SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UH99

- SUN2_HUMAN

UniProt

Q9UH99 - SUN2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
SUN domain-containing protein 2
Gene
SUN2, FRIGG, KIAA0668, RAB5IP, UNC84B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 RAB5.1 Publication

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. lamin binding Source: UniProtKB
  3. microtubule binding Source: UniProtKB
  4. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. centrosome localization Source: UniProtKB
  2. cytoskeletal anchoring at nuclear membrane Source: UniProtKB
  3. mitotic spindle organization Source: UniProtKB
  4. nuclear envelope organization Source: MGI
  5. nuclear matrix anchoring at nuclear membrane Source: UniProtKB
  6. nuclear migration Source: UniProtKB
  7. nuclear migration along microfilament Source: UniProtKB
  8. positive regulation of cell migration Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_75792. Meiotic synapsis.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SUN2
Synonyms:FRIGG, KIAA0668, RAB5IP, UNC84B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:14210. SUN2.

Subcellular locationi

Nucleus inner membrane; Single-pass type II membrane protein. Endosome membrane; Single-pass type II membrane protein Inferred 5 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 212212Nuclear1 Publication
Add
BLAST
Transmembranei213 – 23321Helical
Add
BLAST
Topological domaini234 – 717484Perinuclear space1 Publication
Add
BLAST

GO - Cellular componenti

  1. SUN-KASH complex Source: UniProtKB
  2. condensed nuclear chromosome Source: Ensembl
  3. endosome membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
  5. nuclear chromosome, telomeric region Source: Ensembl
  6. nuclear envelope Source: UniProtKB
  7. nuclear inner membrane Source: UniProtKB-SubCell
  8. nuclear membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA165378369.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 717717SUN domain-containing protein 2
PRO_0000218913Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine1 Publication
Modified residuei38 – 381Phosphoserine1 Publication
Modified residuei54 – 541Phosphoserine2 Publications
Modified residuei116 – 1161Phosphoserine1 Publication
Glycosylationi636 – 6361N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9UH99.
PaxDbiQ9UH99.
PRIDEiQ9UH99.

PTM databases

PhosphoSiteiQ9UH99.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

ArrayExpressiQ9UH99.
BgeeiQ9UH99.
CleanExiHS_UNC84B.
GenevestigatoriQ9UH99.

Organism-specific databases

HPAiHPA001209.

Interactioni

Subunit structurei

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 TMEM43.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-1044964,EBI-1044964
COPB1P536182EBI-1044964,EBI-359063
EMDP504023EBI-1044964,EBI-489887
KPNA2P522923EBI-1044964,EBI-349938
SYNE1Q8NF913EBI-1044964,EBI-928867
SYNE1Q8NF91-12EBI-1044964,EBI-6170938
SYNE2Q8WXH05EBI-1044964,EBI-2372294
SYNE2Q8WXH0-12EBI-1044964,EBI-6170976

Protein-protein interaction databases

BioGridi117312. 15 interactions.
IntActiQ9UH99. 18 interactions.
MINTiMINT-3080157.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi525 – 54016
Turni541 – 5444
Helixi552 – 5543
Beta strandi557 – 5637
Helixi571 – 5744
Turni575 – 5773
Beta strandi579 – 5846
Helixi588 – 5925
Beta strandi601 – 6055
Beta strandi609 – 62719
Helixi631 – 6333
Helixi635 – 6373
Beta strandi645 – 65511
Beta strandi660 – 6667
Beta strandi669 – 6713
Beta strandi673 – 6786
Beta strandi687 – 6948
Beta strandi697 – 6993
Beta strandi701 – 7066
Beta strandi708 – 7147

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNPX-ray2.39A520-717[»]
4DXRX-ray2.32A522-717[»]
4DXSX-ray2.71A522-717[»]
4DXTX-ray2.22A522-717[»]
4FI9X-ray3.05A523-717[»]
ProteinModelPortaliQ9UH99.
SMRiQ9UH99. Positions 522-717.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini555 – 716162SUN
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 139139LMNA-binding By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili273 – 29624 Reviewed prediction
Add
BLAST
Coiled coili348 – 44093 Reviewed prediction
Add
BLAST
Coiled coili475 – 50632 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 164163Ser-rich
Add
BLAST
Compositional biasi100 – 1056Poly-Arg
Compositional biasi316 – 3227Poly-Gly
Compositional biasi468 – 4714Poly-Gly

Domaini

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

Sequence similaritiesi

Contains 1 SUN domain.

