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Q6ZMZ3

- SYNE3_HUMAN

UniProt

Q6ZMZ3 - SYNE3_HUMAN

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Protein

Nesprin-3

Gene

SYNE3

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. Involved in the maintenance of nuclear organization and structural integrity. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells.3 Publications

GO - Molecular functioni

  1. actin filament binding Source: UniProtKB

GO - Biological processi

  1. cytoskeletal anchoring at nuclear membrane Source: UniProtKB
  2. cytoskeleton organization Source: UniProtKB
  3. establishment of protein localization to membrane Source: UniProtKB
  4. regulation of cell shape Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Nesprin-3
Alternative name(s):
Nuclear envelope spectrin repeat protein 3
Gene namesi
Name:SYNE3
Synonyms:C14orf49
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:19861. SYNE3.

Subcellular locationi

Nucleus outer membrane 1 Publication; Single-pass type IV membrane protein 1 Publication. Nucleus envelope 1 Publication. Rough endoplasmic reticulum By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 925925CytoplasmicPROSITE-ProRule annotationAdd
BLAST
Transmembranei926 – 94621Helical; Anchor for type IV membrane proteinPROSITE-ProRule annotationAdd
BLAST
Topological domaini947 – 97529Perinuclear spacePROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
  4. nuclear envelope Source: UniProtKB
  5. nuclear outer membrane Source: Ensembl
  6. SUN-KASH complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134931380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 975975Nesprin-3PRO_0000281120Add
BLAST

Proteomic databases

MaxQBiQ6ZMZ3.
PaxDbiQ6ZMZ3.
PRIDEiQ6ZMZ3.

PTM databases

PhosphoSiteiQ6ZMZ3.

Expressioni

Tissue specificityi

Expressed in aortic endothelial cells (at protein level).1 Publication

Gene expression databases

BgeeiQ6ZMZ3.
CleanExiHS_C14orf49.
ExpressionAtlasiQ6ZMZ3. baseline and differential.
GenevestigatoriQ6ZMZ3.

Organism-specific databases

HPAiHPA055227.

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 PLEC (via actin-binding domain). Interacts with DST. Interacts with SYNE1 via spectrin repeats. Interacts (via KASH domain) with TOR1A (ATP-bound); the interaction is required for SYNE3 nuclear envelope localization.3 Publications

Protein-protein interaction databases

STRINGi9606.ENSP00000334308.

Structurei

3D structure databases

ProteinModelPortaliQ6ZMZ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati220 – 325106Spectrin 1Add
BLAST
Repeati647 – 74094Spectrin 2Add
BLAST
Domaini917 – 97559KASHPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili617 – 64529Sequence AnalysisAdd
BLAST

Domaini

The KASH domain is involved in the binding to SUN1 and SUN2 through recognition of their SUN domains.1 Publication

Sequence similaritiesi

Belongs to the nesprin family.Curated
Contains 1 KASH domain.PROSITE-ProRule annotation
Contains 2 spectrin repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG145316.
GeneTreeiENSGT00440000039367.
HOGENOMiHOG000154475.
HOVERGENiHBG094014.
InParanoidiQ6ZMZ3.
OMAiIKAQWEE.
OrthoDBiEOG7XM2X7.
PhylomeDBiQ6ZMZ3.
TreeFamiTF331132.

Family and domain databases

InterProiIPR012315. KASH.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF10541. KASH. 1 hit.
PF00435. Spectrin. 1 hit.
[Graphical view]
SMARTiSM00150. SPEC. 3 hits.
[Graphical view]
PROSITEiPS51049. KASH. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6ZMZ3-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha

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
MTQQPQDDFD RSVEDAQAWM KAVQDQLQVN DNTQGPRAAL EARLWETEKI
60 70 80 90 100
CQLEPEGRVR VDLVLRMAEA LLACCPGDQK PGILARLKDI KAQWEETVTY
110 120 130 140 150
MTHCHSRIEW VWLHWSEYLL ARDEFYRWFQ KMMVTLEPHI ELQLGLKEKQ
160 170 180 190 200
WQLSHAQVLL HNVDNQAVLL DRLLEEAASL FNRIGDPSVD EDAQKRMKAE
210 220 230 240 250
YDAVKAKAQK RVDLLEQVAR EHEEYQAGVD EFQLWLKAVV EKVNGCLGRN
260 270 280 290 300
CKLPITQRLS TLQDIAKDFP RGEESLETLE EQSAGVIRNT SPLGAEKITG
310 320 330 340 350
ELEEMRKVLE KLRALWEEEE ERLRGLLRSR GAWEQQIKQL EAELSEFRMV
360 370 380 390 400
LQRLAQEGLQ PAAKAGTEDE LVAHWRRYSA TRAALASEEP RVDRLQAQLK
410 420 430 440 450
ELIVFPHNLK PLSDSVIATI QEYQSLKVKS ARLRNAAAVE LWQHFQRPLQ
460 470 480 490 500
DLQLWKALAQ RLLEVTASLP DLPSLHTFLP QIEAALMESS RLKELLTMLQ
510 520 530 540 550
LKKDLLIGIF GQERATALLE QVAGSMRDRD LLHNSLLQRK SKLQSLLAQH
560 570 580 590 600
KDFGAAFEPL QRKLLDLQVR VQAEKGLQRD LPGKQAQLSR LQGLQEEGLD
610 620 630 640 650
LGAQMEAARP LVQENPNHQH KMDQLSSDFQ ALQRSLEDLV DRCRQSVQEH
660 670 680 690 700
CTFSHQLLEL RQWIVVTTQK LEAHRGEAGP GDAESQEAEF ERLVAEFPEK
710 720 730 740 750
EAQLSLVEAQ GWLVMEKSSP EGAAVVQEEL RELAESWRAL RLLEESLLSL
760 770 780 790 800
IRNWHLQRME VDSGKKMVFT NNIPKSGFLI NPMDPIPRHR RRANLLQEEE
810 820 830 840 850
GSHEDFSQLL RNFGQWLQVE NSKLVRIIAM RTSTAEDLRT RKSKLQELEA
860 870 880 890 900
RVPEGQHLFE NLLRLGPARG TSDELEDLRY QWMLYKSKLK DSGHLLTQSS
910 920 930 940 950
PGEPTGFQKT RRWRGLGSLF RRACCVALPL QLLLLLFLLL LFLLPIREED
960 970
RSCTLANNFA RSFTLMLRYN GPPPT
Length:975
Mass (Da):112,216
Last modified:March 20, 2007 - v2
Checksum:iA409AF86E1E781F4
GO
Isoform 2 (identifier: Q6ZMZ3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     793-797: Missing.

Note: No experimental confirmation available.

Show »
Length:970
Mass (Da):111,677
Checksum:i1A0FB44FD60A578D
GO
Isoform 3 (identifier: Q6ZMZ3-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     593-596: GLQE → VRGL
     597-975: Missing.

Show »
Length:596
Mass (Da):68,582
Checksum:i093499D5CF2671F4
GO

Sequence cautioni

The sequence BAC05312.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD18582.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAD62365.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti668 – 6681T → M.2 Publications
Corresponds to variant rs9671369 [ dbSNP | Ensembl ].
VAR_031231
Natural varianti795 – 7951Missing.1 Publication
Corresponds to variant rs76499929 [ dbSNP | Ensembl ].
VAR_068433
Natural varianti864 – 8641R → H.
Corresponds to variant rs17092216 [ dbSNP | Ensembl ].
VAR_031232
Natural varianti923 – 9231A → V.1 Publication
Corresponds to variant rs12434757 [ dbSNP | Ensembl ].
VAR_031233
Natural varianti946 – 9461I → V.
Corresponds to variant rs10130647 [ dbSNP | Ensembl ].
VAR_031234

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei593 – 5964GLQE → VRGL in isoform 3. 1 PublicationVSP_023976
Alternative sequencei597 – 975379Missing in isoform 3. 1 PublicationVSP_023977Add
BLAST
Alternative sequencei793 – 7975Missing in isoform 2. 1 PublicationVSP_023978

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248076 mRNA. Translation: CAD62365.1. Different initiation.
AL138539 Genomic DNA. No translation available.
BC146604 mRNA. Translation: AAI46605.1.
AK098471 mRNA. Translation: BAC05312.1. Different initiation.
AK131436 mRNA. Translation: BAD18582.1. Different initiation.
CCDSiCCDS9935.1. [Q6ZMZ3-1]
RefSeqiNP_689805.3. NM_152592.3. [Q6ZMZ3-1]
XP_005267433.1. XM_005267376.2. [Q6ZMZ3-1]
XP_005267434.1. XM_005267377.1. [Q6ZMZ3-1]
XP_006720126.1. XM_006720063.1. [Q6ZMZ3-1]
XP_006720127.1. XM_006720064.1. [Q6ZMZ3-2]
UniGeneiHs.354645.

Genome annotation databases

EnsembliENST00000334258; ENSP00000334308; ENSG00000176438. [Q6ZMZ3-1]
ENST00000553340; ENSP00000450774; ENSG00000176438. [Q6ZMZ3-3]
ENST00000557275; ENSP00000450562; ENSG00000176438. [Q6ZMZ3-2]
GeneIDi161176.
KEGGihsa:161176.
UCSCiuc001yei.4. human. [Q6ZMZ3-1]
uc001yej.1. human. [Q6ZMZ3-3]
uc010avi.3. human. [Q6ZMZ3-2]

Polymorphism databases

DMDMi134035037.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248076 mRNA. Translation: CAD62365.1 . Different initiation.
AL138539 Genomic DNA. No translation available.
BC146604 mRNA. Translation: AAI46605.1 .
AK098471 mRNA. Translation: BAC05312.1 . Different initiation.
AK131436 mRNA. Translation: BAD18582.1 . Different initiation.
CCDSi CCDS9935.1. [Q6ZMZ3-1 ]
RefSeqi NP_689805.3. NM_152592.3. [Q6ZMZ3-1 ]
XP_005267433.1. XM_005267376.2. [Q6ZMZ3-1 ]
XP_005267434.1. XM_005267377.1. [Q6ZMZ3-1 ]
XP_006720126.1. XM_006720063.1. [Q6ZMZ3-1 ]
XP_006720127.1. XM_006720064.1. [Q6ZMZ3-2 ]
UniGenei Hs.354645.

3D structure databases

ProteinModelPortali Q6ZMZ3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000334308.

PTM databases

PhosphoSitei Q6ZMZ3.

Polymorphism databases

DMDMi 134035037.

Proteomic databases

MaxQBi Q6ZMZ3.
PaxDbi Q6ZMZ3.
PRIDEi Q6ZMZ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334258 ; ENSP00000334308 ; ENSG00000176438 . [Q6ZMZ3-1 ]
ENST00000553340 ; ENSP00000450774 ; ENSG00000176438 . [Q6ZMZ3-3 ]
ENST00000557275 ; ENSP00000450562 ; ENSG00000176438 . [Q6ZMZ3-2 ]
GeneIDi 161176.
KEGGi hsa:161176.
UCSCi uc001yei.4. human. [Q6ZMZ3-1 ]
uc001yej.1. human. [Q6ZMZ3-3 ]
uc010avi.3. human. [Q6ZMZ3-2 ]

Organism-specific databases

CTDi 161176.
GeneCardsi GC14M095884.
H-InvDB HIX0011939.
HGNCi HGNC:19861. SYNE3.
HPAi HPA055227.
MIMi 610861. gene.
neXtProti NX_Q6ZMZ3.
PharmGKBi PA134931380.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG145316.
GeneTreei ENSGT00440000039367.
HOGENOMi HOG000154475.
HOVERGENi HBG094014.
InParanoidi Q6ZMZ3.
OMAi IKAQWEE.
OrthoDBi EOG7XM2X7.
PhylomeDBi Q6ZMZ3.
TreeFami TF331132.

Miscellaneous databases

GenomeRNAii 161176.
NextBioi 88029.
PROi Q6ZMZ3.
SOURCEi Search...

Gene expression databases

Bgeei Q6ZMZ3.
CleanExi HS_C14orf49.
ExpressionAtlasi Q6ZMZ3. baseline and differential.
Genevestigatori Q6ZMZ3.

Family and domain databases

InterProi IPR012315. KASH.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view ]
Pfami PF10541. KASH. 1 hit.
PF00435. Spectrin. 1 hit.
[Graphical view ]
SMARTi SM00150. SPEC. 3 hits.
[Graphical view ]
PROSITEi PS51049. KASH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: B-cell.
  2. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 1), VARIANTS MET-668 AND LEU-795 DEL.
  4. "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] OF 41-975 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 411-975 (ISOFORM 1), VARIANTS MET-668 AND VAL-923.
    Tissue: Synovial cell and Thyroid.
  5. "Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin."
    Wilhelmsen K., Litjens S.H.M., Kuikman I., Tshimbalanga N., Janssen H., van den Bout I., Raymond K., Sonnenberg A.
    J. Cell Biol. 171:799-810(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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: FUNCTION, DOMAIN, INTERACTION WITH SUN1 AND SUN2.
  7. "TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
    Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
    J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TOR1A.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Nesprin-3 regulates endothelial cell morphology, perinuclear cytoskeletal architecture, and flow-induced polarization."
    Morgan J.T., Pfeiffer E.R., Thirkill T.L., Kumar P., Peng G., Fridolfsson H.N., Douglas G.C., Starr D.A., Barakat A.I.
    Mol. Biol. Cell 22:4324-4334(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. Cited for: INTERACTION WITH SYNE1.

Entry informationi

Entry nameiSYNE3_HUMAN
AccessioniPrimary (citable) accession number: Q6ZMZ3
Secondary accession number(s): A6H8H3, Q86SX5, Q8N7G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: October 29, 2014
This is version 95 of the entry and version 2 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 14
    Human chromosome 14: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3