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Protein

Nucleoporin-62 C-terminal-like protein

Gene

NUP62CL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoporin-62 C-terminal-like protein
Gene namesi
Name:NUP62CL
Synonyms:NUP62L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:25960. NUP62CL.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA145148360.

Polymorphism and mutation databases

BioMutaiNUP62CL.
DMDMi317373409.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 184184Nucleoporin-62 C-terminal-like proteinPRO_0000257834Add
BLAST

Proteomic databases

PaxDbiQ9H1M0.

Expressioni

Gene expression databases

BgeeiQ9H1M0.
CleanExiHS_NUP62CL.
ExpressionAtlasiQ9H1M0. baseline and differential.
GenevisibleiQ9H1M0. HS.

Organism-specific databases

HPAiHPA001884.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AGR2O959943EBI-751933,EBI-712648
OGTO152944EBI-751933,EBI-539828

Protein-protein interaction databases

BioGridi120184. 9 interactions.
IntActiQ9H1M0. 2 interactions.
MINTiMINT-1482653.
STRINGi9606.ENSP00000361544.

Structurei

3D structure databases

ProteinModelPortaliQ9H1M0.
SMRiQ9H1M0. Positions 105-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili117 – 15135Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 4333Thr-richAdd
BLAST

Sequence similaritiesi

Belongs to the nucleoporin NSP1/NUP62 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2196. Eukaryota.
ENOG410XT5X. LUCA.
GeneTreeiENSGT00730000111010.
HOGENOMiHOG000171766.
HOVERGENiHBG082003.
InParanoidiQ9H1M0.
OrthoDBiEOG7PZRZB.
PhylomeDBiQ9H1M0.

Family and domain databases

InterProiIPR026010. NSP1/NUP62.
IPR007758. Nucleoporin_NSP1_C.
[Graphical view]
PANTHERiPTHR12084. PTHR12084. 1 hit.
PfamiPF05064. Nsp1_C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H1M0-1) [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
MQFTSISNSL TSTAAIGLSF TTSTTTTATF TTNTTTTITS GFTVNQNQLL
60 70 80 90 100
SRGFENLVPY TSTVSVVATP VMTYGHLEGL INEWNLELED QEKYFLLQAT
110 120 130 140 150
QVNAWDHTLI ENGEMIRILH GEVNKVKLDQ KRLEQELDFI LSQQQELEFL
160 170 180
LTYLEESTRD QSGLHYLQDA DEEHVEISTR SAEF
Length:184
Mass (Da):20,837
Last modified:January 11, 2011 - v3
Checksum:iAF5CA4AC5DCEB344
GO
Isoform 2 (identifier: Q9H1M0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     65-72: SVVATPVM → RFVFYMEK
     73-184: Missing.

Show »
Length:72
Mass (Da):7,880
Checksum:i0B88E1359C41F611
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541F → L.
Corresponds to variant rs16987290 [ dbSNP | Ensembl ].
VAR_050569
Natural varianti177 – 1771I → T.2 Publications
Corresponds to variant rs1298577 [ dbSNP | Ensembl ].
VAR_028920

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei65 – 728SVVATPVM → RFVFYMEK in isoform 2. 1 PublicationVSP_021367
Alternative sequencei73 – 184112Missing in isoform 2. 1 PublicationVSP_021368Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000137 mRNA. Translation: BAA90968.1.
AL390039 Genomic DNA. Translation: CAC19637.1.
CH471120 Genomic DNA. Translation: EAX02718.1.
CH471120 Genomic DNA. Translation: EAX02720.1.
BC016327 mRNA. Translation: AAH16327.1.
BC017799 mRNA. Translation: AAH17799.1.
CCDSiCCDS14527.1. [Q9H1M0-1]
RefSeqiNP_060151.2. NM_017681.2. [Q9H1M0-1]
UniGeneiHs.163629.

Genome annotation databases

EnsembliENST00000372466; ENSP00000361544; ENSG00000198088. [Q9H1M0-1]
ENST00000484614; ENSP00000433269; ENSG00000198088. [Q9H1M0-2]
GeneIDi54830.
KEGGihsa:54830.
UCSCiuc004ena.4. human. [Q9H1M0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000137 mRNA. Translation: BAA90968.1.
AL390039 Genomic DNA. Translation: CAC19637.1.
CH471120 Genomic DNA. Translation: EAX02718.1.
CH471120 Genomic DNA. Translation: EAX02720.1.
BC016327 mRNA. Translation: AAH16327.1.
BC017799 mRNA. Translation: AAH17799.1.
CCDSiCCDS14527.1. [Q9H1M0-1]
RefSeqiNP_060151.2. NM_017681.2. [Q9H1M0-1]
UniGeneiHs.163629.

3D structure databases

ProteinModelPortaliQ9H1M0.
SMRiQ9H1M0. Positions 105-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120184. 9 interactions.
IntActiQ9H1M0. 2 interactions.
MINTiMINT-1482653.
STRINGi9606.ENSP00000361544.

Polymorphism and mutation databases

BioMutaiNUP62CL.
DMDMi317373409.

Proteomic databases

PaxDbiQ9H1M0.

Protocols and materials databases

DNASUi54830.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372466; ENSP00000361544; ENSG00000198088. [Q9H1M0-1]
ENST00000484614; ENSP00000433269; ENSG00000198088. [Q9H1M0-2]
GeneIDi54830.
KEGGihsa:54830.
UCSCiuc004ena.4. human. [Q9H1M0-1]

Organism-specific databases

CTDi54830.
GeneCardsiNUP62CL.
HGNCiHGNC:25960. NUP62CL.
HPAiHPA001884.
neXtProtiNX_Q9H1M0.
PharmGKBiPA145148360.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2196. Eukaryota.
ENOG410XT5X. LUCA.
GeneTreeiENSGT00730000111010.
HOGENOMiHOG000171766.
HOVERGENiHBG082003.
InParanoidiQ9H1M0.
OrthoDBiEOG7PZRZB.
PhylomeDBiQ9H1M0.

Miscellaneous databases

GenomeRNAii54830.
PROiQ9H1M0.

Gene expression databases

BgeeiQ9H1M0.
CleanExiHS_NUP62CL.
ExpressionAtlasiQ9H1M0. baseline and differential.
GenevisibleiQ9H1M0. HS.

Family and domain databases

InterProiIPR026010. NSP1/NUP62.
IPR007758. Nucleoporin_NSP1_C.
[Graphical view]
PANTHERiPTHR12084. PTHR12084. 1 hit.
PfamiPF05064. Nsp1_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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] (ISOFORM 1), VARIANT THR-177.
    Tissue: Colon.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-177.
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Bone marrow and Lung.

Entry informationi

Entry nameiN62CL_HUMAN
AccessioniPrimary (citable) accession number: Q9H1M0
Secondary accession number(s): D3DUX4, Q8WVL6, Q9NXP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: January 11, 2011
Last modified: June 8, 2016
This is version 97 of the entry and version 3 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.