEGGhsa:8883.
UCSCuc002eqe.3. human. [Q13564-2]
uc002eqf.3. human. [Q13564-1]

Organism-specific databases

CTD8883.
GeneCardsGC16M066836.
HGNCHGNC:621. NAE1.
HPAHPA041178.
HPA042041.
MIM603385. gene.
neXtProtNX_Q13564.
PharmGKBPA162396730.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0476.
HOGENOMHOG000216537.
HOVERGENHBG079761.
KOK04532.
OMATNQYVPI.
PhylomeDBQ13564.
TreeFamTF313972.

Enzyme and pathway databases

UniPathwayUPA00885.

Gene expression databases

ArrayExpressQ13564.
BgeeQ13564.
CleanExHS_NAE1.
GenevestigatorQ13564.

Family and domain databases

Gene3D3.40.50.720. 3 hits.
InterProIPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PfamPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMSSF69572. SSF69572. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNAE1. human.
EvolutionaryTraceQ13564.
GeneWikiAPPBP1.
GenomeRNAi8883.
NextBio33357.
PROQ13564.
SOURCESearch...

Entry information

Entry nameULA1_HUMAN
AccessionPrimary (citable) accession number: Q13564
Secondary accession number(s): A6NCK0 expand/collapse secondary AC list , 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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM