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Protein

Protein FAM161A

Gene

FAM161A

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

Functioni

Involved in ciliogenesis.1 Publication

GO - Biological processi

  • cilium assembly Source: UniProtKB
  • response to stimulus Source: UniProtKB-KW
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FAM161A
Gene namesi
Name:FAM161A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:25808. FAM161A.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • ciliary basal body Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • photoreceptor connecting cilium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 28 (RP28)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.

See also OMIM:606068

Keywords - Diseasei

Ciliopathy, Retinitis pigmentosa

Organism-specific databases

MIMi606068. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA162386876.

Polymorphism and mutation databases

BioMutaiFAM161A.
DMDMi182705173.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 660660Protein FAM161APRO_0000329052Add
BLAST

Proteomic databases

MaxQBiQ3B820.
PaxDbiQ3B820.
PRIDEiQ3B820.

PTM databases

PhosphoSiteiQ3B820.

Expressioni

Tissue specificityi

Isoform 1 and isoform 3 are widely expressed with highest levels in retina and testis, with isoform 1 being the most abundant in all tissues tested.2 Publications

Gene expression databases

BgeeiQ3B820.
CleanExiHS_FAM161A.
ExpressionAtlasiQ3B820. baseline and differential.
GenevisibleiQ3B820. HS.

Organism-specific databases

HPAiHPA032119.

Interactioni

Subunit structurei

Interacts (via C-terminus) with microtubules. Interacts with LCA5, CEP290 and SDCCAG8. Interacts with FAM161B. Interacts with POC1B.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BEND3Q5T5X73EBI-719941,EBI-1211496
BEND5Q7L4P63EBI-719941,EBI-724373
CADPSA2RRN73EBI-719941,EBI-10179719
CALCOCO1Q9P1Z23EBI-719941,EBI-749920
CALCOCO2Q131373EBI-719941,EBI-739580
CARD9Q9H2573EBI-719941,EBI-751319
CCDC102BA1A4H13EBI-719941,EBI-10171570
CCDC136Q96JN2-23EBI-719941,EBI-10171416
CCDC155Q8N6L03EBI-719941,EBI-749265
CCDC57Q2TAC23EBI-719941,EBI-2808286
CDR2Q018503EBI-719941,EBI-1181367
CEP44Q9C0F13EBI-719941,EBI-744115
CEP57L1Q8IYX8-23EBI-719941,EBI-10181988
CEP63Q96MT83EBI-719941,EBI-741977
CEP70Q8NHQ13EBI-719941,EBI-739624
DHX32Q7L7V13EBI-719941,EBI-2807297
DKFZp451B226Q5HYH73EBI-719941,EBI-10173842
DOCK8Q8NF50-23EBI-719941,EBI-10174653
EHMT2A2ABF93EBI-719941,EBI-10174566
FAM9BQ8IZU03EBI-719941,EBI-10175124
FSD2A1L4K13EBI-719941,EBI-5661036
HMBOX1Q6NT763EBI-719941,EBI-2549423
IKZF1Q134223EBI-719941,EBI-745305
KIAA0753Q2KHM93EBI-719941,EBI-2805604
KRTAP10-7P604093EBI-719941,EBI-10172290
KRTAP10-9P604113EBI-719941,EBI-10172052
KRTAP5-9P263713EBI-719941,EBI-3958099
LZTS2Q9BRK43EBI-719941,EBI-741037
MCM6Q145663EBI-719941,EBI-374900
MDFIQ997503EBI-719941,EBI-724076
MID2Q9UJV3-23EBI-719941,EBI-10172526
MIPOL1Q8TD103EBI-719941,EBI-2548751
MTUS2Q5JR593EBI-719941,EBI-742948
NECAB2H3BTW23EBI-719941,EBI-10172876
NINLQ9Y2I63EBI-719941,EBI-719716
NUTM1Q86Y263EBI-719941,EBI-10178410
PDE4DIPQ5VU433EBI-719941,EBI-1105124
PDE4DIPQ8TBR03EBI-719941,EBI-10240575
PHC2Q8IXK03EBI-719941,EBI-713786
PNMA2Q9UL423EBI-719941,EBI-302355
POC5Q8NA723EBI-719941,EBI-2561090
PPFIA1Q131363EBI-719941,EBI-745426
RINT1Q6NUQ13EBI-719941,EBI-726876
RUNDC3AQ59EK93EBI-719941,EBI-747225
SPERTQ8NA613EBI-719941,EBI-741724
SSX2IPQ9Y2D83EBI-719941,EBI-2212028
STX11O755583EBI-719941,EBI-714135
SYCE1Q8N0S23EBI-719941,EBI-6872807
TFIP11Q9UBB93EBI-719941,EBI-1105213
TMCC2Q7Z6C63EBI-719941,EBI-10177480
TNIP1Q150253EBI-719941,EBI-357849
TRAF1Q130773EBI-719941,EBI-359224
TRIM15Q9C0193EBI-719941,EBI-2342111
TRIM37O949723EBI-719941,EBI-741602
TRIM54Q9BYV23EBI-719941,EBI-2130429
ZBTB1Q9Y2K13EBI-719941,EBI-2682961
ZBTB14O438293EBI-719941,EBI-10176632
ZBTB43O432983EBI-719941,EBI-740718
ZBTB8AQ96BR93EBI-719941,EBI-742740

Protein-protein interaction databases

BioGridi123909. 66 interactions.
IntActiQ3B820. 61 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ3B820.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili93 – 12028Sequence AnalysisAdd
BLAST
Coiled coili296 – 32025Sequence AnalysisAdd
BLAST
Coiled coili522 – 55231Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi47 – 526Poly-Glu
Compositional biasi609 – 65850Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the FAM161 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG80167.
GeneTreeiENSGT00530000063901.
HOGENOMiHOG000049209.
HOVERGENiHBG107870.
InParanoidiQ3B820.
KOiK16772.
OMAiAEKHYSN.
PhylomeDBiQ3B820.
TreeFamiTF321199.

Family and domain databases

InterProiIPR019579. UPF0564.
[Graphical view]
PfamiPF10595. UPF0564. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3B820-1) [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

        10         20         30         40         50
MATSHRVAKL VASSLQTPVN PITGARVAQY EREDPLKALA AAEAILEDEE
60 70 80 90 100
EEKVAQPAGA SADLNTSFSG VDEHAPISYE DFVNFPDIHH SNEEYFKKVE
110 120 130 140 150
ELKAAHIETM AKLEKMYQDK LHLKEVQPVV IREDSLSDSS RSVSEKNSYH
160 170 180 190 200
PVSLMTSFSE PDLGQSSSLY VSSSEEELPN LEKEYPRKNR MMTYAKELIN
210 220 230 240 250
NMWTDFCVED YIRCKDTGFH AAEKRRKKRK EWVPTITVPE PFQMMIREQK
260 270 280 290 300
KKEESMKSKS DIEMVHKALK KQEEDPEYKK KFRANPVPAS VFLPLYHDLV
310 320 330 340 350
KQKEERRRSL KEKSKEALLA SQKPFKFIAR EEQKRAAREK QLRDFLKYKK
360 370 380 390 400
KTNRFKARPI PRSTYGSTTN DKLKEEELYR NLRTQLRAQE HLQNSSPLPC
410 420 430 440 450
RSACGCRNPR CPEQAVKLKC KHKVRCPTPD FEDLPERYQK HLSEHKSPKL
460 470 480 490 500
LTVCKPFDLH ASPHASIKRE KILADIEADE ENLKETRWPY LSPRRKSPVR
510 520 530 540 550
CAGVNPVPCN CNPPVPTVSS RGREQAVRKS EKERMREYQR ELEEREEKLK
560 570 580 590 600
KRPLLFERVA QKNARMAAEK HYSNTLKALG ISDEFVSKKG QSGKVLEYFN
610 620 630 640 650
NQETKSVTED KESFNEEEKI EERENGEENY FIDTNSQDSY KEKDEANEES
660
EEEKSVEESH
Length:660
Mass (Da):76,752
Last modified:April 8, 2008 - v2
Checksum:iE2C0D443C1A0DAA5
GO
Isoform 2 (identifier: Q3B820-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-109: Missing.

Note: No experimental confirmation available.
Show »
Length:551
Mass (Da):64,836
Checksum:iF31A08F7C2AB938E
GO
Isoform 3 (identifier: Q3B820-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     527-527: V → VRRSLEEKKMLEEERNRILTKQKQRMKELQKLLTTRAKAYDSHQSLAQISKSRVKCL

Show »
Length:716
Mass (Da):83,492
Checksum:iC2346158DFD127CD
GO

Sequence cautioni

The sequence BAG58969.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451E → G in BX648834 (PubMed:17974005).Curated
Sequence conflicti167 – 1671S → F in BAB14544 (PubMed:14702039).Curated
Sequence conflicti534 – 5341R → M in BAG58969 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071I → M.1 Publication
Corresponds to variant rs11125895 [ dbSNP | Ensembl ].
VAR_060180
Natural varianti236 – 2361I → V.
Corresponds to variant rs17513722 [ dbSNP | Ensembl ].
VAR_042630
Natural varianti273 – 2731E → K.
Corresponds to variant rs6733774 [ dbSNP | Ensembl ].
VAR_042631

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 109109Missing in isoform 2. 1 PublicationVSP_032935Add
BLAST
Alternative sequencei527 – 5271V → VRRSLEEKKMLEEERNRILT KQKQRMKELQKLLTTRAKAY DSHQSLAQISKSRVKCL in isoform 3. 1 PublicationVSP_039126

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX648834 mRNA. No translation available.
BX649029 mRNA. No translation available.
AC107081 Genomic DNA. No translation available.
AK023367 mRNA. Translation: BAB14544.1.
AK296255 mRNA. Translation: BAG58969.1. Different initiation.
BC107162 mRNA. No translation available.
BC107163 mRNA. No translation available.
CCDSiCCDS42687.2. [Q3B820-1]
CCDS56120.1. [Q3B820-3]
RefSeqiNP_001188472.1. NM_001201543.1. [Q3B820-3]
NP_115556.2. NM_032180.2. [Q3B820-1]
UniGeneiHs.440466.

Genome annotation databases

EnsembliENST00000404929; ENSP00000385158; ENSG00000170264. [Q3B820-3]
ENST00000405894; ENSP00000385893; ENSG00000170264.
GeneIDi84140.
KEGGihsa:84140.
UCSCiuc002sbm.4. human. [Q3B820-3]
uc002sbn.4. human. [Q3B820-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX648834 mRNA. No translation available.
BX649029 mRNA. No translation available.
AC107081 Genomic DNA. No translation available.
AK023367 mRNA. Translation: BAB14544.1.
AK296255 mRNA. Translation: BAG58969.1. Different initiation.
BC107162 mRNA. No translation available.
BC107163 mRNA. No translation available.
CCDSiCCDS42687.2. [Q3B820-1]
CCDS56120.1. [Q3B820-3]
RefSeqiNP_001188472.1. NM_001201543.1. [Q3B820-3]
NP_115556.2. NM_032180.2. [Q3B820-1]
UniGeneiHs.440466.

3D structure databases

ProteinModelPortaliQ3B820.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123909. 66 interactions.
IntActiQ3B820. 61 interactions.

PTM databases

PhosphoSiteiQ3B820.

Polymorphism and mutation databases

BioMutaiFAM161A.
DMDMi182705173.

Proteomic databases

MaxQBiQ3B820.
PaxDbiQ3B820.
PRIDEiQ3B820.

Protocols and materials databases

DNASUi84140.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000404929; ENSP00000385158; ENSG00000170264. [Q3B820-3]
ENST00000405894; ENSP00000385893; ENSG00000170264.
GeneIDi84140.
KEGGihsa:84140.
UCSCiuc002sbm.4. human. [Q3B820-3]
uc002sbn.4. human. [Q3B820-1]

Organism-specific databases

CTDi84140.
GeneCardsiGC02M062051.
GeneReviewsiFAM161A.
H-InvDBHIX0002084.
HGNCiHGNC:25808. FAM161A.
HPAiHPA032119.
MIMi606068. phenotype.
613596. gene.
neXtProtiNX_Q3B820.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA162386876.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG80167.
GeneTreeiENSGT00530000063901.
HOGENOMiHOG000049209.
HOVERGENiHBG107870.
InParanoidiQ3B820.
KOiK16772.
OMAiAEKHYSN.
PhylomeDBiQ3B820.
TreeFamiTF321199.

Miscellaneous databases

GenomeRNAii84140.
NextBioi73449.
PROiQ3B820.
SOURCEiSearch...

Gene expression databases

BgeeiQ3B820.
CleanExiHS_FAM161A.
ExpressionAtlasiQ3B820. baseline and differential.
GenevisibleiQ3B820. HS.

Family and domain databases

InterProiIPR019579. UPF0564.
[Graphical view]
PfamiPF10595. UPF0564. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT MET-107.
    Tissue: Colon endothelium and Retina.
  2. "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].
  3. "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 1-545 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-660 (ISOFORMS 1/2).
    Tissue: Ovary and Thalamus.
  4. "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] OF 43-660 (ISOFORM 1).
  5. Cited for: INVOLVEMENT IN RP28, TISSUE SPECIFICITY.
  6. "Homozygosity mapping reveals null mutations in FAM161A as a cause of autosomal-recessive retinitis pigmentosa."
    Bandah-Rozenfeld D., Mizrahi-Meissonnier L., Farhy C., Obolensky A., Chowers I., Pe'er J., Merin S., Ben-Yosef T., Ashery-Padan R., Banin E., Sharon D.
    Am. J. Hum. Genet. 87:382-391(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RP28, TISSUE SPECIFICITY.
  7. "FAM161A, associated with retinitis pigmentosa, is a component of the cilia-basal body complex and interacts with proteins involved in ciliopathies."
    Di Gioia S.A., Letteboer S.J., Kostic C., Bandah-Rozenfeld D., Hetterschijt L., Sharon D., Arsenijevic Y., Roepman R., Rivolta C.
    Hum. Mol. Genet. 21:5174-5184(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LCA5; CEP290 AND SDCCAG8.
  8. "The retinitis pigmentosa 28 protein FAM161A is a novel ciliary protein involved in intermolecular protein interaction and microtubule association."
    Zach F., Grassmann F., Langmann T., Sorusch N., Wolfrum U., Stohr H.
    Hum. Mol. Genet. 21:4573-4586(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICROTUBULES AND FAM161B.
  9. Cited for: INTERACTION WITH POC1B.

Entry informationi

Entry nameiF161A_HUMAN
AccessioniPrimary (citable) accession number: Q3B820
Secondary accession number(s): B4DJV7, Q9H8R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 8, 2008
Last modified: July 22, 2015
This is version 81 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 2
    Human chromosome 2: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.