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P98198 (AT8B2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipid-transporting ATPase ID

EC=3.6.3.1
Alternative name(s):
ATPase class I type 8B member 2
P4-ATPase flippase complex alpha subunit ATP8B2
Gene names
Name:ATP8B2
Synonyms:ATPID, KIAA1137
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1209 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules Probable.

Catalytic activity

ATP + H2O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).

Subunit structure

Component of a P4-ATPase flippase complex which consists of a catalytic alpha subunit and an accessory beta subunit Probable. The probable flippase ATP8B2:TMEM30A complex can form an intermediate phosphoenzyme in vitro. The interaction with TMEM30B is reported conflictingly.

Subcellular location

Membrane Potential; Multi-pass membrane protein. Cell membrane. Note: TMEM30A, but not TMEM30B, is required for its export from ER to the plasma membrane. Ref.8 Ref.9

Tissue specificity

Isoform 3 is ubiquitous, with highest expression in aorta, cerebellum and uterus. Ref.1

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily. [View classification]

Sequence caution

The sequence AAH30288.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB70822.1 differs from that shown. Reason: Frameshift at position 364.

The sequence BAG65556.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P98198-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: P98198-2)

The sequence of this isoform differs from the canonical sequence as follows:
     434-461: GDVFDVLGHKAELGERPEPVDFSFNPLA → VGSEGPRRKGPSWPGTVAHAYSHSTLGG
     462-1209: Missing.
Isoform 3 (identifier: P98198-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MTVPKEMPEKWARAQAPPSWSRKKPSWGT → MDTLRAVPLFSISGLFSFPYRVSHGIAGILLGEMAVCAKKRPP
Isoform 4 (identifier: P98198-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: MTVPKEMPEKWARAQAPPSWSRKKPSWGT → MAVCAKKRPP
     364-406: SVEVIRLGHS...TLNEELGQVE → RYVPSLTWGL...KSSSSCTVNI
     407-1209: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12091209Phospholipid-transporting ATPase ID
PRO_0000046365

Regions

Topological domain1 – 6464Cytoplasmic Potential
Transmembrane65 – 8622Helical; Potential
Topological domain87 – 926Exoplasmic loop Potential
Transmembrane93 – 11220Helical; Potential
Topological domain113 – 295183Cytoplasmic Potential
Transmembrane296 – 31722Helical; Potential
Topological domain318 – 34629Exoplasmic loop Potential
Transmembrane347 – 36822Helical; Potential
Topological domain369 – 889521Cytoplasmic Potential
Transmembrane890 – 91021Helical; Potential
Topological domain911 – 92212Exoplasmic loop Potential
Transmembrane923 – 94220Helical; Potential
Topological domain943 – 97230Cytoplasmic Potential
Transmembrane973 – 99422Helical; Potential
Topological domain995 – 100814Exoplasmic loop Potential
Transmembrane1009 – 103123Helical; Potential
Topological domain1032 – 10376Cytoplasmic Potential
Transmembrane1038 – 105821Helical; Potential
Topological domain1059 – 107820Exoplasmic loop Potential
Transmembrane1079 – 110325Helical; Potential
Topological domain1104 – 1209106Cytoplasmic Potential

Sites

Active site41114-aspartylphosphate intermediate By similarity
Metal binding8331Magnesium By similarity
Metal binding8371Magnesium By similarity

Natural variations

Alternative sequence1 – 2929MTVPK…PSWGT → MDTLRAVPLFSISGLFSFPY RVSHGIAGILLGEMAVCAKK RPP in isoform 3.
VSP_037147
Alternative sequence1 – 2929MTVPK…PSWGT → MAVCAKKRPP in isoform 4.
VSP_037148
Alternative sequence364 – 40643SVEVI…LGQVE → RYVPSLTWGLSRESGGPIEL FFSMKMKSLRSNEKSSSSCT VNI in isoform 4.
VSP_037149
Alternative sequence407 – 1209803Missing in isoform 4.
VSP_037150
Alternative sequence434 – 46128GDVFD…FNPLA → VGSEGPRRKGPSWPGTVAHA YSHSTLGG in isoform 2.
VSP_007302
Alternative sequence462 – 1209748Missing in isoform 2.
VSP_007303

Experimental info

Sequence conflict8341G → E in BAA86451. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: D905A97E9D9724BD

FASTA1,209137,440
        10         20         30         40         50         60 
MTVPKEMPEK WARAQAPPSW SRKKPSWGTE EERRARANDR EYNEKFQYAS NCIKTSKYNI 

        70         80         90        100        110        120 
LTFLPVNLFE QFQEVANTYF LFLLILQLIP QISSLSWFTT IVPLVLVLTI TAVKDATDDY 

       130        140        150        160        170        180 
FRHKSDNQVN NRQSQVLING ILQQEQWMNV CVGDIIKLEN NQFVAADLLL LSSSEPHGLC 

       190        200        210        220        230        240 
YIETAELDGE TNMKVRQAIP VTSELGDISK LAKFDGEVIC EPPNNKLDKF SGTLYWKENK 

       250        260        270        280        290        300 
FPLSNQNMLL RGCVLRNTEW CFGLVIFAGP DTKLMQNSGR TKFKRTSIDR LMNTLVLWIF 

       310        320        330        340        350        360 
GFLVCMGVIL AIGNAIWEHE VGMRFQVYLP WDEAVDSAFF SGFLSFWSYI IILNTVVPIS 

       370        380        390        400        410        420 
LYVSVEVIRL GHSYFINWDK KMFCMKKRTP AEARTTTLNE ELGQVEYIFS DKTGTLTQNI 

       430        440        450        460        470        480 
MVFNKCSING HSYGDVFDVL GHKAELGERP EPVDFSFNPL ADKKFLFWDP SLLEAVKIGD 

       490        500        510        520        530        540 
PHTHEFFRLL SLCHTVMSEE KNEGELYYKA QSPDEGALVT AARNFGFVFR SRTPKTITVH 

       550        560        570        580        590        600 
EMGTAITYQL LAILDFNNIR KRMSVIVRNP EGKIRLYCKG ADTILLDRLH HSTQELLNTT 

       610        620        630        640        650        660 
MDHLNEYAGE GLRTLVLAYK DLDEEYYEEW AERRLQASLA QDSREDRLAS IYEEVENNMM 

       670        680        690        700        710        720 
LLGATAIEDK LQQGVPETIA LLTLANIKIW VLTGDKQETA VNIGYSCKML TDDMTEVFIV 

       730        740        750        760        770        780 
TGHTVLEVRE ELRKAREKMM DSSRSVGNGF TYQDKLSSSK LTSVLEAVAG EYALVINGHS 

       790        800        810        820        830        840 
LAHALEADME LEFLETACAC KAVICCRVTP LQKAQVVELV KKYKKAVTLA IGDGANDVSM 

       850        860        870        880        890        900 
IKTAHIGVGI SGQEGIQAVL ASDYSFSQFK FLQRLLLVHG RWSYLRMCKF LCYFFYKNFA 

       910        920        930        940        950        960 
FTMVHFWFGF FCGFSAQTVY DQYFITLYNI VYTSLPVLAM GVFDQDVPEQ RSMEYPKLYE 

       970        980        990       1000       1010       1020 
PGQLNLLFNK REFFICIAQG IYTSVLMFFI PYGVFADATR DDGTQLADYQ SFAVTVATSL 

      1030       1040       1050       1060       1070       1080 
VIVVSVQIGL DTGYWTAINH FFIWGSLAVY FAILFAMHSN GLFDMFPNQF RFVGNAQNTL 

      1090       1100       1110       1120       1130       1140 
AQPTVWLTIV LTTVVCIMPV VAFRFLRLNL KPDLSDTVRY TQLVRKKQKA QHRCMRRVGR 

      1150       1160       1170       1180       1190       1200 
TGSRRSGYAF SHQEGFGELI MSGKNMRLSS LALSSFTTRS SSSWIESLRR KKSDSASSPS 


GGADKPLKG 

« Hide

Isoform 2 [UniParc].

Checksum: 15CAABEAAE6862DC
Show »

FASTA46152,624
Isoform 3 [UniParc].

Checksum: 61AF805A0511A143
Show »

FASTA1,223138,719
Isoform 4 [UniParc].

