Reviewed, UniProtKB/Swiss-Prot O15504 (NUPL2_HUMAN)

Names and origin

Protein names

Recommended name:
    Nucleoporin-like 2
Alternative name(s):
    NLP-1
      Short name=hCG1
    NUP42 homolog

Gene names

Name:	NUPL2
Synonyms:	CG1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for the export of mRNAs containing poly(A) tails from the nucleus into the cytoplasm. In case of infection by HIV-1, it may participate in the docking of viral Vpr at the nuclear envelope. Ref.7 Ref.10
Subunit structure	Probable component of the nuclear pore complex (NPC). Interacts with nuclear export protein NXF1. Interacts with GLE1. Able to form a heterotrimer with NUP155 and GLE1 in vitro. Interacts with the HIV-1 virus proteins Rev and Vpr. The interaction with HIV-1 Rev, a protein that mediates nuclear export of unspliced viral RNAs, suggests that its function may be bypassed by the HIV-1 virus. Ref.10 Ref.6 Ref.8 Ref.9
Subcellular location	Nucleus › nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note: Excluded from the nucleolus. Ref.10 Ref.8 Ref.9
Tissue specificity	Ubiquitously expressed. Ref.8
Domain	The FG repeats are interaction sites for karyopherins (importins, exportins) and form probably an affinity gradient, guiding the transport proteins unidirectionally with their cargo through the NPC By similarity.
Post-translational modification	O-glycosylated. Ref.8
Sequence similarities	Contains 1 C3H1-type zinc finger.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Membrane Nuclear pore complex Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	intracellular protein transmembrane transport Inferred from electronic annotation. Source: UniProtKB-KW mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW protein export from nucleus Ref.8 Traceable author statement. Source: ProtInc
Cellular component	cytosol Ref.9 Inferred from Experiment. Source: Reactome nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	nuclear export signal receptor activity Ref.8 Traceable author statement. Source: ProtInc nucleic acid binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O15504-1)

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: O15504-2)

The sequence of this isoform differs from the canonical sequence as follows:
     204-224: LSDVKDGVNQAAPAFGFGSSQ → KCLWKIYTHLSPKIYGPDCAL
     225-423: Missing.

Isoform 3 (identifier: O15504-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-228: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 423	423	Nucleoporin-like 2		PRO_0000204895
Regions
	Repeat	14 – 15	2	FG 1
	Repeat	95 – 96	2	FG 2
	Repeat	218 – 219	2	FG 3
	Repeat	220 – 221	2	FG 4
	Repeat	265 – 266	2	FG 5
	Repeat	271 – 272	2	FG 6
	Repeat	288 – 289	2	FG 7
	Repeat	290 – 291	2	FG 8
	Repeat	311 – 312	2	FG 9
	Repeat	336 – 337	2	FG 10
	Repeat	345 – 346	2	FG 11
	Repeat	364 – 365	2	FG 12
	Zinc finger	1 – 25	25	C3H1-type
	Region	94 – 170	77	Interaction with HIV-1 Vpr
	Region	365 – 423	59	Interaction with GLE1
	Compositional bias	238 – 378	141	Ser-rich
Natural variations
	Alternative sequence	1 – 228	228	Missing in isoform 3.		VSP_016480
	Alternative sequence	204 – 224	21	LSDVK…FGSSQ → KCLWKIYTHLSPKIYGPDCA L in isoform 2.		VSP_016481
	Alternative sequence	225 – 423	199	Missing in isoform 2.		VSP_016482
	Natural variant	391	1	D → N: dbSNP rs13243961.		VAR_050572
	Natural variant	392	1	K → N: dbSNP rs34902971.		VAR_050573

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 6F8B95073312E999	FASTA	423	44,872
	10 20 30 40 50 60 MAICQFFLQG RCRFGDRCWN EHPGARGAGG GRQQPQQQPS GNNRRGWNTT SQRYSNVIQP 70 80 90 100 110 120 SSFSKSTPWG GSRDQEKPYF SSFDSGASTN RKEGFGLSEN PFASLSPDEQ KDEKKLLEGI 130 140 150 160 170 180 VKDMEVWESS GQWMFSVYSP VKKKPNISGF TDISPEELRL EYHNFLTSNN LQSYLNSVQR 190 200 210 220 230 240 LINQWRNRVN ELKSLNISTK VALLSDVKDG VNQAAPAFGF GSSQAATFMS PGFPVNNSSS 250 260 270 280 290 300 DNAQNFSFKT NSGFAAASSG SPAGFGSSPA FGAAASTSSG ISTSAPAFGF GKPEVTSAAS 310 320 330 340 350 360 FSFKSPAASS FGSPGFSGLP ASLATGPVRA PVAPAFGGGS SVAGFGSPGS HSHTAFSKPS 370 380 390 400 410 420 SDTFGNSSIS TSLSASSSII ATDNVLFTPR DKLTVEELEQ FQSKKFTLGK IPLKPPPLEL LNV
	Isoform 2. Checksum: 2EBE880F1494052D	FASTA	224	25,542
	10 20 30 40 50 60 MAICQFFLQG RCRFGDRCWN EHPGARGAGG GRQQPQQQPS GNNRRGWNTT SQRYSNVIQP 70 80 90 100 110 120 SSFSKSTPWG GSRDQEKPYF SSFDSGASTN RKEGFGLSEN PFASLSPDEQ KDEKKLLEGI 130 140 150 160 170 180 VKDMEVWESS GQWMFSVYSP VKKKPNISGF TDISPEELRL EYHNFLTSNN LQSYLNSVQR 190 200 210 220 LINQWRNRVN ELKSLNISTK VALKCLWKIY THLSPKIYGP DCAL
	Isoform 3. Checksum: 90FAD1990293952F	FASTA	195	19,312
	10 20 30 40 50 60 MSPGFPVNNS SSDNAQNFSF KTNSGFAAAS SGSPAGFGSS PAFGAAASTS SGISTSAPAF 70 80 90 100 110 120 GFGKPEVTSA ASFSFKSPAA SSFGSPGFSG LPASLATGPV RAPVAPAFGG GSSVAGFGSP 130 140 150 160 170 180 GSHSHTAFSK PSSDTFGNSS ISTSLSASSS IIATDNVLFT PRDKLTVEEL EQFQSKKFTL 190 GKIPLKPPPL ELLNV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Refined mapping of a gene for autosomal dominant progressive sensorineural hearing loss (DFNA5) to a 2-cM region, and exclusion of a candidate gene that is expressed in the cochlea." Van Laer L., Van Camp G., van Zuylen D., Green E.D., Verstreken M., Schatteman I., Van de Heyning P., Balemans W., Coucke P., Greinwald J.H., Smith R.J.H., Huizing E., Willems P. Eur. J. Hum. Genet. 5:397-405(1997) [PubMed: 9450185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed: 12690205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Testis and Urinary bladder.
[6]	"The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human." Katahira J., Straesser K., Podtelejnikov A., Mann M., Jung J.U., Hurt E. EMBO J. 18:2593-2609(1999) [PubMed: 10228171] [Abstract] Cited for: INTERACTION WITH NXF1.
[7]	"The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr255p." Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M., Stutz F. EMBO J. 18:5761-5777(1999) [PubMed: 10610322] [Abstract] Cited for: FUNCTION.
[8]	"A new nucleoporin-like protein interacts with both HIV-1 Rev nuclear export signal and CRM-1." Farjot G., Sergeant A., Mikaelian I. J. Biol. Chem. 274:17309-17317(1999) [PubMed: 10358091] [Abstract] Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, INTERACTION WITH XPO1 AND HIV-1 VIRUS REV PROTEIN.
[9]	"Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1." Le Rouzic E., Mousnier A., Rustum C., Stutz F., Hallberg E., Dargemont C., Benichou S. J. Biol. Chem. 277:45091-45098(2002) [PubMed: 12228227] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH HIV-1 VIRUS VPR PROTEIN.
[10]	"Interaction between the shuttling mRNA export factor Gle1 and the nucleoporin hCG1: a conserved mechanism in the export of Hsp70 mRNA." Kendirgi F., Rexer D.J., Alcazar-Roman A.R., Onishko H.M., Wente S.R. Mol. Biol. Cell 16:4304-4315(2005) [PubMed: 16000379] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GLE1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U97198 mRNA. Translation: AAC33794.1. BT007409 mRNA. Translation: AAP36077.1. AK298183 mRNA. Translation: BAG60454.1. CH236948 Genomic DNA. Translation: EAL24260.1. BC005327 mRNA. Translation: AAH05327.1. BC039333 mRNA. Translation: AAH39333.1.
IPI	IPI00010654. IPI00187080. IPI00477209.
RefSeq	NP_031368.1.
UniGene	Hs.408241
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	O15504.
Proteomic databases
PRIDE	O15504.
Genome annotation databases
Ensembl	ENSG00000136243. Homo sapiens. [Contig view]
GeneID	11097.
KEGG	hsa:11097.
Organism-specific databases
GeneCards	GC07P023188.
H-InvDB	HIX0006518.
HGNC	HGNC:17010. NUPL2.
PharmGKB	PA134990469.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O15504.
HOVERGEN	O15504.
OMA	O15504. RCWNEHP.
Enzyme and pathway databases
Reactome	REACT_6185. HIV Infection.
Gene expression databases
ArrayExpress	O15504.
Bgee	O15504.
CleanEx	HS_NUPL2.
GermOnline	ENSG00000136243. Homo sapiens.
Family and domain databases
InterPro	IPR000571. Znf_CCCH. [Graphical view]
Pfam	PF00642. zf-CCCH. 1 hit. [Graphical view]
PROSITE	PS50103. ZF_C3H1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	42186.

Entry information

Entry name

NUPL2_HUMAN

Accession

Primary (citable) accession number: O15504
Secondary accession number(s): A4D143 , B4DP42, Q49AE7, Q9BS49

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)