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG285464.
HOGENOMiHOG000253025.
HOVERGENiHBG056957.
OMAiVGTTWYR.
OrthoDBiEOG7J446H.
PhylomeDBiQ9UH99.
TreeFamiTF323915.

Family and domain databases

InterProiIPR012919. Sad1_UNC_C.
[Graphical view]
PfamiPF07738. Sad1_UNC. 1 hit.
[Graphical view]
PROSITEiPS51469. SUN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UH99-1) [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

MSRRSQRLTR YSQGDDDGSS SSGGSSVAGS QSTLFKDSPL RTLKRKSSNM    50
KRLSPAPQLG PSSDAHTSYY SESLVHESWF PPRSSLEELH GDANWGEDLR 100
VRRRRGTGGS ESSRASGLVG RKATEDFLGS SSGYSSEDDY VGYSDVDQQS 150
SSSRLRSAVS RAGSLLWMVA TSPGRLFRLL YWWAGTTWYR LTTAASLLDV 200
FVLTRRFSSL KTFLWFLLPL LLLTCLTYGA WYFYPYGLQT FHPALVSWWA 250
AKDSRRPDEG WEARDSSPHF QAEQRVMSRV HSLERRLEAL AAEFSSNWQK 300
EAMRLERLEL RQGAPGQGGG GGLSHEDTLA LLEGLVSRRE AALKEDFRRE 350
TAARIQEELS ALRAEHQQDS EDLFKKIVRA SQESEARIQQ LKSEWQSMTQ 400
ESFQESSVKE LRRLEDQLAG LQQELAALAL KQSSVAEEVG LLPQQIQAVR 450
DDVESQFPAW ISQFLARGGG GRVGLLQREE MQAQLRELES KILTHVAEMQ 500
GKSAREAAAS LSLTLQKEGV IGVTEEQVHH IVKQALQRYS EDRIGLADYA 550
LESGGASVIS TRCSETYETK TALLSLFGIP LWYHSQSPRV ILQPDVHPGN 600
CWAFQGPQGF AVVRLSARIR PTAVTLEHVP KALSPNSTIS SAPKDFAIFG 650
FDEDLQQEGT LLGKFTYDQD GEPIQTFHFQ APTMATYQVV ELRILTNWGH 700
PEYTCIYRFR VHGEPAH 717
Length:717
Mass (Da):80,311
Last modified:March 25, 2003 - v3
Checksum:iCCF43C118E935E84
GO
Isoform 2 (identifier: Q9UH99-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: V → VEDSEGRGSKVTETEPVSSFPA

Note: No experimental confirmation available.

Show »
Length:738
Mass (Da):82,502
Checksum:iBD17ECBB9F58069B
GO
Isoform 3 (identifier: Q9UH99-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     683-717: TMATYQVVELRILTNWGHPEYTCIYRFRVHGEPAH → SSFPLCPWRLLPILGVCIYVAYHGGLGSWER

Note: No experimental confirmation available.

Show »
Length:713
Mass (Da):79,612
Checksum:i1D110119E43E562C
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331T → A.
Corresponds to variant rs2072799 [ dbSNP | Ensembl ].
VAR_052282
Natural varianti89 – 891L → R.1 Publication
Corresponds to variant rs35496634 [ dbSNP | Ensembl ].
VAR_052283
Natural varianti348 – 3481R → C.
Corresponds to variant rs138708 [ dbSNP | Ensembl ].
VAR_052284
Natural varianti671 – 6711G → S.1 Publication
Corresponds to variant rs2072797 [ dbSNP | Ensembl ].
VAR_024624

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei141 – 1411V → VEDSEGRGSKVTETEPVSSF PA in isoform 2.
VSP_045882
Alternative sequencei683 – 71735TMATY…GEPAH → SSFPLCPWRLLPILGVCIYV AYHGGLGSWER in isoform 3.
VSP_053702Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti644 – 6441K → R in CAD97926. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13978.1. [Q9UH99-1]
CCDS56231.1. [Q9UH99-2]
PIRiT00371.
RefSeqiNP_001186508.1. NM_001199579.1. [Q9UH99-2]
NP_001186509.1. NM_001199580.1. [Q9UH99-1]
NP_056189.1. NM_015374.2. [Q9UH99-1]
XP_005261558.1. XM_005261501.2. [Q9UH99-1]
UniGeneiHs.517622.
Hs.744734.

Genome annotation databases

EnsembliENST00000216064; ENSP00000216064; ENSG00000100242. [Q9UH99-1]
ENST00000405018; ENSP00000385616; ENSG00000100242. [Q9UH99-2]
ENST00000405510; ENSP00000385740; ENSG00000100242. [Q9UH99-1]
ENST00000406622; ENSP00000383992; ENSG00000100242. [Q9UH99-1]
GeneIDi25777.
KEGGihsa:25777.
UCSCiuc003awh.2. human. [Q9UH99-1]
uc010gxq.2. human.

Polymorphism databases

DMDMi29337242.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13978.1. [Q9UH99-1 ]
CCDS56231.1. [Q9UH99-2 ]
PIRi T00371.
RefSeqi NP_001186508.1. NM_001199579.1. [Q9UH99-2 ]
NP_001186509.1. NM_001199580.1. [Q9UH99-1 ]
NP_056189.1. NM_015374.2. [Q9UH99-1 ]
XP_005261558.1. XM_005261501.2. [Q9UH99-1 ]
UniGenei Hs.517622.
Hs.744734.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNP X-ray 2.39 A 520-717 [» ]
4DXR X-ray 2.32 A 522-717 [» ]
4DXS X-ray 2.71 A 522-717 [» ]
4DXT X-ray 2.22 A 522-717 [» ]
4FI9 X-ray 3.05 A 523-717 [» ]
ProteinModelPortali Q9UH99.
SMRi Q9UH99. Positions 522-717.
ModBasei Search...

Protein-protein interaction databases

BioGridi 117312. 15 interactions.
IntActi Q9UH99. 18 interactions.
MINTi MINT-3080157.

PTM databases

PhosphoSitei Q9UH99.

Polymorphism databases

DMDMi 29337242.

Proteomic databases

MaxQBi Q9UH99.
PaxDbi Q9UH99.
PRIDEi Q9UH99.

Protocols and materials databases

DNASUi 25777.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216064 ; ENSP00000216064 ; ENSG00000100242 . [Q9UH99-1 ]
ENST00000405018 ; ENSP00000385616 ; ENSG00000100242 . [Q9UH99-2 ]
ENST00000405510 ; ENSP00000385740 ; ENSG00000100242 . [Q9UH99-1 ]
ENST00000406622 ; ENSP00000383992 ; ENSG00000100242 . [Q9UH99-1 ]
GeneIDi 25777.
KEGGi hsa:25777.
UCSCi uc003awh.2. human. [Q9UH99-1 ]
uc010gxq.2. human.

Organism-specific databases

CTDi 25777.
GeneCardsi GC22M039418.
H-InvDB HIX0159176.
HGNCi HGNC:14210. SUN2.
HPAi HPA001209.
MIMi 613569. gene.
neXtProti NX_Q9UH99.
PharmGKBi PA165378369.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG285464.
HOGENOMi HOG000253025.
HOVERGENi HBG056957.
OMAi VGTTWYR.
OrthoDBi EOG7J446H.
PhylomeDBi Q9UH99.
TreeFami TF323915.

Enzyme and pathway databases

Reactomei REACT_75792. Meiotic synapsis.

Miscellaneous databases

ChiTaRSi SUN2. human.
GeneWikii UNC84B.
GenomeRNAii 25777.
NextBioi 46920.
PROi Q9UH99.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UH99.
Bgeei Q9UH99.
CleanExi HS_UNC84B.
Genevestigatori Q9UH99.

Family and domain databases

InterProi IPR012919. Sad1_UNC_C.
[Graphical view ]
Pfami PF07738. Sad1_UNC. 1 hit.
[Graphical view ]
PROSITEi PS51469. SUN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSUN2_HUMAN
AccessioniPrimary (citable) accession number: Q9UH99
Secondary accession number(s): B0QY62
, O75156, Q2NKN8, Q2T9F7, Q504T5, Q6B4H1, Q7Z3E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: March 25, 2003
Last modified: September 3, 2014
This is version 130 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi