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Q9UH99 (SUN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SUN domain-containing protein 2
Alternative name(s):
Protein unc-84 homolog B
Rab5-interacting protein
Short name=Rab5IP
Sad1/unc-84 protein-like 2
Gene names
Name:SUN2
Synonyms:FRIGG, KIAA0668, RAB5IP, UNC84B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length717 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5. Ref.16

Subunit structure

Core component of the LINC complex which is composed of inner nuclear membrane SUN domain-containing proteins coupled to outer nuclear membrane KASH domain-containing nesprins. SUN domain-containing proteins interact with A-type lamins of the nuclear lamina, while at the other end of the complex, nesprins interact with unique cytoskeletal components. Interacts with SYNE1, SYNE2 and SYNE3. Interacts with A-type lamin. Interaction with lamins B1 and C is hardly detectable By similarity. Interacts with EMD and RAB5A. Interacts with TMEM43. Ref.1 Ref.2 Ref.15 Ref.16 Ref.19

Subcellular location

Nucleus inner membrane; Single-pass type II membrane protein. Endosome membrane; Single-pass type II membrane protein Probable Ref.1 Ref.2 Ref.11 Ref.12 Ref.14.

Tissue specificity

Widely expressed. Highly expressed in heart, lung and muscle. Weakly expressed in fetal heart. Slightly overexpressed in some heart tissues form patients with congenital heart defects. Ref.1 Ref.9

Domain

The SUN domain may play a role in the nuclear anchoring and/or migration.

Sequence similarities

Contains 1 SUN domain.

Caution

It is uncertain whether Met-1 or Met-50 is the initiator.

Sequence caution

The sequence BAA31643.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentEndosome
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Signal-anchor
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcentrosome localization

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeletal anchoring at nuclear membrane

Inferred from direct assay Ref.16. Source: UniProtKB

mitotic spindle organization

Traceable author statement Ref.8. Source: UniProtKB

nuclear envelope organization

Inferred from genetic interaction PubMed 16380439. Source: MGI

nuclear matrix anchoring at nuclear membrane

Inferred from direct assay PubMed 19933576. Source: UniProtKB

nuclear migration

Traceable author statement PubMed 10508607. Source: UniProtKB

nuclear migration along microfilament

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentSUN-KASH complex

Inferred from direct assay Ref.16. Source: UniProtKB

condensed nuclear chromosome

Inferred from electronic annotation. Source: Ensembl

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear chromosome, telomeric region

Inferred from electronic annotation. Source: Ensembl

nuclear envelope

Inferred from direct assay PubMed 19933576. Source: UniProtKB

nuclear inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from direct assay. Source: HPA

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 22632968. Source: IntAct

lamin binding

Inferred from direct assay PubMed 19933576. Source: UniProtKB

microtubule binding

Traceable author statement Ref.8. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UH99-1)

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: Q9UH99-2)

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: V → VEDSEGRGSKVTETEPVSSFPA
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9UH99-3)

The sequence of this isoform differs from the canonical sequence as follows:
     683-717: TMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH → SSFPLCPWRLLPILGVCIYVAYHGGLGSWER
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 717717SUN domain-containing protein 2
PRO_0000218913

Regions

Topological domain1 – 212212Nuclear Ref.12
Transmembrane213 – 23321Helical
Topological domain234 – 717484Perinuclear space Ref.12
Domain555 – 716162SUN
Region1 – 139139LMNA-binding By similarity
Coiled coil273 – 29624 Potential
Coiled coil348 – 44093 Potential
Coiled coil475 – 50632 Potential
Compositional bias2 – 164163Ser-rich
Compositional bias100 – 1056Poly-Arg
Compositional bias316 – 3227Poly-Gly
Compositional bias468 – 4714Poly-Gly

Amino acid modifications

Modified residue121Phosphoserine Ref.10
Modified residue381Phosphoserine Ref.18
Modified residue541Phosphoserine Ref.10 Ref.13
Modified residue1161Phosphoserine Ref.10
Glycosylation6361N-linked (GlcNAc...) Ref.17

Natural variations

Alternative sequence1411V → VEDSEGRGSKVTETEPVSSF PA in isoform 2.
VSP_045882
Alternative sequence683 – 71735TMATY…GEPAH → SSFPLCPWRLLPILGVCIYV AYHGGLGSWER in isoform 3.
VSP_053702
Natural variant331T → A.
Corresponds to variant rs2072799 [ dbSNP | Ensembl ].
VAR_052282
Natural variant891L → R. Ref.7
Corresponds to variant rs35496634 [ dbSNP | Ensembl ].
VAR_052283
Natural variant3481R → C.
Corresponds to variant rs138708 [ dbSNP | Ensembl ].
VAR_052284
Natural variant6711G → S. Ref.7
Corresponds to variant rs2072797 [ dbSNP | Ensembl ].
VAR_024624

Experimental info

Sequence conflict6441K → R in CAD97926. Ref.5

Secondary structure

....................................... 717
Helix Strand Turn

Details...

Sequences

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

Last modified March 25, 2003. Version 3.
Checksum: CCF43C118E935E84

FASTA71780,311
        10         20         30         40         50         60 
MSRRSQRLTR YSQGDDDGSS SSGGSSVAGS QSTLFKDSPL RTLKRKSSNM KRLSPAPQLG 

        70         80         90        100        110        120 
PSSDAHTSYY SESLVHESWF PPRSSLEELH GDANWGEDLR VRRRRGTGGS ESSRASGLVG 

       130        140        150        160        170        180 
RKATEDFLGS SSGYSSEDDY VGYSDVDQQS SSSRLRSAVS RAGSLLWMVA TSPGRLFRLL 

       190        200        210        220        230        240 
YWWAGTTWYR LTTAASLLDV FVLTRRFSSL KTFLWFLLPL LLLTCLTYGA WYFYPYGLQT 

       250        260        270        280        290        300 
FHPALVSWWA AKDSRRPDEG WEARDSSPHF QAEQRVMSRV HSLERRLEAL AAEFSSNWQK 

       310        320        330        340        350        360 
EAMRLERLEL RQGAPGQGGG GGLSHEDTLA LLEGLVSRRE AALKEDFRRE TAARIQEELS 

       370        380        390        400        410        420 
ALRAEHQQDS EDLFKKIVRA SQESEARIQQ LKSEWQSMTQ ESFQESSVKE LRRLEDQLAG 

       430        440        450        460        470        480 
LQQELAALAL KQSSVAEEVG LLPQQIQAVR DDVESQFPAW ISQFLARGGG GRVGLLQREE 

       490        500        510        520        530        540 
MQAQLRELES KILTHVAEMQ GKSAREAAAS LSLTLQKEGV IGVTEEQVHH IVKQALQRYS 

       550        560        570        580        590        600 
EDRIGLADYA LESGGASVIS TRCSETYETK TALLSLFGIP LWYHSQSPRV ILQPDVHPGN 

       610        620        630        640        650        660 
CWAFQGPQGF AVVRLSARIR PTAVTLEHVP KALSPNSTIS SAPKDFAIFG FDEDLQQEGT 

       670        680        690        700        710 
LLGKFTYDQD GEPIQTFHFQ APTMATYQVV ELRILTNWGH PEYTCIYRFR VHGEPAH 

« Hide

Isoform 2 [UniParc].

Checksum: BD17ECBB9F58069B
Show »

FASTA73882,502
Isoform 3 [UniParc].

Checksum: 1D110119E43E562C
Show »

FASTA71379,612

References

« Hide 'large scale' references
[1]"A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion."
Hoffenberg S., Liu X., Nikolova L., Hall H.S., Dai W., Baughn R.E., Dickey B.F., Barbieri M.A., Aballay A., Stahl P.D., Knoll B.J.
J. Biol. Chem. 275:24661-24669(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RAB5A.
Tissue: B-cell.
[2]"Characterization of the structures involved in localization of the SUN proteins to the nuclear envelope and the centrosome."
Wang Q., Du X., Cai Z., Greene M.I.
DNA Cell Biol. 25:554-562(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, SUBUNIT, ASSOCIATION WITH THE CENTROSOME.
[3]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Fetal kidney.
[6]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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; 2 AND 3), VARIANTS ARG-89 AND SER-671.
Tissue: Brain and Pancreas.
[8]"UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development."
Malone C.J., Fixsen W.D., Horvitz H.R., Han M.
Development 126:3171-3181(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 278-717 (ISOFORM 1).
[9]"Isolation of differentially expressed genes in human heart tissues."
Sun G., Yuen Chan S., Yuan Y., Wang Chan K., Qiu G., Sun K., Ping Leung M.
Biochim. Biophys. Acta 1588:241-246(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies: identification of a novel protein, Frigg, as a protein kinase A substrate."
Gronborg M., Kristiansen T.Z., Stensballe A., Andersen J.S., Ohara O., Mann M., Jensen O.N., Pandey A.
Mol. Cell. Proteomics 1:517-527(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-12; SER-54 AND SER-116.
[11]"Nuclear membrane proteins with potential disease links found by subtractive proteomics."
Schirmer E.C., Florens L., Guan T., Yates J.R. III, Gerace L.
Science 301:1380-1382(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[12]"Sun2 is a novel mammalian inner nuclear membrane protein."
Hodzic D.M., Yeater D.B., Bengtsson L., Otto H., Stahl P.D.
J. Biol. Chem. 279:25805-25812(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Functional association of Sun1 with nuclear pore complexes."
Liu Q., Pante N., Misteli T., Elsagga M., Crisp M., Hodzic D., Burke B., Roux K.J.
J. Cell Biol. 178:785-798(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"Sun1 forms immobile macromolecular assemblies at the nuclear envelope."
Lu W., Gotzmann J., Sironi L., Jaeger V.M., Schneider M., Luke Y., Uhlen M., Szigyarto C.A., Brachner A., Ellenberg J., Foisner R., Noegel A.A., Karakesisoglou I.
Biochim. Biophys. Acta 1783:2415-2426(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUN1.
[16]"Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness."
Stewart-Hutchinson P.J., Hale C.M., Wirtz D., Hodzic D.
Exp. Cell Res. 314:1892-1905(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYNE1; SYNE2 AND SYNE3, FUNCTION OF THE LINC COMPLEXES.
[17]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-636.
Tissue: Liver.
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"TMEM43 mutations in Emery-Dreifuss muscular dystrophy-related myopathy."
Liang W.C., Mitsuhashi H., Keduka E., Nonaka I., Noguchi S., Nishino I., Hayashi Y.K.
Ann. Neurol. 69:1005-1013(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM43.
[20]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB014568 mRNA. Translation: BAA31643.1. Different initiation.
AY682988 mRNA. Translation: AAT90500.1.
CR456474 mRNA. Translation: CAG30360.1.
BX537962 mRNA. Translation: CAD97926.1.
AL008583 Genomic DNA. No translation available.
AL021806 Genomic DNA. No translation available.
AL021707 Genomic DNA. Translation: CAI21604.1.
AL021707 Genomic DNA. Translation: CAQ07913.1.
BC030684 mRNA. Translation: AAH30684.2.
BC094797 mRNA. Translation: AAH94797.1.
BC111549 mRNA. Translation: AAI11550.1.
BC111717 mRNA. Translation: AAI11718.1.
AF202723 mRNA. Translation: AAF15887.1.
PIRT00371.
RefSeqNP_001186508.1. NM_001199579.1.
NP_001186509.1. NM_001199580.1.
NP_056189.1. NM_015374.2.
XP_005261558.1. XM_005261501.2.
UniGeneHs.517622.
Hs.744734.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNPX-ray2.39A520-717[»]
4DXRX-ray2.32A522-717[»]
4DXSX-ray2.71A522-717[»]
4DXTX-ray2.22A522-717[»]
4FI9X-ray3.05A523-717[»]
ProteinModelPortalQ9UH99.
SMRQ9UH99. Positions 522-717.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117312. 15 interactions.
IntActQ9UH99. 18 interactions.
MINTMINT-3080157.

PTM databases

PhosphoSiteQ9UH99.

Polymorphism databases

DMDM29337242.

Proteomic databases

PaxDbQ9UH99.
PRIDEQ9UH99.

Protocols and materials databases

DNASU25777.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216064; ENSP00000216064; ENSG00000100242. [Q9UH99-1]
ENST00000405018; ENSP00000385616; ENSG00000100242. [Q9UH99-2]
ENST00000405510; ENSP00000385740; ENSG00000100242. [Q9UH99-1]
ENST00000406622; ENSP00000383992; ENSG00000100242. [Q9UH99-1]
GeneID25777.
KEGGhsa:25777.
UCSCuc003awh.2. human. [Q9UH99-1]
uc010gxq.2. human.

Organism-specific databases

CTD25777.
GeneCardsGC22M039418.
H-InvDBHIX0159176.
HGNCHGNC:14210. SUN2.
HPAHPA001209.
MIM613569. gene.
neXtProtNX_Q9UH99.
PharmGKBPA165378369.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG285464.
HOGENOMHOG000253025.
HOVERGENHBG056957.
OMAMQGKSAR.
OrthoDBEOG7J446H.
PhylomeDBQ9UH99.
TreeFamTF323915.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ9UH99.
BgeeQ9UH99.
CleanExHS_UNC84B.
GenevestigatorQ9UH99.

Family and domain databases

InterProIPR012919. Sad1_UNC_C.
[Graphical view]
PfamPF07738. Sad1_UNC. 1 hit.
[Graphical view]
PROSITEPS51469. SUN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSUN2. human.
GeneWikiUNC84B.
GenomeRNAi25777.
NextBio46920.
PROQ9UH99.
SOURCESearch...

Entry information

Entry nameSUN2_HUMAN
AccessionPrimary (citable) accession number: Q9UH99
Secondary accession number(s): B0QY62 expand/collapse secondary AC list , O75156, Q2NKN8, Q2T9F7, Q504T5, Q6B4H1, Q7Z3E3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: March 25, 2003
Last modified: April 16, 2014
This is version 126 of the entry and version 3 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

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 22

Human chromosome 22: entries, gene names and cross-references to MIM