Q9UH99 (SUN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SUN2
Synonyms:	FRIGG, KIAA0668, RAB5IP, UNC84B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	717 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Component of LINC complexes composed of SUN domain-containing proteins SUN1 or SUN2 coupled to KASH domain-containing proteins (SYNE1, SYNE2 or SYNE3), also called nesprins. Interacts with EMD, LMNA, RAB5A, SYNE1, SYNE2 and SYNE3. Ref.1 Ref.2 Ref.15 Ref.16
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 component	Endosome Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Signal-anchor Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	centrosome 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 along microfilament Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell migration Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	SUN-KASH complex Inferred from direct assay Ref.16. Source: UniProtKB endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear membrane Inferred from direct assay. Source: HPA
Molecular_function	lamin binding Inferred from direct assay PubMed 19933576. Source: UniProtKB microtubule binding Traceable author statement Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1044964,EBI-1044964
SYNE1	Q8NF91	3	EBI-1044964,EBI-928867
SYNE1	Q8NF91-1	2	EBI-1044964,EBI-6170938
SYNE2	Q8WXH0	5	EBI-1044964,EBI-2372294
SYNE2	Q8WXH0-1	2	EBI-1044964,EBI-6170976

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 717

717

SUN domain-containing protein 2

PRO_0000218913

Regions

Topological domain

1 – 212

212

Nuclear Ref.12

Transmembrane

213 – 233

21

Helical

Topological domain

234 – 717

484

Perinuclear space Ref.12

Domain

555 – 716

162

SUN

Region

1 – 139

139

LMNA-binding By similarity

Coiled coil

273 – 296

24

Potential

Coiled coil

348 – 440

93

Potential

Coiled coil

475 – 506

32

Potential

Compositional bias

2 – 164

163

Ser-rich

Compositional bias

100 – 105

6

Poly-Arg

Compositional bias

316 – 322

7

Poly-Gly

Compositional bias

468 – 471

4

Poly-Gly

Amino acid modifications

Modified residue

12

1

Phosphoserine Ref.10

Modified residue

38

1

Phosphoserine Ref.18

Modified residue

54

1

Phosphoserine Ref.10 Ref.13

Modified residue

116

1

Phosphoserine Ref.10

Glycosylation

636

1

N-linked (GlcNAc...) Ref.17

Natural variations

Alternative sequence

141

1

V → VEDSEGRGSKVTETEPVSSF PA in isoform 2.

VSP_045882

Natural variant

33

1

T → A.
Corresponds to variant rs2072799 [ dbSNP | Ensembl ].

VAR_052282

Natural variant

89

1

L → R. Ref.7
Corresponds to variant rs35496634 [ dbSNP | Ensembl ].

VAR_052283

Natural variant

348

1

R → C.
Corresponds to variant rs138708 [ dbSNP | Ensembl ].

VAR_052284

Natural variant

671

1

G → S. Ref.7
Corresponds to variant rs2072797 [ dbSNP | Ensembl ].

VAR_024624

Experimental info

Sequence conflict

644

1

K → R in CAD97926. Ref.5

Secondary structure

1

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717

Helix Strand Turn

Details...

Helix

525 – 540

16

Turn

541 – 544

4

Helix

552 – 554

3

Beta strand

557 – 563

7

Helix

571 – 574

4

Turn

575 – 577

3

Beta strand

579 – 584

6

Helix

588 – 592

5

Beta strand

601 – 605

5

Beta strand

609 – 627

19

Helix

631 – 633

3

Helix

635 – 637

3

Beta strand

645 – 655

11

Beta strand

660 – 666

7

Beta strand

669 – 671

3

Beta strand

673 – 678

6

Beta strand

687 – 694

8

Beta strand

697 – 699

3

Beta strand

701 – 706

6

Beta strand

708 – 714

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 25, 2003. Version 3. Checksum: CCF43C118E935E84	FASTA	717	80,311
	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
	Isoform 2 [UniParc]. Checksum: BD17ECBB9F58069B	FASTA	738	82,502
	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 VEDSEGRGSK VTETEPVSSF PAGYSDVDQQ SSSSRLRSAV 190 200 210 220 230 240 SRAGSLLWMV ATSPGRLFRL LYWWAGTTWY RLTTAASLLD VFVLTRRFSS LKTFLWFLLP 250 260 270 280 290 300 LLLLTCLTYG AWYFYPYGLQ TFHPALVSWW AAKDSRRPDE GWEARDSSPH FQAEQRVMSR 310 320 330 340 350 360 VHSLERRLEA LAAEFSSNWQ KEAMRLERLE LRQGAPGQGG GGGLSHEDTL ALLEGLVSRR 370 380 390 400 410 420 EAALKEDFRR ETAARIQEEL SALRAEHQQD SEDLFKKIVR ASQESEARIQ QLKSEWQSMT 430 440 450 460 470 480 QESFQESSVK ELRRLEDQLA GLQQELAALA LKQSSVAEEV GLLPQQIQAV RDDVESQFPA 490 500 510 520 530 540 WISQFLARGG GGRVGLLQRE EMQAQLRELE SKILTHVAEM QGKSAREAAA SLSLTLQKEG 550 560 570 580 590 600 VIGVTEEQVH HIVKQALQRY SEDRIGLADY ALESGGASVI STRCSETYET KTALLSLFGI 610 620 630 640 650 660 PLWYHSQSPR VILQPDVHPG NCWAFQGPQG FAVVRLSARI RPTAVTLEHV PKALSPNSTI 670 680 690 700 710 720 SSAPKDFAIF GFDEDLQQEG TLLGKFTYDQ DGEPIQTFHF QAPTMATYQV VELRILTNWG 730 HPEYTCIYRF RVHGEPAH

References

	« Hide 'large scale' referencesShow '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. , 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 AND 2), 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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.
BC111717 mRNA. Translation: AAI11718.1.
AF202723 mRNA. Translation: AAF15887.1.

IPI

IPI00295940.
IPI00878697.

PIR

T00371.

RefSeq

NP_001186508.1. NM_001199579.1.
NP_001186509.1. NM_001199580.1.
NP_056189.1. NM_015374.2.

UniGene

Hs.517622.
Hs.729395.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9UH99.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UH99. 12 interactions.

PTM databases

PhosphoSite

Q9UH99.

Polymorphism databases

DMDM

29337242.

Proteomic databases

PaxDb

Q9UH99.

PRIDE

Q9UH99.

Protocols and materials databases

DNASU

25777.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216064; ENSP00000216064; ENSG00000100242.
ENST00000405018; ENSP00000385616; ENSG00000100242.
ENST00000405510; ENSP00000385740; ENSG00000100242.
ENST00000406622; ENSP00000383992; ENSG00000100242.

GeneID

25777.

KEGG

hsa:25777.

UCSC

uc003awh.2. human.

Organism-specific databases

CTD

25777.

GeneCards

GC22M039132.

H-InvDB

HIX0159176.

HGNC

HGNC:14210. SUN2.

HPA

HPA001209.

MIM

613569. gene.

neXtProt

NX_Q9UH99.

PharmGKB

PA165378369.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG285464.

HOGENOM

HOG000253025.

HOVERGEN

HBG056957.

OrthoDB

EOG40K7ZH.

PhylomeDB

Q9UH99.

Enzyme and pathway databases

Reactome

REACT_111183. Meiosis.
REACT_115566. Cell Cycle.

Gene expression databases

ArrayExpress

Q9UH99.

Bgee

Q9UH99.

CleanEx

HS_UNC84B.

Genevestigator

Q9UH99.

GermOnline

ENSG00000100242. Homo sapiens.

Family and domain databases

InterPro

IPR012919. Sad1_UNC_C.
[Graphical view]

Pfam

PF07738. Sad1_UNC. 1 hit.
[Graphical view]

PROSITE

PS51469. SUN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SUN2. human.

GenomeRNAi

25777.

NextBio

46920.

SOURCE

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Entry information

Entry name

SUN2_HUMAN

Accession

Primary (citable) accession number: Q9UH99
Secondary accession number(s): B0QY62 , O75156, Q2NKN8, Q504T5, Q6B4H1, Q7Z3E3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	March 25, 2003
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.