Checksum: B4C17CA615F4F952
Show »

FASTA38744,213

References

« Hide 'large scale' references
[1]"FIC1, a P-type ATPase linked to cholestatic liver disease, has homologues (ATP8B2 and ATP8B3) expressed throughout the body."
Harris M.J., Arias I.M.
Biochim. Biophys. Acta 1633:127-131(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORM 4), TISSUE SPECIFICITY.
Tissue: Colon.
[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. expand/collapse author list , 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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 671-1209 (ISOFORMS 1/3).
Tissue: Cerebellum and Uterus.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 447-1209 (ISOFORMS 1/3).
Tissue: Lung, Mammary gland and Muscle.
[6]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 277-1209 (ISOFORMS 1/3).
Tissue: Brain.
[7]"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] OF 1112-1209 (ISOFORM 1).
Tissue: Testis.
[8]"Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases."
van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A., Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.
J. Biol. Chem. 285:40088-40096(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM30A, SUBCELLULAR LOCATION.
[9]"CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery."
Bryde S., Hennrich H., Verhulst P.M., Devaux P.F., Lenoir G., Holthuis J.C.
J. Biol. Chem. 285:40562-40572(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TMEM30A AND TMEM30B, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY302537 mRNA. Translation: AAQ19027.1.
AK054886 mRNA. Translation: BAB70822.1. Frameshift.
AK304806 mRNA. Translation: BAG65556.1. Different initiation.
AL162591 Genomic DNA. Translation: CAH72858.1.
CH471121 Genomic DNA. Translation: EAW53205.1.
BC007837 mRNA. Translation: AAH07837.2.
BC030288 mRNA. Translation: AAH30288.1. Different initiation.
BC069264 mRNA. Translation: AAH69264.1.
AB032963 mRNA. Translation: BAA86451.1.
AL137537 mRNA. Translation: CAB70799.1.
CCDSCCDS1066.1. [P98198-3]
CCDS41405.1. [P98198-4]
PIRT46381.
RefSeqNP_001005855.1. NM_001005855.1. [P98198-4]
NP_065185.1. NM_020452.3. [P98198-3]
XP_005245412.1. XM_005245355.1. [P98198-1]
UniGeneHs.435700.

3D structure databases

ProteinModelPortalP98198.
SMRP98198. Positions 790-956.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121445. 1 interaction.
STRING9606.ENSP00000357475.

PTM databases

PhosphoSiteP98198.

Polymorphism databases

DMDM30316371.

Proteomic databases

MaxQBP98198.
PaxDbP98198.
PRIDEP98198.

Protocols and materials databases

DNASU57198.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341822; ENSP00000340448; ENSG00000143515. [P98198-2]
ENST00000368487; ENSP00000357472; ENSG00000143515. [P98198-4]
ENST00000368489; ENSP00000357475; ENSG00000143515. [P98198-3]
GeneID57198.
KEGGhsa:57198.
UCSCuc001few.3. human. [P98198-4]
uc001fex.3. human. [P98198-3]
uc001fey.1. human. [P98198-2]

Organism-specific databases

CTD57198.
GeneCardsGC01P154298.
HGNCHGNC:13534. ATP8B2.
HPAHPA046680.
MIM605867. gene.
neXtProtNX_P98198.
PharmGKBPA25167.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0474.
HOGENOMHOG000202528.
HOVERGENHBG050601.
KOK01530.
OMAWKESKFP.
OrthoDBEOG7RRF68.
PhylomeDBP98198.
TreeFamTF300654.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP98198.
BgeeP98198.
CleanExHS_ATP8B2.
GenevestigatorP98198.

Family and domain databases

Gene3D2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR006539. ATPase_P-typ_Plipid-transp.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR023214. HAD-like_dom.
[Graphical view]
PANTHERPTHR24092. PTHR24092. 1 hit.
PfamPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF56784. SSF56784. 3 hits.
SSF81660. SSF81660. 1 hit.
TIGRFAMsTIGR01652. ATPase-Plipid. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi57198.
NextBio63288.
PROP98198.
SOURCESearch...

Entry information

Entry nameAT8B2_HUMAN
AccessionPrimary (citable) accession number: P98198
Secondary accession number(s): B4E3P4 expand/collapse secondary AC list , Q6NT69, Q7Z486, Q96I43, Q96NQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 30, 2003
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM