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Q9NVA2

- SEP11_HUMAN

UniProt

Q9NVA2 - SEP11_HUMAN

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Protein
Septin-11
Gene
SEPT11
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Filament-forming cytoskeletal GTPase. May play a role in cytokinesis Reviewed prediction. May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity By similarity. During Listeria monocytogenes infection, not required for the bacterial entry process, but restricts its efficacy.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031GTP; via amide nitrogen By similarity
Binding sitei238 – 2381GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei253 – 2531GTP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 558GTP By similarity
Nucleotide bindingi184 – 1929GTP By similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. protein heterooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-11
Gene namesi
Name:SEPT11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:25589. SEPT11.

Subcellular locationi

Cytoplasmcytoskeleton. Cell junctionsynapse. Cell projectiondendritic spine. Cell projectionaxon By similarity
Note: Partly colocalizes with stress fibers and microtubules. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria.3 Publications

GO - Cellular componenti

  1. axon Source: UniProtKB-SubCell
  2. cell junction Source: UniProtKB-KW
  3. dendritic spine Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProt
  5. septin complex Source: InterPro
  6. stress fiber Source: UniProtKB
  7. synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Synapse

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving SEPT11 may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with KMT2A/MLL1.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481G → A: High reduction in GTPase activity. No effect on GTP-binding. Loss of filament formation. 1 Publication

Organism-specific databases

PharmGKBiPA128394688.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 429428Septin-11
PRO_0000173542Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NVA2.
PaxDbiQ9NVA2.
PeptideAtlasiQ9NVA2.
PRIDEiQ9NVA2.

2D gel databases

OGPiQ9NVA2.
UCD-2DPAGEQ9NVA2.

PTM databases

PhosphoSiteiQ9NVA2.

Expressioni

Tissue specificityi

Widely expressed, except in leukocytes.2 Publications

Gene expression databases

ArrayExpressiQ9NVA2.
BgeeiQ9NVA2.
CleanExiHS_SEPT11.
GenevestigatoriQ9NVA2.

Organism-specific databases

HPAiHPA003459.
HPA005665.

Interactioni

Subunit structurei

Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Interacts with SEPT7, SEPT9 and SEPT12. Forms homooligomers.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SEPT5Q997196EBI-957999,EBI-373345

Protein-protein interaction databases

BioGridi120870. 32 interactions.
IntActiQ9NVA2. 2 interactions.
MINTiMINT-3074824.
STRINGi9606.ENSP00000264893.

Structurei

3D structure databases

ProteinModelPortaliQ9NVA2.
SMRiQ9NVA2. Positions 18-306.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 304267Septin-type G
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili320 – 41596 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5019.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ9NVA2.
KOiK16939.
OMAiEVSNFQK.
OrthoDBiEOG7J9VQK.
PhylomeDBiQ9NVA2.
TreeFamiTF101080.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NVA2-1) [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

MAVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET    50
GIGKSTLMDT LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD 100
TVGFGDQINK DDSYKPIVEY IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC 150
LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP IIAKADTIAK NELHKFKSKI 200
MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST EEVKIGNKMA 250
KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC 300
KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK 350
EKEAELKEAE KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVNNFQKKKA 400
AAQLLQSQAQ QSGAQQTKKD KDKKNASFT 429
Length:429
Mass (Da):49,398
Last modified:January 23, 2007 - v3
Checksum:iD467F1F315FFD028
GO
Isoform 2 (identifier: Q9NVA2-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MAVAVGRPS → MEERKPAHVLRSFKYAAFM

Note: No experimental confirmation available.

Show »
Length:439
Mass (Da):50,823
Checksum:iC8E82F016C56A392
GO

Sequence cautioni

The sequence CAB53741.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence BAB55250.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99MAVAVGRPS → MEERKPAHVLRSFKYAAFM in isoform 2.
VSP_038320

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421Y → H in CAB53741. 1 Publication
Sequence conflicti298 – 2981R → H in CAB53741. 1 Publication
Sequence conflicti321 – 3211E → G in CAB53741. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GU727629 mRNA. Translation: ADU87631.1.
AK001711 mRNA. Translation: BAA91853.1.
AK027633 mRNA. Translation: BAB55250.1. Different initiation.
AK302700 mRNA. Translation: BAH13782.1.
AC104687 Genomic DNA. Translation: AAY40922.1.
AC111196 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05805.1.
BC008083 mRNA. Translation: AAH08083.3.
BC063615 mRNA. Translation: AAH63615.1.
AL110300 mRNA. Translation: CAB53741.2. Sequence problems.
CCDSiCCDS34018.1. [Q9NVA2-1]
RefSeqiNP_060713.1. NM_018243.2. [Q9NVA2-1]
XP_005263177.1. XM_005263120.1. [Q9NVA2-2]
UniGeneiHs.128199.

Genome annotation databases

EnsembliENST00000264893; ENSP00000264893; ENSG00000138758. [Q9NVA2-1]
ENST00000510515; ENSP00000422896; ENSG00000138758. [Q9NVA2-2]
ENST00000541121; ENSP00000443701; ENSG00000138758. [Q9NVA2-2]
GeneIDi55752.
KEGGihsa:55752.
UCSCiuc003hkj.3. human. [Q9NVA2-1]
uc010ijh.1. human. [Q9NVA2-2]

Polymorphism databases

DMDMi50401687.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GU727629 mRNA. Translation: ADU87631.1 .
AK001711 mRNA. Translation: BAA91853.1 .
AK027633 mRNA. Translation: BAB55250.1 . Different initiation.
AK302700 mRNA. Translation: BAH13782.1 .
AC104687 Genomic DNA. Translation: AAY40922.1 .
AC111196 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05805.1 .
BC008083 mRNA. Translation: AAH08083.3 .
BC063615 mRNA. Translation: AAH63615.1 .
AL110300 mRNA. Translation: CAB53741.2 . Sequence problems.
CCDSi CCDS34018.1. [Q9NVA2-1 ]
RefSeqi NP_060713.1. NM_018243.2. [Q9NVA2-1 ]
XP_005263177.1. XM_005263120.1. [Q9NVA2-2 ]
UniGenei Hs.128199.

3D structure databases

ProteinModelPortali Q9NVA2.
SMRi Q9NVA2. Positions 18-306.
ModBasei Search...

Protein-protein interaction databases

BioGridi 120870. 32 interactions.
IntActi Q9NVA2. 2 interactions.
MINTi MINT-3074824.
STRINGi 9606.ENSP00000264893.

PTM databases

PhosphoSitei Q9NVA2.

Polymorphism databases

DMDMi 50401687.

2D gel databases

OGPi Q9NVA2.
UCD-2DPAGE Q9NVA2.

Proteomic databases

MaxQBi Q9NVA2.
PaxDbi Q9NVA2.
PeptideAtlasi Q9NVA2.
PRIDEi Q9NVA2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264893 ; ENSP00000264893 ; ENSG00000138758 . [Q9NVA2-1 ]
ENST00000510515 ; ENSP00000422896 ; ENSG00000138758 . [Q9NVA2-2 ]
ENST00000541121 ; ENSP00000443701 ; ENSG00000138758 . [Q9NVA2-2 ]
GeneIDi 55752.
KEGGi hsa:55752.
UCSCi uc003hkj.3. human. [Q9NVA2-1 ]
uc010ijh.1. human. [Q9NVA2-2 ]

Organism-specific databases

CTDi 55752.
GeneCardsi GC04P077870.
HGNCi HGNC:25589. SEPT11.
HPAi HPA003459.
HPA005665.
MIMi 612887. gene.
neXtProti NX_Q9NVA2.
PharmGKBi PA128394688.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5019.
HOGENOMi HOG000233586.
HOVERGENi HBG065093.
InParanoidi Q9NVA2.
KOi K16939.
OMAi EVSNFQK.
OrthoDBi EOG7J9VQK.
PhylomeDBi Q9NVA2.
TreeFami TF101080.

Miscellaneous databases

ChiTaRSi SEPT11. human.
GeneWikii SEPT11.
GenomeRNAii 55752.
NextBioi 60745.
PROi Q9NVA2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NVA2.
Bgeei Q9NVA2.
CleanExi HS_SEPT11.
Genevestigatori Q9NVA2.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view ]
PANTHERi PTHR18884. PTHR18884. 1 hit.
Pfami PF00735. Septin. 1 hit.
[Graphical view ]
PIRSFi PIRSF006698. Septin. 1 hit.
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS51719. G_SEPTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
    Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
    Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Epididymis.
  2. "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] (ISOFORMS 1 AND 2).
    Tissue: Teratocarcinoma and Testis.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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).
    Tissue: Colon and Skin.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-337.
    Tissue: Fetal kidney.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-14 (ISOFORM 1), ACETYLATION AT ALA-2.
    Tissue: Platelet.
  8. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 15-34; 55-79; 84-93; 96-110; 176-184; 309-336; 387-397 AND 400-418, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  9. "Biochemical and cell biological characterization of a mammalian septin, Sept11."
    Hanai N., Nagata K., Kawajiri A., Shiromizu T., Saitoh N., Hasegawa Y., Murakami S., Inagaki M.
    FEBS Lett. 568:83-88(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-48, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  10. "Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11."
    Nagata K., Asano T., Nozawa Y., Inagaki M.
    J. Biol. Chem. 279:55895-55904(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEPT7 AND SEPT9.
  11. "FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23)."
    Kojima K., Sakai I., Hasegawa A., Niiya H., Azuma T., Matsuo Y., Fujii N., Tanimoto M., Fujita S.
    Leukemia 18:998-1005(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
  12. "Expression profiling the human septin gene family."
    Hall P.A., Jung K., Hillan K.J., Russell S.E.H.
    J. Pathol. 206:269-278(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are associated with altered interactions with SEPT4/SEPT11 and resistance to Rho/Rhotekin-signaling."
    Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.
    Hum. Mutat. 28:1005-1013(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "SEPT12 interacts with SEPT6 and this interaction alters the filament structure of SEPT6 in Hela cells."
    Ding X., Yu W., Liu M., Shen S., Chen F., Wan B., Yu L.
    J. Biochem. Mol. Biol. 40:973-978(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEPT12.
  15. Cited for: ROLE IN BACTERIAL INFECTION.
  16. Cited for: INTERACTION WITH SEPT9, SUBCELLULAR LOCATION.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSEP11_HUMAN
AccessioniPrimary (citable) accession number: Q9NVA2
Secondary accession number(s): B7Z7Z6
, E9KL32, Q4W5G1, Q7L4N1, Q96SP1, Q9UFY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 116 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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